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Studies on the molecular significance in the interaction of bilirubin with collagen
- Source :
- International journal of biological macromolecules. 61
- Publication Year :
- 2013
-
Abstract
- The present investigation is aimed to understand the physiological significance of bilirubin interaction with collagen. In human skin, collagen absorbs both free bilirubin and serum bound bilirubin from the human system. Interaction between bilirubin and collagen depends on time, temperature and concentration of bilirubin. There is an increase in the aggregation rate of collagen in the presence of biliruibin. At physiological condition, 125 nM of bilirubin is the maximum concentration absorbed by per mg of collagen molecule. Bilirubin accelerates the lateral growth of collagen fibrils by shifting its rate of nucleation. Moreover, collagen-bilirubin complex exhibit a tendency to undergo adsorption onto the surface of the fibroblast cells, showing detrimental effects on fibroblasts proliferations. Based on the collagen binding assays, the binding of bilirubin to collagen is found to be electrostatic in nature, which confirms binding between the amino acid fragment of α1 (I) region of collagen and carboxyl group of bilirubin. The biotinylated bilirubin derivatives show better binding to α1 (I) chain rather than α2 (I) chains which clearly designates that bilirubin shows greater affinity to α1 chains of collagen. This novel approach directs to reduce the occurrence of bilirubin in hyperbilirubinemia patients.
- Subjects :
- Male
Bilirubin
Human skin
Biochemistry
Collagen fibril
chemistry.chemical_compound
Blood serum
Structural Biology
medicine
Animals
Humans
Fibroblast
Molecular Biology
chemistry.chemical_classification
Binding Sites
Temperature
Aggregation rate
General Medicine
Fibroblasts
Hydrogen-Ion Concentration
Amino acid
Rats
Kinetics
medicine.anatomical_structure
chemistry
Biotinylation
Collagen
Protein Binding
Subjects
Details
- ISSN :
- 18790003
- Volume :
- 61
- Database :
- OpenAIRE
- Journal :
- International journal of biological macromolecules
- Accession number :
- edsair.doi.dedup.....040e68ca47b4d50004eb7ad22d2e1490