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Title: | Design of Helical Peptide Foldamers through α,β → β,γ Double-Bond Migration |
Authors: | VEERESH, KURUVA GOPI, HOSAHUDYA N. Dept. of Chemistry |
Keywords: | Beta-Amino Acid Gamma-Peptides Secondary Structures Structural Features Alpha/Beta-Peptides Hybrid Peptides Biosynthesis Ansamitocin Sequences Residues TOC-JUL-2019 2019 |
Issue Date: | Jun-2019 |
Publisher: | American Chemical Society |
Citation: | Organic Letters, 21(12), 4500-4504. |
Abstract: | The direct transformation of nonhelical α,γ-hybrid peptides composed of alternating α- and E-vinylogous amino acids into 12-helical structures through a base-mediated α,β → β,γ double-bond migration is reported. The conformations of double-bond-migrated new 12-helices were studied in single crystals and in solution. Instructively, the 12-helices reported here were found to be acid labile, and they completely break down into the corresponding amino acid derivatives upon treatment with acids. |
URI: | http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/3751 https://doi.org/10.1021/acs.orglett.9b01365 |
ISSN: | 1523-7060 1523-7052 |
Appears in Collections: | JOURNAL ARTICLES |
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