Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Amino acids that specify structure through hydrophobic clustering and histidine-aromatic interactions lead to biologically active peptidomimetics

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Graciani, N. R.
  • Tsang, K. Y.
  • McCutchen, S. L.
  • Kelly, Jeffery

publication date

  • 1994

journal

  • Bioorganic & Medicinal Chemistry  Journal

abstract

  • Acyclic beta-sheet structure can be nucleated in heptapeptides when the 4-(2-aminoethyl)-6-dibenzofuranpropanoic acid residue (1) is flanked in sequence by two His residues, a His residue and a hydrophobic residue or by two hydrophobic residues. Acyclic beta-sheet peptidomimetics having an appropriate sequence have sufficient structural integrity to exhibit antimicrobial activity equivalent to that of gramicidin S.

subject areas

  • Amino Acid Sequence
  • Amino Acids
  • Chemistry, Physical
  • Circular Dichroism
  • Histidine
  • Kinetics
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Oligopeptides
  • Peptides
  • Peptides, Cyclic
  • Physicochemical Phenomena
  • Protein Conformation
  • Protein Structure, Secondary
  • Structure-Activity Relationship
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0968-0896 (Print) 0968-0896 (Linking)

PubMed ID

  • 7712134
scroll to property group menus

Additional Document Info

start page

  • 999

end page

  • 1006

volume

  • 2

issue

  • 9

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support