Identification of Bilirubin Binding Site in Type I Collagen View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2013-12

AUTHORS

Nagarajan Usharani, Gladstone Christopher Jayakumar, Swarna V. Kanth, Jonnalagadda Raghava Rao, Bangaru Chandrasekaran, Balachandran Unni Nair

ABSTRACT

The interaction of bilirubin with collagen in the significance of jaundice incidence have been previously reported and investigated. The novel peptide sequences containing bilirubin binding domain was identified and located to develop a basis for further studies investigating the interactions of collagen with bilirubin in the present study. In this study an intricate interaction between bilirubin and collagen was characterized and their binding domain has been established using in-gel digestion and LC–MS/MS analysis based on the collagen sequencing and peptide mass fingerprinting. The biotinylated bilirubin derivatives bind to α1(I) chain but not to α2(I) chains which clearly designates that bilirubin shows greater affinity to α1 chains of collagen. The intact proteins collected after analyzing the resulting complex mixture of peptides was used for peptide mapping. Using the electrospray method, among the other peptide sequence information obtained, the molecular weight of collagen alpha-2(I) chain was obtained by locating a 130 kDa weight peptide sequences with greater pi value (9.14) with 1,364 amino acid residues and collagen alpha-1(I) chain with 1,463 amino acid residues with 138.9 kDa molecular weight. This information leads to locate the exact sequence of these helices focussing on the domain identification. The total charge of the peptide domain sequences infers that the bilirubin participates in the electrostatic mode of interaction with collagen peptide. Moreover, other modes of interactions such as hydrogen bonding, covalent interactions and hydrophobic interactions are possible. More... »

PAGES

357-364

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10989-013-9359-7

DOI

http://dx.doi.org/10.1007/s10989-013-9359-7

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