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Fe(III)-binding collagen mimetics.

Garth A Kinberger·Joseph P Taulane·Murray Goodman
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Abstract

The synthesis and characterization of hydroxamic acid containing single-chain and TRIS-assembled (where TRIS is tris(carboxyethoxymethyl)aminomethane) collagen mimetics are reported. We have engineered an Fe(III)-binding domain by placing a hydroxamic acid group at the C termini of collagen mimetic chains composed of the Gly-Pro-NLeu sequence. The circular dichroism spectra and thermal denaturation studies show an enhancement in triple-helical thermal stability upon the addition of Fe(III) for the TRIS-assembled structure. No triple-helical structure was detected for the single-chain collagen mimetic. From the absorbance shown in the UV-vis spectra, we believe that the thermal stabilization of the triple helix is the direct result of a coordination complex between Fe(III) and the hydroxamate groups tethered to the C termini of the collagen mimetic peptide chains.

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Binding SitesCollagenHydroxamic AcidsIronMethylaminesMolecular StructureStructure-Activity RelationshipTemperatureJournal ArticleResearch Support, U.S. Gov't, Non-P.H.S.

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Garth A Kinberger, Joseph P Taulane, Murray Goodman. 2006-02-06. Fe(III)-binding collagen mimetics.. https://doi.org/10.1021/ic0520059

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