Structure and function of RGD peptides derived from disintegrin proteins

Jiun Kim, Sung Yu Hong, Hye Seo Park, Doo Sik Kim, Weontae Lee

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18 Citations (Scopus)

Abstract

The Arg-Gly-Asp (RGD) sequence serves as the primary recognition site in extracellular matrix proteins, and peptides containing this sequence can mimic the biological activities of matrix proteins. We have initiated structure-function studies of two RGD containing peptides, RGD-5(AGGDD) and cyclic RGD-6(CARGDDC). Assays have shown that cyclic RGD-peptides inhibit platelet aggregation more efficiently than linear ones. NMR data revealed that RGD-5 and RGD-6 have entirely different conformation. RGD-5 has a linear extended structure and RGD-6 has a stable loop conformation. In RGD-5 the guanidinium group of Arg2 and the carboxyl group of Asp4 lie in parallel, whereas the side-chains of Arg3 and Asp5 of RGD-6 are located in different planes, supporting the idea that the stability of the cyclic form derives from the packing of the side chain of the Arg and Asp residues. The structural features of these peptides could provide a basis for designing new drugs against diseases related to platelet aggregation and as cancer antagonists.

Original languageEnglish
Pages (from-to)205-211
Number of pages7
JournalMolecules and cells
Volume19
Issue number2
Publication statusPublished - 2005 Dec 1

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All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

Cite this

Kim, J., Hong, S. Y., Park, H. S., Kim, D. S., & Lee, W. (2005). Structure and function of RGD peptides derived from disintegrin proteins. Molecules and cells, 19(2), 205-211.