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

Castelletto, V., Newby, G.E. and Hamley, I.W. ORCID: https://orcid.org/0000-0002-4549-0926 (2008) Interactions of KLVFF-PEG peptide conjugate with fibrinogen in neutral aqueous solutions. Macromolecular Bioscience, 8 (12). pp. 1182-1189. ISSN 1616-5187

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To link to this item DOI: 10.1002/mabi.200800065

Abstract/Summary

In this work we report on the interaction of KLVFF-PEG with fibrinogen (Fbg) in neutral aqueous solutions at 20 degrees C, for particular ratios of KLVFF-PEG to Fbg concentration, Delta = CKLVFF-PEG/C-Fbg- Our results show the formation of Fbg/KLVFF-PEG complexes for Delta > 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 Delta >= 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.

Item Type:Article
Refereed:Yes
Divisions:Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:11103
Uncontrolled Keywords:peptides, proteins, SAXS, self-assembly, self-organization, HEREDITARY RENAL AMYLOIDOSIS, GLYCOL) LIPID CONJUGATE, FRAME-SHIFT, MUTATION, X-RAY-SCATTERING, ALPHA-CHAIN GENE, BOVINE FIBRINOGEN, CRYSTAL-STRUCTURE, DILUTE-SOLUTIONS, SPECTROSCOPY, AGGREGATION

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