<i>In situ</i> neutralization in Boc‐chemistry solid phase peptide synthesis
書誌事項
- タイトル別名
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- Rapid, high yield assembly of difficult sequences
- 公開日
- 1992-09
- 権利情報
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- http://onlinelibrary.wiley.com/termsAndConditions#vor
- DOI
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- 10.1111/j.1399-3011.1992.tb00291.x
- 公開者
- Wiley
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説明
<jats:p>Simple, effective protocols have been developed for manual and machine‐assisted Boc‐chemistry solid phase peptide synthesis on polystyrene resins. These use <jats:italic>in situ</jats:italic> neutralization [i.e. neutralization simultaneous with coupling], high concentrations (> 0.2 M) of Boc‐amino acid‐OBt esters plus base for rapid coupling, 100% TFA for rapid Boc group removal, and a single short (30 s) DMF flow wash between deprotection/coupling and between coupling/deprotection. Single 10 min coupling times were used throughout. Overall cycle times were 15 min for manual and 19 min for machine‐assisted synthesis (75 residues per day). No racemization was detected in the base‐catalyzed coupling step. Several side reactions were studied, and eliminated. These included: pyrrolidonecarboxylic acid formation from Gln in hot TFA‐DMF; chain‐termination by reaction with excess HBTU; and, chain termination by acetylation (from HOAc in commercial Boc‐amino acids). The <jats:italic>in situ</jats:italic> neutralization protocols gave a significant increase in the efficiency of chain assembly, especially for “difficult” sequences arising from sequence‐dependent peptide chain aggregation in standard (neutralization prior to coupling) Boc‐chemistry SPPS protocols or in Fmoc‐chemistry SPPS. Reported syntheses include HIV‐1 protease(1–50,Cys.amide), HIV‐1 protease(53–99), and the full length HIV‐1 protease(1–99).</jats:p>
収録刊行物
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- International Journal of Peptide and Protein Research
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International Journal of Peptide and Protein Research 40 (3-4), 180-193, 1992-09
Wiley