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 language | English (US) |
|---|---|
| Title of host publication | Handbook of Biologically Active Peptides |
| Publisher | Elsevier Inc. |
| Pages | 573-578 |
| Number of pages | 6 |
| ISBN (Print) | 9780123694423 |
| DOIs | |
| State | Published - 2006 |
| Externally published | Yes |
ASJC Scopus subject areas
- General Biochemistry, Genetics and Molecular Biology