An informatics search for the low-molecular weight chromium-binding peptide

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An informatics search for the low-molecular weight chromium-binding peptide

Please use this identifier to cite or link to this item: http://dx.doi.org/10.1186/1472-6769-4-2

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dc.contributor.author Dinakarpandian, Deendayal
dc.contributor.author Morrissette, Vincent
dc.contributor.author Chaudhary, Shveta
dc.contributor.author Amini, Kambiz
dc.contributor.author Bennett, Brian
dc.contributor.author Van Horn, J David
dc.date.accessioned 2012-08-29T15:30:41Z
dc.date.available 2012-08-29T15:30:41Z
dc.date.issued 2004-12-16
dc.identifier.citation BMC Chemical Biology. 2004 Dec 16;4(1):2
dc.identifier.uri http://dx.doi.org/10.1186/1472-6769-4-2
dc.identifier.uri http://hdl.handle.net/10355/15068
dc.description.abstract Abstract Background The amino acid composition of a low molecular weight chromium binding peptide (LMWCr), isolated from bovine liver, is reportedly E:G:C:D::4:2:2:2, though its sequence has not been discovered. There is some controversy surrounding the exact biochemical forms and the action of Cr(III) in biological systems; the topic has been the subject of many experimental reports and continues to be investigated. Clarification of Cr-protein interactions will further understanding Cr(III) biochemistry and provide a basis for novel therapies based on metallocomplexes or small molecules. Results A genomic search of the non-redundant database for all possible decapeptides of the reported composition yields three exact matches, EDGEECDCGE, DGEECDCGEE and CEGGCEEDDE. The first two sequences are found in ADAM 19 (A Disintegrin and Metalloproteinase domain 19) proteins in man and mouse; the last is found in a protein kinase in rice (Oryza sativa). A broader search for pentameric sequences (and assuming a disulfide dimer) corresponding to the stoichiometric ratio E:D:G:C::2:1:1:1, within the set of human proteins and the set of proteins in, or related to, the insulin signaling pathway, yields a match at an acidic region in the α-subunit of the insulin receptor (-EECGD-, residues 175–184). A synthetic peptide derived from this sequence binds chromium(III) and forms a metal-peptide complex that has properties matching those reported for isolated LMWCr and Cr(III)-containing peptide fractions. Conclusion The search for an acidic decameric sequence indicates that LMWCr may not be a contiguous sequence. The identification of a distinct pentameric sequence in a significant insulin-signaling pathway protein suggests a possible identity for the LMWCr peptide. This identification clarifies directions for further investigation of LMWCr peptide fractions, chromium bio-coordination chemistry and a possible role in the insulin signaling pathway. Implications for models of chromium action in the insulin-signaling pathway are discussed.
dc.title An informatics search for the low-molecular weight chromium-binding peptide
dc.type Journal Article
dc.date.updated 2012-08-29T15:30:41Z
dc.description.version Peer Reviewed
dc.language.rfc3066 en
dc.rights.holder Deendayal Dinakarpandian et al.; licensee BioMed Central Ltd.


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