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A Double-Headed Gly-Pro-Arg-Pro Ligand Mimics the Functions of the E Domain of Fibrin for Promoting the End-To-End Crosslinking of Gamma Chains by Factor XIIIa

A Double-Headed Gly-Pro-Arg-Pro Ligand Mimics the Functions of the E Domain of Fibrin for Promoting the End-To-End Crosslinking of Gamma Chains by Factor XIIIa

L Lorand, K N Parameswaran, S N Murthy

Proc Natl Acad Sci U S A. 1998 Jan 20;95(2):537-41.

PMID: 9435227

Abstract:

The E domain of fibrinogen represents the central region of the protein that, after the removal of fibrinopeptides from the N-termini of its alpha chains by thrombin, orders the noncovalent assembly of fibrin units into a half-staggered array. This structural organization is accomplished purely through noncovalent binding between the E domain of one molecule and the distal D domains of two others. The process of assembly has a physiologically important up-regulatory effect on the next enzymatic phase of blood coagulation, which is the factor XIIIa-catalyzed end-to-end ligation of the gamma chains at the D domains of the protein. Fibrin assembly, as well as the acceleration of the factor XIIIa reaction, could be prevented by Gly-Pro-Arg-Pro, a homologue of the natural sequence of amino acids at the N termini of alpha chains in the E domain. We have now succeeded with a simple double-headed ligand, bis(Gly-Pro-Arg-Pro-amido)polyethylene glycol, in fully replacing the regulatory functions of the large E domains of the native protein.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP67869629	Gly-Pro-Arg-Pro		67869-62-9	Price

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