Please use this identifier to cite or link to this item: http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/3751
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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