Structure-activity relationships of an anti-HIV peptide, T22

Biochem Biophys Res Commun. 1994 Dec 30;205(3):1729-35. doi: 10.1006/bbrc.1994.2868.

Abstract

T22 ([Tyr5,12,Lys7]-polyphemusin II) has been shown to have a strong anti-human immunodeficiency virus (HIV) activity comparable to that of 3'-azido-2',3'-dideoxythymidine (AZT). We studied the structure-anti-HIV activity relationships of T22 and determined the following information. The number of Arg residues in the N-terminal and C-terminal regions of T22 is closely related with anti-HIV activity. Disulfide rings, especially the major disulfide ring, are indispensable for anti-HIV activity and maintenance of the secondary structure. Between two repeats of Tyr-Arg-Lys, which are a characteristic structure contained in T22, Tyr-Arg-Lys in the N-terminal portion is more closely related with anti-HIV activity. We found some compounds having a higher selectivity index (50% cytotoxic concentration/50% effective concentration) than that of T22.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antimicrobial Cationic Peptides*
  • Antiviral Agents / chemistry*
  • Antiviral Agents / pharmacology*
  • Arginine / chemistry
  • Binding Sites
  • Cell Line
  • Cytopathogenic Effect, Viral / drug effects
  • Disulfides / chemistry
  • HIV-1 / drug effects*
  • HIV-1 / pathogenicity
  • Humans
  • Molecular Sequence Data
  • Peptides / chemical synthesis
  • Peptides / chemistry*
  • Peptides / pharmacology*
  • Structure-Activity Relationship

Substances

  • Antimicrobial Cationic Peptides
  • Antiviral Agents
  • Disulfides
  • Peptides
  • T22 protein, synthetic
  • Arginine