{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T20:01:14Z","timestamp":1791576074271,"version":"4.3.4"},"reference-count":164,"publisher":"MDPI AG","issue":"8","license":[{"start":{"date-parts":[[2018,8,7]],"date-time":"2018-08-07T00:00:00Z","timestamp":1533600000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>Disintegrins are a family of small cysteine-rich peptides, found in a wide variety of snake venoms of different phylogenetic origin. These peptides selectively bind to integrins, which are heterodimeric adhesion receptors that play a fundamental role in the regulation of many physiological and pathological processes, such as hemostasis and tumor metastasis. Most disintegrins interact with integrins through the RGD (Arg-Gly-Asp) sequence loop, resulting in an active site that modulates the integrin activity. Some variations in the tripeptide sequence and the variability in its neighborhood result in a different specificity or affinity toward integrin receptors from platelets, tumor cells or neutrophils. Recombinant forms of these proteins are obtained mainly through Escherichia coli, which is the most common host used for heterologous expression. Advances in the study of the structure-activity relationship and importance of some regions of the molecule, especially the hairpin loop and the C-terminus, rely on approaches such as site-directed mutagenesis and the design and expression of chimeric peptides. This review provides highlights of the biological relevance and contribution of recombinant disintegrins to the understanding of their binding specificity, biological activities and therapeutic potential. The biological and pharmacological relevance on the newest discoveries about this family of integrin-binding proteins are discussed.<\/jats:p>","DOI":"10.3390\/toxins10080321","type":"journal-article","created":{"date-parts":[[2018,8,7]],"date-time":"2018-08-07T11:20:23Z","timestamp":1533640823000},"page":"321","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":32,"title":["Recombinant and Chimeric Disintegrins in Preclinical Research"],"prefix":"10.3390","volume":"10","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7865-8481","authenticated-orcid":false,"given":"Victor","family":"David","sequence":"first","affiliation":[{"name":"Laborat\u00f3rio de Hemostase e Venenos, Instituto de Bioqu\u00edmica M\u00e9dica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Barbara Barbosa","family":"Succar","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Hemostase e Venenos, Instituto de Bioqu\u00edmica M\u00e9dica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8563-6432","authenticated-orcid":false,"given":"Jo\u00e3o Alfredo","family":"De Moraes","sequence":"additional","affiliation":[{"name":"Instituto de Ci\u00eancias Biom\u00e9dicas, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roberta Ferreira Gomes","family":"Saldanha-Gama","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Farmacologia Celular e Molecular, Departamento de Biologia Celular, IBRAG, Universidade do Estado do Rio de Janeiro, Rio de Janeiro 20.551-030, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christina","family":"Barja-Fidalgo","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Farmacologia Celular e Molecular, Departamento de Biologia Celular, IBRAG, Universidade do Estado do Rio de Janeiro, Rio de Janeiro 20.551-030, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3156-6923","authenticated-orcid":false,"given":"Russolina Benedeta","family":"Zingali","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Hemostase e Venenos, Instituto de Bioqu\u00edmica M\u00e9dica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2018,8,7]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"2151","DOI":"10.1161\/01.CIR.91.8.2151","article-title":"Multicenter, Randomized, Double-Blind, Placebo-Controlled Trial of the Platelet Integrin Glycoprotein IIb\/IIIa Blocker Integrelin in Elective Coronary Intervention","volume":"91","author":"Tcheng","year":"1995","journal-title":"Circulation"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"168","DOI":"10.3181\/00379727-195-43129B","article-title":"Disintegrins: A family of integrin inhibitory proteins from viper venoms","volume":"195","author":"Gould","year":"1990","journal-title":"Proc. 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