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Interactions of KLVFF-PEG peptide with fibrinogen in neutral aqueous solutions

DOI: 10.1002/mabi.200800065 DOI Help

Authors: Valerie Castelletto (University of Reading) , Ian W. Hamley (University of Reading) , Gemma E. Newby (University of Reading)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Macromolecular Bioscience , VOL 8 (12) , PAGES 1182-1189

State: Published (Approved)
Published: June 2008

Abstract: In this work we report on the interaction of KLVFF-PEG with fibrinogen (Fbg) in neutral aqueous solutions at 20 °C, for particular ratios of KLVFF-PEG to Fbg concentration, Δ = cKLVFF-PEG/cFbg. Our results show the formation of Fbg/KLVFF-PEG complexes for Δ > 0, such that there is not an extended network of complexes throughout the solution. In addition, cleaved protein and Fbg dimers are identified in the solution for Δ ≥ 0. There is a dramatic change in the tertiary structure of the Fbg upon KLVFF-PEG binding, although the KLVFF-PEG binds to the Fbg without affecting the secondary structure elements of the glycoprotein.

Journal Keywords: Peptides; Proteins; Saxs; Self-Assembly; Self-Organization

Subject Areas: Chemistry

Instruments: NONE-No attached Diamond beamline

Added On: 19/08/2009 23:07

Discipline Tags:

Molecular Complexes Chemistry Organic Chemistry

Technical Tags: