Fe(III)-binding collagen mimetics.
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.
Kinberger
Garth A
GA
Department of Chemistry and Biochemistry, University of California-San Diego, La Jolla, California 92093, USA. gkinberger@isisph.com
Taulane
Joseph P
JP
Goodman
Murray
M
D001665:Binding Sites; D003094:Collagen / Q000138:chemical synthesis* / Q000737:chemistry*; D006877:Hydroxamic Acids / Q000737:chemistry; D007501:Iron / Q000737:chemistry*; D008744:Methylamines / Q000737:chemistry*; D015394:Molecular Structure; D013329:Structure-Activity Relationship; D013696:Temperature
D006877:Hydroxamic Acids; D008744:Methylamines; C516275:tris(carboxyethoxymethyl)aminomethane; D003094:Collagen; D007501:Iron