Novel disintegrin-like peptides derived from an amphibian skin cDNA sequence of Hypsiboas punctatus

Diego A.T. Pires, Luisa M.R.A. Tacca, Joseph E. Aslan, André M. Murad, Claudia J. Nascimento, Eder A. Barbosa, Carlos Bloch

Research output: Contribution to journalArticlepeer-review

Abstract

Disintegrins comprise a family of small proteins that bind to and alter the physiological function of integrins, especially integrins that mediate platelet aggregation in blood. Here, we report a lysine-glycine-aspartic acid (KGD) disintegrin-like motif present in a 15-amino acid residue peptide identified in a cDNA library of the amphibian Hypsiboas punctatus skin. The original peptide sequence was used as a template from which five new analogs were designed, chemically synthesized by solid phase, and tested for disintegrin activity and tridimensional structural studies using NMR spectroscopy. The original amphibian peptide had no effect on integrin-mediated responses. Nevertheless, derived peptide analogs inhibited integrin-mediated platelet function, including platelet spreading on fibrinogen.

Original languageEnglish (US)
JournalJournal of Peptide Science
DOIs
StateAccepted/In press - 2021

Keywords

  • amphibian
  • disintegrin motifs
  • peptide
  • platelet activation

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Organic Chemistry

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