Ribbon structure stabilized by C10 and C12 turns in αγ hybrid peptide
| Autor: | Rajni Kant, Vivek K. Gupta, Subrayashastry Aravinda, Rajkishor Rai, Naiem Ahmad Wani |
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| Rok vydání: | 2016 |
| Předmět: |
Pharmacology
chemistry.chemical_classification Oligopeptide 010405 organic chemistry Hydrogen bond Chemistry Organic Chemistry Ribbon diagram Peptide General Medicine 010402 general chemistry 01 natural sciences Biochemistry 0104 chemical sciences Turn (biochemistry) Crystallography Residue (chemistry) Protein stability Structural Biology Drug Discovery Molecular Medicine Molecular Biology Peptide sequence |
| Zdroj: | Journal of Peptide Science. 22:208-213 |
| ISSN: | 1075-2617 |
| DOI: | 10.1002/psc.2864 |
| Popis: | The present study describes the synthesis and crystallographic analysis of αγ hybrid peptides, Boc-Gpn-L-Pro-NHMe (1), Boc-Aib-Gpn-L-Pro-NHMe (2), and Boc-L-Pro-Aib-Gpn-L-Pro-NHMe (3). Peptides 1 and 2 adopt expanded 12-membered (C12 ) helical turn over γα segment. Peptide 3 promotes the ribbon structure stabilized by type II β-turn (C10 ) followed by the expanded C12 helical γα turn. Both right-handed and left-handed helical conformations for Aib residue are observed in peptides 2 and 3, respectively. |
| Databáze: | OpenAIRE |
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