{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1360572092607653504.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1002/cmdc.202000940"}},{"identifier":{"@type":"URI","@value":"https://onlinelibrary.wiley.com/doi/pdf/10.1002/cmdc.202000940"}},{"identifier":{"@type":"URI","@value":"https://onlinelibrary.wiley.com/doi/full-xml/10.1002/cmdc.202000940"}},{"identifier":{"@type":"URI","@value":"https://chemistry-europe.onlinelibrary.wiley.com/doi/pdf/10.1002/cmdc.202000940"}},{"identifier":{"@type":"PMID","@value":"33565721"}}],"resourceType":"学術雑誌論文(journal article)","dc:title":[{"@value":"Helical Antimicrobial Peptide Foldamers Containing Non‐proteinogenic Amino Acids"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:title>Abstract</jats:title><jats:p>Antimicrobial peptides (AMPs) are potential novel therapeutic drugs against microbial infections. Most AMPs function by disrupting microbial membranes because of their amphipathic properties and ordered secondary structures. In this minireview, we describe recent efforts to develop helical AMP foldamers containing non‐proteinogenic amino acids, such as α,α‐disubstituted α‐amino acids, β‐amino acids, γ‐amino acids, side‐chain stapling and N‐alkyl glycines.</jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1420285329318075008","@type":"Researcher","personIdentifier":[{"@type":"KAKEN_RESEARCHERS","@value":"80881424"},{"@type":"NRID","@value":"1000080881424"},{"@type":"NRID","@value":"9000410315671"},{"@type":"NRID","@value":"9000412546596"},{"@type":"NRID","@value":"9000409788079"},{"@type":"NRID","@value":"9000408665227"},{"@type":"NRID","@value":"9000413571350"},{"@type":"NRID","@value":"9000408634277"},{"@type":"RESEARCHMAP","@value":"https://researchmap.jp/HYokoo"}],"foaf:name":[{"@value":"Hidetomo Yokoo"}],"jpcoar:affiliationName":[{"@value":"Division of Organic Chemistry National Institute of Health Sciences  3-25-26, Tonomachi, Kawasaki Kanagawa 210-9501 Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1380572092607653376","@type":"Researcher","foaf:name":[{"@value":"Motoharu Hirano"}],"jpcoar:affiliationName":[{"@value":"Division of Organic Chemistry National Institute of Health Sciences  3-25-26, Tonomachi, Kawasaki Kanagawa 210-9501 Japan"},{"@value":"Graduate School of Medical Life Science Yokohama City University  1-7-29, Yokohama Kanagawa 230-0045 Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1420564276185438208","@type":"Researcher","personIdentifier":[{"@type":"KAKEN_RESEARCHERS","@value":"40709820"},{"@type":"NRID","@value":"1000040709820"},{"@type":"NRID","@value":"9000006405016"},{"@type":"NRID","@value":"9000408665231"},{"@type":"NRID","@value":"9000283259763"},{"@type":"NRID","@value":"9000406366682"},{"@type":"NRID","@value":"9000397866334"},{"@type":"NRID","@value":"9000273034139"},{"@type":"NRID","@value":"9000389547133"},{"@type":"NRID","@value":"9000283148348"},{"@type":"NRID","@value":"9000387906408"},{"@type":"NRID","@value":"9000304974315"},{"@type":"NRID","@value":"9000303990499"},{"@type":"NRID","@value":"9000408634281"},{"@type":"RESEARCHMAP","@value":"https://researchmap.jp/t-misawa"}],"foaf:name":[{"@value":"Takashi Misawa"}],"jpcoar:affiliationName":[{"@value":"Division of Organic Chemistry National Institute of Health Sciences  3-25-26, Tonomachi, Kawasaki Kanagawa 210-9501 Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1380572092607653248","@type":"Researcher","foaf:name":[{"@value":"Yosuke Demizu"}],"jpcoar:affiliationName":[{"@value":"Division of Organic Chemistry National Institute of Health Sciences  3-25-26, Tonomachi, Kawasaki Kanagawa 210-9501 Japan"},{"@value":"Graduate School of Medical Life Science Yokohama City University  1-7-29, Yokohama Kanagawa 230-0045 Japan"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"18607179"},{"@type":"EISSN","@value":"18607187"}],"prism:publicationName":[{"@value":"ChemMedChem"}],"dc:publisher":[{"@value":"Wiley"}],"prism:publicationDate":"2021-02-10","prism:volume":"16","prism:number":"8","prism:startingPage":"1226","prism:endingPage":"1233"},"reviewed":"false","dc:rights":["http://onlinelibrary.wiley.com/termsAndConditions#vor"],"url":[{"@id":"https://onlinelibrary.wiley.com/doi/pdf/10.1002/cmdc.202000940"},{"@id":"https://onlinelibrary.wiley.com/doi/full-xml/10.1002/cmdc.202000940"},{"@id":"https://chemistry-europe.onlinelibrary.wiley.com/doi/pdf/10.1002/cmdc.202000940"}],"createdAt":"2021-02-10","modifiedAt":"2025-10-12","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=Protein%20Conformation,%20alpha-Helical","dc:title":"Protein Conformation, alpha-Helical"},{"@id":"https://cir.nii.ac.jp/all?q=Bacteria","dc:title":"Bacteria"},{"@id":"https://cir.nii.ac.jp/all?q=Amino%20Acid%20Sequence","dc:title":"Amino Acid Sequence"},{"@id":"https://cir.nii.ac.jp/all?q=Amino%20Acids","dc:title":"Amino Acids"},{"@id":"https://cir.nii.ac.jp/all?q=Antimicrobial%20Peptides","dc:title":"Antimicrobial Peptides"},{"@id":"https://cir.nii.ac.jp/all?q=Anti-Bacterial%20Agents","dc:title":"Anti-Bacterial Agents"}],"project":[{"@id":"https://cir.nii.ac.jp/crid/1040000782004072064","@type":"Project","projectIdentifier":[{"@type":"KAKEN","@value":"18K14880"},{"@type":"JGN","@value":"JP18K14880"},{"@type":"URI","@value":"https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-18K14880/"}],"notation":[{"@language":"ja","@value":"生体応用を志向した細胞膜高透過性ヘリカルペプチドの開発"},{"@language":"en","@value":"Development of cell penetrating peptides based on helical promoter for biomedical application"}]},{"@id":"https://cir.nii.ac.jp/crid/1040282256944313472","@type":"Project","projectIdentifier":[{"@type":"KAKEN","@value":"17K08385"},{"@type":"JGN","@value":"JP17K08385"},{"@type":"URI","@value":"https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-17K08385/"}],"notation":[{"@language":"ja","@value":"二次構造制御を基軸としたペプチド創薬研究"},{"@language":"en","@value":"Peptide foldamers in drug discovery"}]},{"@id":"https://cir.nii.ac.jp/crid/1040282256971659776","@type":"Project","projectIdentifier":[{"@type":"KAKEN","@value":"18H05502"},{"@type":"JGN","@value":"JP18H05502"},{"@type":"URI","@value":"https://kaken.nii.ac.jp/grant/KAKENHI-PLANNED-18H05502/"}],"notation":[{"@language":"ja","@value":"ケミカルプロテインノックダウン技術の開発と細胞制御"},{"@language":"en","@value":"Chemical protein knockdown technology and cell regulation"}]},{"@id":"https://cir.nii.ac.jp/crid/1040285696983605376","@type":"Project","projectIdentifier":[{"@type":"KAKEN","@value":"20K22711"},{"@type":"JGN","@value":"JP20K22711"},{"@type":"URI","@value":"https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-20K22711/"}],"notation":[{"@language":"ja","@value":"ユビキチン化により機能調節を受けるタンパク質を標的とした分解誘導剤の開発"},{"@language":"en","@value":"Development of degrader targeting proteins regulated by ubiquitination"}]},{"@id":"https://cir.nii.ac.jp/crid/1040569382214934528","@type":"Project","projectIdentifier":[{"@type":"KAKEN","@value":"21K05320"},{"@type":"JGN","@value":"JP21K05320"},{"@type":"URI","@value":"https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-21K05320/"}],"notation":[{"@language":"ja","@value":"革新的中分子医薬品創出を目指したペプチドフォルダマー研究"},{"@language":"en","@value":"Peptide Foldamers for Innovative Drug Development"}]}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1050292561213784576","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Helical Foldamers and Stapled Peptides as New Modalities in Drug Discovery: Modulators of Protein-Protein Interactions"}]},{"@id":"https://cir.nii.ac.jp/crid/1360002215834130816","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Development of helix-stabilized antimicrobial peptides composed of lysine and hydrophobic α,α-disubstituted α-amino acid residues"}]},{"@id":"https://cir.nii.ac.jp/crid/1360002216872912256","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Conformational studies on peptides containing α,α-disubstituted α-amino acids: chiral cyclic α,α-disubstituted α-amino acid as an α-helical inducer"}]},{"@id":"https://cir.nii.ac.jp/crid/1360004230102541952","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"α‐Helical Structures of Oligopeptides with an Alternating l‐Leu‐Aib Segment"}]},{"@id":"https://cir.nii.ac.jp/crid/1360004233120102784","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Rational Design and Synthesis of Post-Functionalizable Peptide Foldamers as Helical Templates"}]},{"@id":"https://cir.nii.ac.jp/crid/1360011144320021888","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Antimicrobial host defence peptides: functions and clinical potential"}]},{"@id":"https://cir.nii.ac.jp/crid/1360011144553724160","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"De Novo Design of Antibacterial β-Peptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1360011144637654784","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Residue-based control of helix shape in β-peptide oligomers"}]},{"@id":"https://cir.nii.ac.jp/crid/1360011144672934784","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Design of stapled antimicrobial peptides that are stable, nontoxic and kill antibiotic-resistant bacteria in mice"}]},{"@id":"https://cir.nii.ac.jp/crid/1360011145527315968","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Macromolecular-clustered facial amphiphilic antimicrobials"}]},{"@id":"https://cir.nii.ac.jp/crid/1360011145549592192","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Synthetic foldamers"}]},{"@id":"https://cir.nii.ac.jp/crid/1360011146157378176","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Alamethicin, a transmembrane channel"}]},{"@id":"https://cir.nii.ac.jp/crid/1360011146553659776","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"1,2,3‐Triazolium‐Based Cationic Amphipathic Peptoid Oligomers Mimicking Antimicrobial Helical Peptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1360017280632783872","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Helix-forming aliphatic homo-δ-peptide foldamers based on the conformational restriction effects of cyclopropane"}]},{"@id":"https://cir.nii.ac.jp/crid/1360025429414068224","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Stabilization of optically inactive α-helices of peptidic foldamers through sequence control and <i>i</i>, <i>i</i> + 4 stapling"}]},{"@id":"https://cir.nii.ac.jp/crid/1360292618490035968","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"A polyamine dendritic polymer–copper complex: a reusable catalyst for the additive-free amination of aryl bromides, and iodides"}]},{"@id":"https://cir.nii.ac.jp/crid/1360292618633504896","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"A Field Guide to Foldamers"}]},{"@id":"https://cir.nii.ac.jp/crid/1360292619155713536","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Hydrophobicity and Helicity Regulate the Antifungal Activity of 14-Helical β-Peptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1360298345425832576","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"The Biological Stability of β-Peptides: No Interactions between α- and β-Peptidic Structures?"}]},{"@id":"https://cir.nii.ac.jp/crid/1360298755614593280","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Structure–Activity Relationship Studies of Substitutions of Cationic Amino Acid Residues on Antimicrobial Peptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1360298757399613952","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Development of a penetratin-conjugated stapled peptide that inhibits Wnt/β-catenin signaling"}]},{"@id":"https://cir.nii.ac.jp/crid/1360567183084489472","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Preorganized Cyclic α,α-Disubstituted α-Amino Acids Bearing Functionalized Side Chains That Act as Peptide-Helix Inducers"}]},{"@id":"https://cir.nii.ac.jp/crid/1360572092607700608","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"De Novo Design of Cell‐Penetrating Foldamers"}]},{"@id":"https://cir.nii.ac.jp/crid/1360574094186011648","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Designing antimicrobial peptides: form follows function"}]},{"@id":"https://cir.nii.ac.jp/crid/1360574094765492224","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"A Novel Trp-rich Model Antimicrobial Peptoid with Increased Protease Stability"}]},{"@id":"https://cir.nii.ac.jp/crid/1360574095381230592","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Therapeutic Potential of Foldamers: From Chemical Biology Tools To Drug Candidates?"}]},{"@id":"https://cir.nii.ac.jp/crid/1360574095513175040","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Control of cell selectivity of antimicrobial peptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1360574095627344512","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Effects of Aib residues insertion on the structural–functional properties of the frog skin-derived peptide esculentin-1a(1–21)NH2"}]},{"@id":"https://cir.nii.ac.jp/crid/1360574095693783552","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Synthesis and Characterization of <i>trans</i>-2-Aminocyclohexanecarboxylic Acid Oligomers:  An Unnatural Helical Secondary Structure and Implications for β-Peptide Tertiary Structure"}]},{"@id":"https://cir.nii.ac.jp/crid/1360574095742839808","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"An overview of peptide and peptoid foldamers in medicinal chemistry"}]},{"@id":"https://cir.nii.ac.jp/crid/1360574095872369152","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Helices and other secondary structures of β‐ and γ‐peptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1360574095996189056","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Mimicry of Host-Defense Peptides by Unnatural Oligomers:  Antimicrobial β-Peptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1360574096006670720","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Design and synthesis of cationic Aib‐containing antimicrobial peptides: conformational and biological studies"}]},{"@id":"https://cir.nii.ac.jp/crid/1360588381050852224","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Selection of MDM2-binding peptides in <i>Escherichia coli</i> using an engineered split intein and aminoglycoside phosphotransferase"}]},{"@id":"https://cir.nii.ac.jp/crid/1360849943436321024","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Development of 2-aminoisobutyric acid (Aib)-rich cell-penetrating foldamers for efficient siRNA delivery"}]},{"@id":"https://cir.nii.ac.jp/crid/1360855568690693632","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Handedness preference and switching of peptide helices. Part II: Helices based on noncoded<i>α</i>‐amino acids"}]},{"@id":"https://cir.nii.ac.jp/crid/1360855568773761536","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Modifications on amphiphilicity and cationicity of unnatural amino acid containing peptides for the improvement of antimicrobial activity against pathogenic bacteria"}]},{"@id":"https://cir.nii.ac.jp/crid/1360855569438937472","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"β-Peptides: a surprise at every turn"}]},{"@id":"https://cir.nii.ac.jp/crid/1360855570297839104","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"The twists and turns of β‐peptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1360865814729689728","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Sculpting Secondary Structure of a Cyclic Peptide: Conformational Analysis of a Cyclic Hexapeptide Containing a Combination of <scp>l</scp>-Leu, <scp>d</scp>-Leu, and Aib Residues"}]},{"@id":"https://cir.nii.ac.jp/crid/1361137043880288640","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Antibacterial mechanisms of GN‐2 derived peptides and peptoids against <i>Escherichia coli</i>"}]},{"@id":"https://cir.nii.ac.jp/crid/1361137045811947776","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Novel Stapling by Lysine Tethering Provides Stable and Low Hemolytic Cationic Antimicrobial Peptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1361137045841094528","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Dimeric γ-AApeptides With Potent and Selective Antibacterial Activity"}]},{"@id":"https://cir.nii.ac.jp/crid/1361137045846024576","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Stapled Peptides Inhibitors: A New Window for Target Drug Discovery"}]},{"@id":"https://cir.nii.ac.jp/crid/1361137046000327168","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Magainin 2 Induces Bacterial Cell Death Showing Apoptotic Properties"}]},{"@id":"https://cir.nii.ac.jp/crid/1361418518390474624","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Synergy with Rifampin and Kanamycin Enhances Potency, Kill Kinetics, and Selectivity of<i>De</i><i>Novo</i>-Designed Antimicrobial Peptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1361418519301027584","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Helical Antimicrobial Sulfono-γ-AApeptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1361418519506765312","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Sensitivity of polypeptide conformation to geometry. Theoretical conformational analysis of oligomers of .alpha.-aminoisobutyric acid"}]},{"@id":"https://cir.nii.ac.jp/crid/1361418520108541440","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Inhibition of Bacterial Gene Transcription with an RpoN-Based Stapled Peptide"}]},{"@id":"https://cir.nii.ac.jp/crid/1361418520260972288","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Antimicrobial Activity of α-Peptide/β-Peptoid Lysine-Based Peptidomimetics Against Colistin-Resistant Pseudomonas aeruginosa Isolated From Cystic Fibrosis Patients"}]},{"@id":"https://cir.nii.ac.jp/crid/1361418520439778176","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Synthesis and Screening of Stereochemically Diverse Combinatorial Libraries of Peptide Tertiary Amides"}]},{"@id":"https://cir.nii.ac.jp/crid/1361418520716624128","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Intramolecular cyclization of the antimicrobial peptide Polybia‐MPI with triazole stapling: influence on stability and bioactivity"}]},{"@id":"https://cir.nii.ac.jp/crid/1361694364501244288","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Development of Amphipathic Antimicrobial Peptide Foldamers Based on Magainin 2 Sequence"}]},{"@id":"https://cir.nii.ac.jp/crid/1361699993760555136","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Foldamers as versatile frameworks for the design and evolution of function"}]},{"@id":"https://cir.nii.ac.jp/crid/1361699994538537472","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Constrained cell penetrating peptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1361699996498787968","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Membrane Active Antimicrobial Peptides: Translating Mechanistic Insights to Design"}]},{"@id":"https://cir.nii.ac.jp/crid/1361975842930254848","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"A Peptoid with Extended Shape in Water"}]},{"@id":"https://cir.nii.ac.jp/crid/1361981468764239104","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Conformational photoswitching of a synthetic peptide foldamer bound within a phospholipid bilayer"}]},{"@id":"https://cir.nii.ac.jp/crid/1361981469552618496","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Design of Folded Peptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1361981470107728384","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Structure−Activity Studies of 14-Helical Antimicrobial β-Peptides:  Probing the Relationship between Conformational Stability and Antimicrobial Potency"}]},{"@id":"https://cir.nii.ac.jp/crid/1361981471130155904","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Identification of γ-AApeptides with potent and broad-spectrum antimicrobial activity"}]},{"@id":"https://cir.nii.ac.jp/crid/1362262944991931520","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Lipidated Cyclic γ-AApeptides Display Both Antimicrobial and Anti-inflammatory Activity"}]},{"@id":"https://cir.nii.ac.jp/crid/1362262945068610816","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Design and synthesis of unprecedented cyclic γ-AApeptides for antimicrobial development"}]},{"@id":"https://cir.nii.ac.jp/crid/1362262945376982400","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Local and Tunable n→π* Interactions Regulate Amide Isomerism in the Peptoid Backbone"}]},{"@id":"https://cir.nii.ac.jp/crid/1362262945633385728","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Peptide/Peptoid Hybrid Oligomers: The Influence of Hydrophobicity and Relative Side-Chain Length on Antibacterial Activity and Cell Selectivity"}]},{"@id":"https://cir.nii.ac.jp/crid/1362262946303349760","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera"}]},{"@id":"https://cir.nii.ac.jp/crid/1362262946389239936","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"A voltage-gated ion channel model inferred from the crystal structure of alamethicin at 1.5-Å resolution"}]},{"@id":"https://cir.nii.ac.jp/crid/1362544419074691072","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Controls exerted by the Aib residue: Helix formation and helix reversal This article is a US Government work and, as such, is in the public domain in the United States of America."}]},{"@id":"https://cir.nii.ac.jp/crid/1362544421038188672","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Antimicrobial lipopeptaibol trichogin GA IV: role of the three Aib residues on conformation and bioactivity"}]},{"@id":"https://cir.nii.ac.jp/crid/1362544421350626560","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Control of peptide conformation by the Thorpe-Ingold effect (C?-tetrasubstitution)"}]},{"@id":"https://cir.nii.ac.jp/crid/1362825893493885056","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Incorporation of β-Amino Acids Enhances the Antifungal Activity and Selectivity of the Helical Antimicrobial Peptide Aurein 1.2"}]},{"@id":"https://cir.nii.ac.jp/crid/1362825894284707840","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Switchable foldamer ion channels with antibacterial activity"}]},{"@id":"https://cir.nii.ac.jp/crid/1362825896091401984","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor."}]},{"@id":"https://cir.nii.ac.jp/crid/1362825896171771776","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Peptoids that mimic the structure, function, and mechanism of helical antimicrobial peptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1363107369146778496","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Effect of side chain hydrophobicity and cationic charge on antimicrobial activity and cytotoxicity of helical peptoids"}]},{"@id":"https://cir.nii.ac.jp/crid/1363107369756188800","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Potent Antimicrobial Activity of Lipidated Short α,γ‐Hybrid Peptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1363107369812946560","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Action Potentials induced in Biomolecular Lipid Membranes"}]},{"@id":"https://cir.nii.ac.jp/crid/1363107370321302016","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Helical Peptoid Mimics of Magainin-2 Amide"}]},{"@id":"https://cir.nii.ac.jp/crid/1363388844129846656","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Enantiomeric glycosylated cationic block co-beta-peptides eradicate Staphylococcus aureus biofilms and antibiotic-tolerant persisters"}]},{"@id":"https://cir.nii.ac.jp/crid/1363388845248535552","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Antimicrobial α,α-Dialkylated Amino Acid Rich Peptides with <i>in-Vivo </i>Activity against an Intracellular Pathogen"}]},{"@id":"https://cir.nii.ac.jp/crid/1363388845258473216","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Antimicrobial properties of peptides from <i>Xenopus</i> granular gland secretions"}]},{"@id":"https://cir.nii.ac.jp/crid/1363388845882910848","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Synthesis of azobenzene-tethered DNA for reversible photo-regulation of DNA functions: hybridization and transcription"}]},{"@id":"https://cir.nii.ac.jp/crid/1363670318390601984","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Sequence-specific polypeptoids: A diverse family of heteropolymers with stable secondary structure"}]},{"@id":"https://cir.nii.ac.jp/crid/1363670318745958144","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Integrated evolutionary analysis reveals antimicrobial peptides with limited resistance"}]},{"@id":"https://cir.nii.ac.jp/crid/1363670318826735616","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Peptide Design Principles for Antimicrobial Applications"}]},{"@id":"https://cir.nii.ac.jp/crid/1363670318961328512","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Structure-Activity Relationship Study of Novel Peptoids That Mimic the Structure of Antimicrobial Peptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1363670319144112640","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Non-haemolytic β-amino-acid oligomers"}]},{"@id":"https://cir.nii.ac.jp/crid/1363670319191334144","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Synthesis of all-hydrocarbon stapled α-helical peptides by ring-closing olefin metathesis"}]},{"@id":"https://cir.nii.ac.jp/crid/1363670319526428544","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Short Alkylated Peptoid Mimics of Antimicrobial Lipopeptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1363670320014290944","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Mono-substitution effects on antimicrobial activity of stapled heptapeptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1363670320804662144","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Antimicrobial activity of doubly-stapled alanine/lysine-based peptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1363951793976418944","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Tailoring the Physicochemical Properties of Antimicrobial Peptides onto a Thiazole-Based γ-Peptide Foldamer"}]},{"@id":"https://cir.nii.ac.jp/crid/1363951794223773824","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Structure of antiamoebin I from high resolution field desorption and gas chromatographic mass spectrometry studies"}]},{"@id":"https://cir.nii.ac.jp/crid/1363951795041608832","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Hydrophobic interactions modulate antimicrobial peptoid selectivity towards anionic lipid membranes"}]},{"@id":"https://cir.nii.ac.jp/crid/1363951795200973312","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Activation of Apoptosis in Vivo by a Hydrocarbon-Stapled BH3 Helix"}]},{"@id":"https://cir.nii.ac.jp/crid/1363951795260226304","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Optochemical control of genetically engineered neuronal nicotinic acetylcholine receptors"}]},{"@id":"https://cir.nii.ac.jp/crid/1363951796220671360","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Use of Parallel Synthesis To Probe Structure−Activity Relationships among 12-Helical β-Peptides:  Evidence of a Limit on Antimicrobial Activity"}]},{"@id":"https://cir.nii.ac.jp/crid/1364233269576982656","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"α-Aminoisobutyric Acid, β-Hydroxyleucine, and γ-Methylproline from the Hydrolysis of a Natural Product"}]},{"@id":"https://cir.nii.ac.jp/crid/1364233269727661056","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Antibacterial and Antibiofilm Activity and Mode of Action of Magainin 2 against Drug-Resistant Acinetobacter baumannii"}]},{"@id":"https://cir.nii.ac.jp/crid/1364233269859195008","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Helical screw‐sense preferences of peptides based on chiral, C<sup>α</sup>‐tetrasubstituted α‐amino acids"}]},{"@id":"https://cir.nii.ac.jp/crid/1364233269897248000","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Effect of aminoisobutyric acid (Aib) substitutions on the antimicrobial and cytolytic activities of the frog skin peptide, temporin-1DRa"}]},{"@id":"https://cir.nii.ac.jp/crid/1364233270001749888","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Foldamers:  A Manifesto"}]},{"@id":"https://cir.nii.ac.jp/crid/1364233270797329536","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Membrane targeting cationic antimicrobial peptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001204168204032","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Design and Synthesis of Chiral .ALPHA.,.ALPHA.-Disubstituted Amino Acids and Conformational Study of Their Oligopeptides"},{"@value":"Design and Synthesis of Chiral α,α-Disubstituted Amino Acids and Conformational Study of Their Oligopeptides"},{"@language":"ja-Kana","@value":"Design and Synthesis of Chiral アルファ アルファ Disubstituted Amino Acids and Conformational Study of Their Oligopeptides"}]},{"@id":"https://cir.nii.ac.jp/crid/1390292251331801344","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Peptide Tool-Driven Functional Elucidation of Biomolecules Related to Endocrine System and Metabolism"}]},{"@id":"https://cir.nii.ac.jp/crid/1390298997211622912","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Rational Design of Amphipathic Antimicrobial Peptides with Alternating L-/D-Amino Acids That Form Helical Structures"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1002/cmdc.202000940"},{"@type":"KAKEN","@value":"PRODUCT-23615988"},{"@type":"KAKEN","@value":"PRODUCT-24031691"},{"@type":"KAKEN","@value":"PRODUCT-23471605"},{"@type":"KAKEN","@value":"PRODUCT-23663053"},{"@type":"KAKEN","@value":"PRODUCT-23400839"},{"@type":"OPENAIRE","@value":"doi_dedup___::56b8ef82d73c30ab3c91b2a4d521945c"},{"@type":"CROSSREF","@value":"10.1039/d2ob01715f_references_DOI_Ju3wx0UUw30ZUH8paqXCZR5uihI"},{"@type":"CROSSREF","@value":"10.1039/d5ob00244c_references_DOI_Ju3wx0UUw30ZUH8paqXCZR5uihI"},{"@type":"CROSSREF","@value":"10.3390/pr10050924_references_DOI_Ju3wx0UUw30ZUH8paqXCZR5uihI"},{"@type":"CROSSREF","@value":"10.3390/antibiotics12010019_references_DOI_Ju3wx0UUw30ZUH8paqXCZR5uihI"},{"@type":"CROSSREF","@value":"10.1016/j.bmc.2022.117021_references_DOI_Ju3wx0UUw30ZUH8paqXCZR5uihI"},{"@type":"CROSSREF","@value":"10.1248/cpb.c22-00048_references_DOI_Ju3wx0UUw30ZUH8paqXCZR5uihI"},{"@type":"CROSSREF","@value":"10.1248/cpb.c23-00465_references_DOI_Ju3wx0UUw30ZUH8paqXCZR5uihI"},{"@type":"CROSSREF","@value":"10.1039/d4cc06138a_references_DOI_Ju3wx0UUw30ZUH8paqXCZR5uihI"},{"@type":"CROSSREF","@value":"10.1021/acsomega.3c06397_references_DOI_Ju3wx0UUw30ZUH8paqXCZR5uihI"}]}