Effects of D-Leu Residues on the Helical Secondary Structures of L-Leu-Based Nonapeptides
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- Demizu Yosuke
- Division of Organic Chemistry, National Institute of Health Sciences
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- Yamashita Hiroko
- Division of Organic Chemistry, National Institute of Health Sciences Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology
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- Misawa Takashi
- Division of Organic Chemistry, National Institute of Health Sciences
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- Doi Mitsunobu
- Osaka University of Pharmaceutical Sciences
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- Tanaka Masakazu
- Graduate School of Biomedical Sciences, Nagasaki University
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- Kurihara Masaaki
- Division of Organic Chemistry, National Institute of Health Sciences Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology
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Abstract
The influence of D-Leu residues on the helical structures of L-Leu-based-nonapeptides was investigated. Specifically, the preferred conformations of four diastereomeric nonapeptides, Boc-(L-Leu-L-Leu-Aib)3-OMe (1); Boc-(L-Leu-L-Leu-Aib)2-L-Leu-D-Leu-Aib-OMe (2), which contained one D-Leu residue; Boc-L-Leu-D-Leu-Aib-L-Leu-L-Leu-Aib-L-Leu-D-Leu-Aib-OMe (3), which contained two D-Leu residues; and Boc-(L-Leu-D-Leu-Aib)3-OMe (4), were analyzed in solution and in the crystalline state. Peptide 1 formed a right-handed (P) 310-helix in solution. Peptides 2 and 3 both formed (P) 310-helices in solution and (P) α-helices in the crystalline state. Peptide 4 formed a (P) α-helix both in solution and in the crystalline state.
Journal
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- Chemical and Pharmaceutical Bulletin
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Chemical and Pharmaceutical Bulletin 63 (3), 218-224, 2015
The Pharmaceutical Society of Japan
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Details 詳細情報について
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- CRID
- 1390282679153307904
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- NII Article ID
- 130004803775
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- NII Book ID
- AA00602100
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- ISSN
- 13475223
- 00092363
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- HANDLE
- 10069/35273
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- NDL BIB ID
- 026193109
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- PubMed
- 25757493
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- Text Lang
- en
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- Data Source
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- JaLC
- IRDB
- NDL
- Crossref
- PubMed
- CiNii Articles
- KAKEN
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- Abstract License Flag
- Disallowed