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.

scholarly journals The Effects of Salts on the Stability of the Collagen Helix Under Acidic Conditions

1968 ◽  
Vol 21 (4) ◽  
pp. 821 ◽  
Author(s):  
Anne FW oodlock ◽  
BS Harrap
Keyword(s):  
Thermal Stability ◽  
Carboxyl Groups ◽  
Neutral Ph ◽  
Acid Ph ◽  
Helix Stability ◽  
Acidic Conditions ◽  
Anions And Cations ◽  
The Stability ◽  
Thermal Stability Of ◽  
Positively Charged

In the acid pH region, the relative effects of various salts on the thermal stability of the collagen helix are quite different from their effects at neutral pH. The magnitude of the decrease in thermal stability brought about by the salts studied depends mainly on the nature and concentration of the anion and very little on the nature of the cation, whereas at neutral pH the nature of both anions and cations affects the collagen helix stability, the effects of the two ions being roughly additive. The magnitude of the effect of salts at acid pH is much greater than that at neutral pH whereas for a non-ionized denaturant, urea, the magnitudes at both neutral and acid pH are similar. The data are discussed in terms of possible interactions between salts and the positively charged protein with particular consideration of the effects of salts on the pKa of protein carboxyl groups.

Two States of the Triple Helix in the Thermal Transition of the Collagen Model Peptide (Pro-Pro-Gly)10

2004 ◽  
Vol 22 (1) ◽  
pp. 51-58 ◽  
Author(s):  
Tsutomu Kai ◽  
Susumu Uchiyama ◽  
Yoshinori Nishi ◽  
Yuji Kobayashi ◽  
Tetsuo Tomiyama
Keyword(s):  
Triple Helix ◽  
Thermal Transition ◽  
Model Peptide

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 Anionic surfactant sulfate dodecyl sodium (SDS)-induced thermodynamics and conformational changes of collagen by ultrasensitive microcalorimetry

2021 ◽  
Vol 3 (1) ◽  
Author(s):  
Jie Zhang ◽  
Chunhua Wang ◽  
Fengteng Zhang ◽  
Wei Lin
Keyword(s):  
Thermal Stability ◽  
Conformational Changes ◽  
Triple Helix ◽  
Striking Difference ◽  
Thermal Transition ◽  
Scanning Calorimetry ◽  
Helix Structure ◽  
Stabilizing Effect ◽  
Collagen Molecules ◽  
Thermal Stability Of

Abstract In this communication, sulfate dodecyl sodium (SDS)-induced thermodynamics and conformational changes of collagen were studied. We used ultrasensitive differential scanning calorimetry (US-DSC) to directly monitor the thermal transition of collagen in the presence of SDS. The results show that SDS affects the conformation and thermal stability of collagen very differently depending on its concentrations. At CSDS ≤ 0.05 mM, the enhanced thermal stability of collagen indicates the stabilizing effect by SDS. However, a further increase of SDS leads to the denaturation of collagen, verifying the well-known ability of SDS to unfold proteins. This striking difference in thermodynamics and conformational changes of collagen caused by SDS concentrations can be explained in terms of their interactions. With increasing SDS, the binding of SDS to collagen can be dominated by electrostatic interaction shifting to hydrophobic interaction, and the latter plays a key role in loosening and unfolding the triple-helix structure of collagen. The important finding in the present study is the stabilizing effect of SDS on collagen molecules at extreme low concentration. Graphical abstract

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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