Author
Yu, Haining; Muñoz, Eva M.; Edens, R. Erik; Linhardt, Robert J.
Other Contributors
Date Issued
2005-11-15
Subject
Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
Degree
Terms of Use
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Full Citation
Kinetic Studies on the Interaction of Heparin and Complement Proteins using Surface Plasmon Resonance, H. Yu, E.M. Muñoz, F. Zhang, R.E. Edens, R.J. Linhardt, Biochemica Biophysica Acta, Biochemica Biophysica Acta, 1726, 168-176, 2005.
Abstract
Heparin is a naturally occurring polysaccharide known to interact with complement proteins and regulate multiple steps in the complement cascade. Quantitative information, in the form of affinity constants for heparin-complement interactions, is not generally available and there are no reports of a comprehensive analysis using the same interaction method. Such information should improve our understanding of how exogenously administered pharmaceutical heparin and the related endogenous polysaccharide, heparan sulfate, regulate complement activation. The current study provides the first comprehensively analysis of the binding of various complement proteins to heparin using surface plasmon resonance (SPR). Complement proteins C1, C2, C3, C4, C5, C6, C7, C8, C9, C1INH, factor I, factor H, factor B and factor P all bind heparin but exhibit different binding kinetics and dissociation constants (Kd) ranging from 2 to 320 nM. By taking into account these Kd values and the serum concentrations of these complement proteins, the percentage of each binding to exogenously administered heparin was calculated and found to range from 2% to 41%. This study provides essential information required for the rational design of new therapeutic agents capable of regulating the complement activation.;
Description
Biochemica Biophysica Acta, Biochemica Biophysica Acta, 1726, 168-176; Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Department
The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
Publisher
Elsevier
Relationships
The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Biochimica et Biophysica Acta - General Subjects; https://harc.rpi.edu/;
Access
A full text version is available in DSpace@RPI;