Structure and Design of Multipotent Peptide Microbicides

Abstract

The goal of this project is to design novel peptide antibiotics using a naturally occurring family of peptides, known as defensins, as models. Defensins are homologous peptides, 29-34 residues in length, which are major constituents of the cytoplasmic granules of polymorphonuclear leukocytes. The structural hallmark of the defensin peptide family is a conserved infrastructure comprised of 1 arginine, 1 glycine, and 6 disulfide-linked cysteine residues. Although the peptides are similar in their overall fold, they possess diverse antimicrobial spectra and potencies. By correlating specific biocidal activities with unique structural features, we seek to design custom peptide antimicrobials based on structure-function principles derived from these studies. Insight into the molecule details of the peptide-target cell interactions may contribute to the general understanding of protein-membrane recognition processes. Keywords: Neutrophils, Synthesis(Chemistry).

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Document Details

Document Type
Technical Report
Publication Date
Aug 01, 1988
Accession Number
ADA199085

Entities

People

  • Michael E. Selsted

Organizations

  • UCLA David Geffen School of Medicine

Tags

Communities of Interest

  • Biomedical

DTIC Thesaurus Topics

  • Amino Acids
  • Anhydrides
  • Animals
  • Anti-Bacterial Agents
  • Anti-Infective Agents
  • Cells
  • Chemical Synthesis
  • Chemistry
  • Cysteine
  • Cytoplasmic Granules
  • Eukaryotes
  • Granulocytes
  • Lagomorphs
  • Membranes
  • Polymorphonuclear Leukocytes
  • Rodents
  • Spectra

Readers

  • Molecular and Cellular Biochemistry
  • Systems Analysis and Design