NDLI: Studies on the chemico-biological characteristics of bilirubin binding with collagen.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Nagarajan, Usharani Christopher, Jayakumar Gladstone Jonnalagadda, Raghava Rao Chandrasekaran, Bangaru Balachandran, Unni Nair
Description	Country affiliation: India Author Affiliation: Nagarajan U ( CSIR-Central Leather Research Institute, Council of Scientific and Industrial Research, Adyar, Chennai 600 020, India.)
Abstract	The clinical impact of bilirubin on collagen is investigated using various physical, chemical and biological methods. Thermo gravimetric analysis and differential scanning analysis of collagen-bilirubin complex matrices indicate that crosslinking does not alter their thermal behavior of collagen. The polydispersity of collagen-bilirubin complex increases in the reacting medium suggesting that there is an increase in the number of interacting points between them. Based on the zeta potential values, the rate of mobility of interacted complex decreases by inferring the extent of binding compared to the control collagen. Emission intensity begins to increase with increase in concentration of bilirubin which ascribes the conformational changes around the aromatic amino acids in collagen. Binding is indicated by an increase in resonance units and the responses are corrected by subtraction of those obtained for native collagen. Bilirubin showed a higher affinity for collagen at a concentration of about 25 nM/mg. In this study, the association rate has been calculated which depicts the increased affinity of bilirubin to collagen. Affinity for bilirubin to collagen has been found to be 8.89×10(-3) s(-1). The greater part of binding of bilirubin to collagen is found to be electrostatic in nature. The investigation leads to comprehend the affinity of collagen-bilirubin complex during jaundice diseased tissues.
File Format	HTM / HTML
ISSN	09284931
Issue Number	8
Volume Number	33
e-ISSN	18730191
Journal	Materials Science and Engineering: C
Language	English
Publisher	Elsevier
Publisher Date	2013-12-01
Publisher Place	Netherlands
Access Restriction	Subscribed
Subject Keyword	Discipline Materials Science Bilirubin Metabolism Collagen Type I Animals Chemistry Immobilized Proteins Male Protein Binding Rats Rats, Wistar Spectrometry, Fluorescence Static Electricity Tail Journal Article
Content Type	Text
Resource Type	Article
Subject	Mechanics of Materials Biomaterials Condensed Matter Physics Bioengineering Mechanical Engineering

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