2009
DOI: 10.1016/j.ijbiomac.2009.06.003
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Effect of surfactants on the thermal, conformational and rheological properties of collagen

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Cited by 30 publications
(19 citation statements)
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“…4). However, because the conformational difference is small (as previously reported [22]), it is at best attributable to a different helix pitch, with the overall collagen helix conformation maintained. Nevertheless, the rheology related to these two conformations [23] is different, as seen from the D curves in the QCM-D results for each pH (Figs.…”
Section: A Plausible Attribution Of Two Species With the Aid Of CDmentioning
confidence: 52%
“…4). However, because the conformational difference is small (as previously reported [22]), it is at best attributable to a different helix pitch, with the overall collagen helix conformation maintained. Nevertheless, the rheology related to these two conformations [23] is different, as seen from the D curves in the QCM-D results for each pH (Figs.…”
Section: A Plausible Attribution Of Two Species With the Aid Of CDmentioning
confidence: 52%
“…Surfactants are known to act as denaturants. 16 Since both crosslinking agent like curcumin and denaturants like surfactants are decreasing the surface tension of the protein, there may be two different mechanisms operating to influence the surface activity. Curcumin is likely to alter the hydration network around the protein while denaturants break the water structure.…”
Section: Surface Tension Changes In Collagen On Interaction With Curcmentioning
confidence: 99%
“…The software CD pro was applied to yield information about the changes in the secondary structure of the protein. Prior to characterization, all the samples were incubated at 25 • C for 12 h in PBS buffer (pH 7.4, 10 mM) [29].…”
Section: Circular Dichroism Spectroscopic Studiesmentioning
confidence: 99%