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

Valeria Castelletto1, Gemma E Newby, Ian W Hamley

  • 1School of Chemistry, Food Biosciences and Pharmacy, The University of Reading, Whiteknights, Reading, UK. v.castelletto@reading.ac.uk

Macromolecular Bioscience
|June 21, 2008
PubMed

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 = c(KLVFF-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 >or= 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.

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