Identification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database

Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. doi: 10.1128/AAC.01448-09. Epub 2010 Jan 19.

Abstract

To identify novel anti-HIV-1 peptides based on the antimicrobial peptide database (APD; http://aps.unmc.edu/AP/main.php), we have screened 30 candidates and found 11 peptides with 50% effective concentrations (EC(50)) of <10 microM and therapeutic indices (TI) of up to 17. Furthermore, among the eight peptides (with identical amino acid compositions but different sequences) generated by shuffling the sequence of an aurein 1.2 analog, two had a TI twice that of the original sequence. Because antiviral peptides in the database have an arginine/lysine (R/K) ratio of >1, increases in the Arg contents of amphibian maximin H5 and dermaseptin S9 peptides and the database-derived GLK-19 peptide improved the TIs. These examples demonstrate that the APD is a rich resource and a useful tool for developing novel HIV-1-inhibitory peptides.

Publication types

  • Research Support, N.I.H., Intramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amphibian Proteins / chemistry
  • Amphibian Proteins / genetics
  • Amphibian Proteins / pharmacology
  • Animals
  • Anti-HIV Agents* / chemistry
  • Anti-HIV Agents* / pharmacology
  • Antimicrobial Cationic Peptides* / chemistry
  • Antimicrobial Cationic Peptides* / genetics
  • Antimicrobial Cationic Peptides* / pharmacology
  • Databases, Protein
  • Drug Design
  • HIV-1 / drug effects*
  • Humans
  • Microbial Sensitivity Tests
  • Molecular Sequence Data
  • Structure-Activity Relationship

Substances

  • Amphibian Proteins
  • Anti-HIV Agents
  • Antimicrobial Cationic Peptides