Biological properties of low molecular mass peptide dendrimers

Int J Pharm. 2006 Feb 17;309(1-2):208-17. doi: 10.1016/j.ijpharm.2005.10.039. Epub 2006 Jan 18.

Abstract

A series of new, low molecular mass, lysine-based peptide dendrimers with varying distribution of cationic and aromatic groups in the structure were synthesized. They expressed antimicrobial activity against Gram-positive (Staphylococcus aureus) and Gram-negative (Escherichia coli) bacteria as well as against fungal pathogens (Candida albicans). Their cytotoxic, haematotoxic, and genotoxic effects were studied. It appears that degree of branching and steric distribution and types of hydrophobic (aromatic) groups and cationic centres are important components of dendrimeric structure and influence both antimicrobial potency and toxicity. Such 3D structure of our dendrimers mimics that of the natural antimicrobial peptides and can be achieved by application of dendrimer chemistry.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Anti-Infective Agents / chemical synthesis
  • Anti-Infective Agents / pharmacology*
  • Anti-Infective Agents / toxicity
  • Candida albicans / drug effects
  • Candida albicans / growth & development
  • Cell Line
  • Cell Survival / drug effects
  • Cricetinae
  • DNA / chemistry
  • Dendrimers / chemical synthesis
  • Dendrimers / pharmacology*
  • Dendrimers / toxicity
  • Escherichia coli / drug effects
  • Escherichia coli / growth & development
  • Hemolysis / drug effects
  • Humans
  • Inhibitory Concentration 50
  • Lysine / chemistry
  • Microbial Sensitivity Tests
  • Molecular Weight
  • Oligopeptides / chemical synthesis
  • Oligopeptides / pharmacology*
  • Oligopeptides / toxicity
  • Protein Conformation
  • Staphylococcus aureus / drug effects
  • Staphylococcus aureus / growth & development

Substances

  • Anti-Infective Agents
  • Dendrimers
  • Oligopeptides
  • DNA
  • Lysine