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Choline-Based Amino Acid ILs–Collagen Interaction: Enunciating Its Role in Stabilization/Destabilization Phenomena

Given the potential of productive interaction between choline-based amino acid ionic liquids (CAAILs) and collagen, we investigated the role of four CAAILs, viz., choline serinate, threoninate, lysinate, and phenylalaninate, and the changes mediated by them in the structure of collagen at different hierarchical orderings, that is, at molecular and fibrillar levels. The rheological, dielectric behavior and the secondary structural changes signify the alteration in the triple helical structure of collagen at higher concentrations of CAAILs. A marginal swelling and slight decrease in the thermal stability of rat tail tendon collagen fibers were observed for choline serinate and threoninate, albeit distortions in banding patterns were noticed for choline lysinate and phenylalaninate, suggesting chaotropicity of the ions at the fibrillar level. This signifies the changes in the hydrogen-bonding environment of collagen with increasing concentrations of CAAILs, which could be due to competitive hydrogen bonding ...

Authors:   Aafiya Tarannum; J. Raghava Rao; N. Nishad Fathima
Journal:   Journal of Physical Chemistry B
Year:   2018
DOI:   10.1021/acs.jpcb.7b10645
Publication date:   10-Jan-2018
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