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

Journal of peptide science : an official publication of the European Peptide Society 2022 May

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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. © 2021 European Peptide Society and John Wiley & Sons, Ltd.

Citation

Diego A T Pires, Luisa M R A Tacca, Joseph E Aslan, André M Murad, Claudia J Nascimento, Eder A Barbosa, Carlos Bloch. Novel disintegrin-like peptides derived from an amphibian skin cDNA sequence of Hypsiboas punctatus. Journal of peptide science : an official publication of the European Peptide Society. 2022 May;28(5):e3382