Literature DB >> 1530602

Conformational study of cyclo(1,5)-Ac-Pen-Arg-Gly-Asp-Cys-NH2 in water by NMR and molecular dynamics.

T J Siahaan1, S Chakrabarti, D Vander Velde.   

Abstract

Cyclo(1,5)-Ac-Pen-Arg-Gly-Asp-Cys-NH2 (3) is a potent inhibitor of platelet aggregation. Nuclear magnetic resonance (NMR) and restrained molecular dynamics were used to study the conformations of 3. Elucidation of RGD conformations in 3 will increase the understanding of interaction between the RGD-sequence with GPIIb/IIIa.

Entities:  

Mesh：

Substances：

Year:  1992        PMID： 1530602     DOI： 10.1016/0006-291x(92)91302-7

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


  3 in total

1.  Mechanistic Basis for the Binding of RGD- and AGDV-Peptides to the Platelet Integrin αIIbβ3.

Authors:  Olga Kononova; Rustem I Litvinov; Dmitry S Blokhin; Vladimir V Klochkov; John W Weisel; Joel S Bennett; Valeri Barsegov
Journal:  Biochemistry       Date:  2017-03-22       Impact factor: 3.162

2.  The importance of structural factors on the rate and the extent of N,O-acyl migration in cyclic and linear peptides.

Authors:  R Oliyai; T J Siahaan; V J Stella
Journal:  Pharm Res       Date:  1995-03       Impact factor: 4.200

3.  Three-dimensional structure of echistatin and dynamics of the active site.

Authors:  Y Chen; A K Suri; D Kominos; G Sanyal; A M Naylor; S M Pitzenberger; V M Garsky; R M Levy; J Baum
Journal:  J Biomol NMR       Date:  1994-05       Impact factor: 2.835
  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.