Novel disintegrin‐like peptides derived from an amphibian skin cDNA sequence of Hypsiboas punctatus
| Autor: | Luisa M. R. A. Tacca, Claudia Jorge do Nascimento, Diego Arantes Teixeira Pires, Eder Alves Barbosa, André M. Murad, Joseph E. Aslan, Carlos Bloch |
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| Rok vydání: | 2021 |
| Předmět: |
DNA
Complementary Platelet Aggregation Disintegrins Integrin Peptide Biochemistry Amphibians Structural Biology Complementary DNA Drug Discovery Disintegrin Animals Platelet activation Molecular Biology Peptide sequence Pharmacology chemistry.chemical_classification biology cDNA library Organic Chemistry General Medicine chemistry biology.protein Molecular Medicine Peptides Function (biology) |
| Zdroj: | Journal of Peptide Science. 28 |
| ISSN: | 1099-1387 1075-2617 |
| DOI: | 10.1002/psc.3382 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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