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Preferred conformations of RDGX tetrapeptides to inhibit the binding of fibrinogen to platelets
- Preferred conformations of RDGX tetrapeptides to inhibit the binding of fibrinogen to platelets
- Park H.S.; Kim C.; Kang Y.K.
- Ewha Authors
- SCOPUS Author ID
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- Journal Title
- vol. 63, no. 5, pp. 298 - 313
- SCI; SCIE; SCOPUS
- The conformational study on Arg-Gly-Asp (RGD)-containing tetrapeptides in the unhydrated and hydrated states has been carried out using the force field ECEPP/3 and the hydration shell model. The tetrapeptides studied here are H-RGDX-OH (X = Trp, Tyr, Phe, Leu, Val, Cys, Gln, and Ser), which show the inhibitory activity for binding of fibrinogen to platelets in the order of RGDW ≈ RGDY ≈ RGDF ≈ RGDL > RGDV ≥ RGDC ≥ RGDQ ≥ RGDS. The backbone conformations with two C7 backbone-to-backbone hydrogen bonds between Asp and Arg residues and between Xaa and Gly residues are in common most probable for the RGD sequence of RGDX tetrapeptides in the hydrated state. The dominant β-turns for RGDX are found to be the types V' and IV at Gly-Asp and Asp-Xaa sequences, respectively, which are quite similar to the types II' and I (or II), respectively. However, it cannot be ruled out that the extended conformations are also remarkably feasible for RGDX tetrapeptides in water by peering the distributions of backbone conformations. These calculated results are consistent with the experimental results on RGD-containing proteins and conformationally constrained RGD-containing peptides. The reason why the RGDX becomes more potent as the side chain of the X residue is more hydrophobic may be ascribed to that the more hydrophobic is the residue X, the more populated are β-turn structures for the Gly-Asp sequence. The hydrophobic side chain of X residue exposed to water is likely to interact with the hydrophobic region of receptor easily. © 2002 Wiley Periodicals, Inc.
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