STABILIZATION OF THE COLLAGEN TRIPLE HELIX WITH A RUTHENIUM(II) ANCHOR
Author
Banzon, Patrick D.
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.
Date
2017-05-04
Citation:
APA:
Banzon, Patrick D..
(May 2017).
STABILIZATION OF THE COLLAGEN TRIPLE HELIX WITH A RUTHENIUM(II) ANCHOR
(Honors Thesis, East Carolina University). Retrieved from the Scholarship.
(http://hdl.handle.net/10342/6253.)
MLA:
Banzon, Patrick D..
STABILIZATION OF THE COLLAGEN TRIPLE HELIX WITH A RUTHENIUM(II) ANCHOR.
Honors Thesis. East Carolina University,
May 2017. The Scholarship.
http://hdl.handle.net/10342/6253.
March 29, 2024.
Chicago:
Banzon, Patrick D.,
“STABILIZATION OF THE COLLAGEN TRIPLE HELIX WITH A RUTHENIUM(II) ANCHOR”
(Honors Thesis., East Carolina University,
May 2017).
AMA:
Banzon, Patrick D..
STABILIZATION OF THE COLLAGEN TRIPLE HELIX WITH A RUTHENIUM(II) ANCHOR
[Honors Thesis]. Greenville, NC: East Carolina University;
May 2017.
Collections
Publisher
East Carolina University