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Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: facets of their conformational features, structure-function correlations and membrane-perturbing abilities.

Abstract
Almost all hemolytic and antimicrobial peptides form part of the defense mechanism of species widely distributed across the evolutionary scale. Although these peptides are of varying lengths and composition, they form amphiphilic structures in a hydrophobic environment. They also have the ability to form channels in natural and model membranes. Hemolytic peptides have proven to be very useful in studying the mechanism of hemolysis and the permeability properties of red blood cells. Preliminary investigations indicate that these peptides may also be useful in the investigation of complex cellular phenomena like exocytosis and neurotransmission. Although molecules like vancomycin, bacitracin and penicillins have been extensively used as antibiotics for therapeutic purposes, most species throughout the evolutionary scale use peptides as antimicrobial agents. These peptides exert their activity by altering the permeability properties of the bacterial plasma membrane and do not interfere with macro molecular synthesis like the other antibiotics that are presently used in therapies. Hence it is likely that resistance to peptide antibacterial agents may not develop easily. Since the problem of antibiotic resistance is presently a particularly severe one, peptide antibiotics may be the drugs of choice in the future.
AuthorsG Saberwal, R Nagaraj
JournalBiochimica et biophysica acta (Biochim Biophys Acta) Vol. 1197 Issue 2 Pg. 109-31 (Jun 29 1994) ISSN: 0006-3002 [Print] Netherlands
PMID8031824 (Publication Type: Journal Article, Review)
Chemical References
  • Anti-Infective Agents
  • Antimicrobial Cationic Peptides
  • Designer Drugs
  • Hemolysin Proteins
  • Proteins
Topics
  • Amino Acid Sequence
  • Animals
  • Anti-Infective Agents (chemistry)
  • Antimicrobial Cationic Peptides
  • Base Sequence
  • Designer Drugs
  • Hemolysin Proteins (chemistry)
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Proteins (chemistry)
  • Structure-Activity Relationship

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