RGD-peptides and Some Immunological Problems

Ignacy Z. Siemion, Alicja Kluczyk, Marek Cebrat

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

This chapter discusses the application of adhesive RGD-peptides and their molecular mimetics as the inhibitors of several cardiovascular and immunological processes. The tetrapeptide RGDS plays a role of the adhesive site of fibronectin. The Arg (R) and Asp (D) residues present in the tetrapeptide play crucial role in this activity. The peptides containing the RGD sequence compete with fibronectin for cellular receptors and may act as anti-adhesive substances. Platelet aggregation consists of the cross-linking of fibrinogen or von Willebrand factor to the GPIIb/IIIa platelet integrin receptor. It takes place during the development of such cardiovascular diseases as myocardial infarction, transient ischemic attacks, strokes, and so on. Disintegrins, very potent inhibitors of the GPIIb/IIIa receptors, are polypeptides containing the exposed RGD motif obtained from the venom of Viperidae snakes and leaches. In barbourin and ussuristatin, only the RGD motif is changed into the KGD sequence. An RGD amide is sufficient for platelet aggregation inhibition at a high concentration. A very important role of RGD peptides in immunological phenomena results from the principal role of adhesion in the immune cell interactions. It plays a key role in antigen presentation, in antibody response, T cell help and suppression, aninflammatory processes, as well as in cytotoxic killing.

Original languageEnglish (US)
Title of host publicationHandbook of Biologically Active Peptides
PublisherElsevier Inc.
Pages573-578
Number of pages6
ISBN (Print)9780123694423
DOIs
Publication statusPublished - 2006
Externally publishedYes

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ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Siemion, I. Z., Kluczyk, A., & Cebrat, M. (2006). RGD-peptides and Some Immunological Problems. In Handbook of Biologically Active Peptides (pp. 573-578). Elsevier Inc.. https://doi.org/10.1016/B978-012369442-3/50085-4