How nature morphs peptide scaffolds into antibiotics

Chembiochem. 2009 Jan 5;10(1):34-53. doi: 10.1002/cbic.200800438.

Abstract

The conventional notion that peptides are poor candidates for orally available drugs because of protease-sensitive peptide bonds, intrinsic hydrophilicity, and ionic charges contrasts with the diversity of antibiotic natural products with peptide-based frameworks that are synthesized and utilized by Nature. Several of these antibiotics, including penicillin and vancomycin, are employed to treat bacterial infections in humans and have been best-selling therapeutics for decades. Others might provide new platforms for the design of novel therapeutics to combat emerging antibiotic-resistant bacterial pathogens.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Anti-Bacterial Agents / chemistry*
  • Anti-Bacterial Agents / pharmacology*
  • Anti-Bacterial Agents / therapeutic use
  • Biological Products / chemistry*
  • Biological Products / pharmacology*
  • Biological Products / therapeutic use
  • Humans
  • Peptides / chemistry*
  • Peptides / pharmacology*
  • Peptides / therapeutic use
  • Ribosomal Proteins / chemistry
  • Ribosomal Proteins / metabolism
  • Ribosomal Proteins / pharmacology
  • Ribosomal Proteins / therapeutic use

Substances

  • Anti-Bacterial Agents
  • Biological Products
  • Peptides
  • Ribosomal Proteins