Fe(Iii)-binding Collagen Mimetics.
From: Department of Chemistry and Biochemistry, University of California-San Diego, La Jolla, California 92093, USA. gkinberger@isisph.com
Inorganic chemistry
- Publish Date: Feb 2006
- ISSN: 0020-1669
- Volume: 45
- Issue: 3
- Pages: 961-3
- Medium: Print
- Language: English
- Citation (JAMA): Kinberger Garth A, Taulane Joseph P, Goodman Murray, et al. Fe(Iii)-binding Collagen Mimetics.. Feb 2006;45:961-3
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.
Mesh Headings (Keywords): Binding Sites, Collagen, Hydroxamic Acids, Iron, Methylamines, Molecular Structure, Structure-Activity Relationship, Temperature
Check for Full Text / PubMed Unique Identifier (PMID): 16441100
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