Enhanced Triple Helix Stability of Collagen Peptides with 4R-Aminoprolyl (Amp) Residues:  Relative Roles of Electrostatic and Hydrogen Bonding Effects

2001 ◽  
Vol 123 (9) ◽  
pp. 2079-2080 ◽  
Author(s):  
I. Ramesh Babu ◽  
Krishna N. Ganesh
Keyword(s):  
Hydrogen Bonding ◽  
Triple Helix ◽  
Collagen Peptides ◽  
Helix Stability

Incorporation of ‘click’ chemistry glycomimetics dramatically alters triple-helix stability in an adiponectin model peptide

2017 ◽  
Vol 15 (26) ◽  
pp. 5602-5608 ◽  
Author(s):  
Katherine R. Lutteroth ◽  
Paul W. R. Harris ◽  
Tom H. Wright ◽  
Harveen Kaur ◽  
Kevin Sparrow ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Click Chemistry ◽  
Triple Helix ◽  
Model Peptide ◽  
Helix Stability

A striking decrease in thermal stability was observed upon incorporation of triazole-linked galactosylated-lysine into an adiponectin model peptide, suggesting possible applications of ‘click’ glycomimetics in bioengineering.

Electrostatic Interactions Involving Lysine Make Major Contributions to Collagen Triple-Helix Stability†

Biochemistry ◽  
2005 ◽  
Vol 44 (5) ◽  
pp. 1414-1422 ◽  
Author(s):  
Anton V. Persikov ◽  
John A. M. Ramshaw ◽  
Alan Kirkpatrick ◽  
Barbara Brodsky
Keyword(s):  
Electrostatic Interactions ◽  
Triple Helix ◽  
Collagen Triple Helix ◽  
Helix Stability

scholarly journals Contrasting Local and Macroscopic Effects of Collagen Hydroxylation

2021 ◽  
Vol 22 (16) ◽  
pp. 9068
Author(s):  
Sameer Varma ◽  
Joseph P. R. O. Orgel ◽  
Jay D. Schieber
Keyword(s):  
Molecular Dynamics ◽  
Hydrogen Bonding ◽  
Local Structure ◽  
Triple Helix ◽  
Type I Collagen ◽  
Chemical Change ◽  
Fibrillar Structure ◽  
Minor Effect ◽  
Type I ◽  
Macroscopic Properties

Collagen is heavily hydroxylated. Experiments show that proline hydroxylation is important to triple helix (monomer) stability, fibril assembly, and interaction of fibrils with other molecules. Nevertheless, experiments also show that even without hydroxylation, type I collagen does assemble into its native D-banded fibrillar structure. This raises two questions. Firstly, even though hydroxylation removal marginally affects macroscopic structure, how does such an extensive chemical change, which is expected to substantially reduce hydrogen bonding capacity, affect local structure? Secondly, how does such a chemical perturbation, which is expected to substantially decrease electrostatic attraction between monomers, affect collagen’s mechanical properties? To address these issues, we conduct a benchmarked molecular dynamics study of rat type I fibrils in the presence and absence of hydroxylation. Our simulations reproduce the experimental observation that hydroxylation removal has a minimal effect on collagen’s D-band length. We also find that the gap-overlap ratio, monomer width and monomer length are minimally affected. Surprisingly, we find that de-hydroxylation also has a minor effect on the fibril’s Young’s modulus, and elastic stress build up is also accompanied by tightening of triple-helix windings. In terms of local structure, de-hydroxylation does result in a substantial drop (23%) in inter-monomer hydrogen bonding. However, at the same time, the local structures and inter-monomer hydrogen bonding networks of non-hydroxylated amino acids are also affected. It seems that it is this intrinsic plasticity in inter-monomer interactions that preclude fibrils from undergoing any large changes in macroscopic properties. Nevertheless, changes in local structure can be expected to directly impact collagen’s interaction with extra-cellular matrix proteins. In general, this study highlights a key challenge in tissue engineering and medicine related to mapping collagen chemistry to macroscopic properties but suggests a path forward to address it using molecular dynamics simulations.

Contributions of cation–π interactions to the collagen triple helix stability

2011 ◽  
Vol 508 (1) ◽  
pp. 46-53 ◽  
Author(s):  
Chia-Ching Chen ◽  
Wei Hsu ◽  
Kuo-Chu Hwang ◽  
Jih Ru Hwu ◽  
Chun-Cheng Lin ◽  
...  
Keyword(s):  
Triple Helix ◽  
Π Interactions ◽  
Collagen Triple Helix ◽  
Helix Stability
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