STABILIZATION OF THE COLLAGEN TRIPLE HELIX WITH A RUTHENIUM(II) ANCHOR

ECU Author/Contributor (non-ECU co-authors, if there are any, appear on document)

Patrick D Banzon (Creator)

Institution

East Carolina University (ECU )

Web Site: http://www.ecu.edu/lib/

Abstract: Two collagen analogues based on a (Pro-Hyp-Gly)7 core were given metal-binding ability by linking histidine to either the N- or C- termini using a six-carbon spacer. Circular dichroism studies confirmed that the isomers , dubbed HPOG and POGH , form triple-helices which cooperatively unwind at Tm = 34.8 and 35.6 °C , respectively. Three strands of the HPOG peptide were bound to a ruthenium ion , by heating in the presence of tris(pyrazol-1-yl)borato ruthenium(II) (Tp-Ru). The strands of the N-Anchored complex unwind at a temperature about 10 °C higher , but do so over a broader temperature span. Thus , immobilization of collagen on a metal ion hub appears to increase helix stability while decreasing cooperativity of folding/unfolding. DFT calculations suggest that the loss of cooperativity arises from the disruption of interstrand hydrogen bonding. Other spacer groups , or other metal ions , may be necessary to promote optimal approach of strands to each other.

Additional Information

Publication

Thesis

Language: English

Date: 2017

Keywords

Collagen, Triple-Helix, Hydrogen Bonding, Protein Synthesis, Organic Chemistry

Subjects

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