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Updated: Jul 3, 2026

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
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Polymerization-defective fibrinogen variant gammaD364A binds knob "A" peptide mimic

Sheryl R Bowley1, Betsy K Merenbloom, Nobuo Okumura

  • 1Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599, USA.

Biochemistry
|July 23, 2008
PubMed
Summary

The negative charge of gamma364Asp is crucial for fibrin polymerization, not the residue itself. This charge facilitates essential electrostatic interactions for the initial step in fibrin clot formation.

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