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On resin side-chain cyclization of complex peptides using CuAAC

Academic Article
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Overview

authors

  • Ingale, S.
  • Dawson, Philip

publication date

  • June 2011

journal

  • Organic Letters  Journal

abstract

  • Triazole tethers have been explored for stabilization of secondary structures in peptides. Despite the utility of this approach, cyclization efficiency in complex peptides remains a significant challenge. A robust, on-resin protocol for side chain to side chain macrocyclization by CuAAC is described. This protocol was applied to the synthesis of a series of 21 amino acid helical peptides presenting a binding dipeptide motif from the membrane proximal external region (MPER) of HIV-1 gp41.

subject areas

  • Amino Acid Sequence
  • Circular Dichroism
  • Copper
  • Cyclization
  • HIV Envelope Protein gp41
  • HIV-1
  • Molecular Structure
  • Peptide Fragments
  • Peptides
  • Triazoles
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Identity

International Standard Serial Number (ISSN)

  • 1523-7060

Digital Object Identifier (DOI)

  • 10.1021/ol200775h

PubMed ID

  • 21553819
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Additional Document Info

start page

  • 2822

end page

  • 2825

volume

  • 13

issue

  • 11

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