Elucidation of a common structure of selective fibrinogen receptor antagonists

In this paper, we investigate the common structural and electrostatic parameters of a series of specific inhibitors of the alpha IIb beta 3 integrin. Molecular dynamics simulations with an explicit aqueous environment led to an original theoretical pattern. Our results may suggest that the studied n...

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Bibliographic Details
Published inJournal of computer-aided molecular design Vol. 12; no. 6; pp. 533 - 542
Main Authors Minoux, H, Moitessier, N, Chapleur, Y, Maigret, B
Format Journal Article
LanguageEnglish
Published Netherlands Springer Nature B.V 01.11.1998
Subjects
Amino Acid Sequence
Aqueous environments
Computer aided design
Computer simulation
Fibrinogen
Inhibitors
Models, Molecular
Molecular dynamics
Molecular Structure
Oligopeptides - chemistry
Platelet Aggregation Inhibitors - chemistry
Platelet Glycoprotein GPIIb-IIIa Complex - antagonists & inhibitors
Proteins
Receptors
Recognition
Static Electricity
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Summary:In this paper, we investigate the common structural and electrostatic parameters of a series of specific inhibitors of the alpha IIb beta 3 integrin. Molecular dynamics simulations with an explicit aqueous environment led to an original theoretical pattern. Our results may suggest that the studied non-peptide alpha IIb beta 3 antagonists developed upon the Arg-Gly-Asp ubiquitous recognition sequence, in fact, should mimic the C-terminus part of the fibrinogen gamma chain. This assumption could, therefore, explain their specificity with respect to other Arg-Gly-Asp-dependent integrins.
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ISSN:0920-654X
1573-4951
DOI:10.1023/A:1008024924329