Inorganic and Physical Chemistry Laboratory, CSIR-Central Leather Research Institute, Adyar, Chennai-20, India.
Inorganic and Physical Chemistry Laboratory, CSIR-Central Leather Research Institute, Adyar, Chennai-20, India.
Spectrochim Acta A Mol Biomol Spectrosc. 2019 Apr 5;212:343-348. doi: 10.1016/j.saa.2019.01.029. Epub 2019 Jan 16.
In protein-ionic liquids (ILs) interactions, anions play an important role. In this work, imidazolium-based ILs (IILs) with varying anions namely dicyanamide (DCA), hydrogen sulfate (HS), dimethyl phosphate (DP), acetate (A), sulfate (S) and dihydrogen phosphate (DHP) have been chosen with the aim of understanding the role of anions in bringing about the destabilization effect on collagen based on the kosmotropicity and chaotropicity of ions. Imidazolium-based ILs destabilized the triple helical structure of collagen, thereby proving as strong denaturants for collagen and this was confirmed by various spectroscopic techniques viz., CD, FT-IR, viscosity and impedance measurements. The solution studies were in accordance to the changes in the dimensional stability of RTT collagen fibres at the fibrillar level. Imidazolium cations with varied anions have exhibited destabilizing effect on collagen in order of ions in Hofmeister series; IDP < IDHP < IA < IDCA < IS < IHS. Presumably, these notable effect and changes were facilitated by electrostatic interactions between the anions and amine functional groups of collagen.
在蛋白质离子液体（ILs）相互作用中，阴离子起着重要作用。在这项工作中，选择了具有不同阴离子的基于咪唑的 ILs（IILs），即双氰胺（DCA）、硫酸氢根（HS）、磷酸二甲酯（DP）、乙酸根（A）、硫酸根（S）和磷酸二氢根（DHP），目的是了解阴离子在根据离子的亲溶和疏溶性质对胶原蛋白产生失稳效应中的作用。基于咪唑的 ILs 使胶原蛋白的三螺旋结构失稳，从而证明其对胶原蛋白是强变性剂，这通过各种光谱技术得到证实，如 CD、FT-IR、粘度和阻抗测量。溶液研究符合 RTT 胶原蛋白纤维在原纤维水平上的尺寸稳定性变化。具有不同阴离子的咪唑阳离子对胶原蛋白表现出失稳效应，按 Hofmeister 序列中的离子顺序为：IDP < IDHP < IA < IDCA < IS < IHS。推测这些显著的影响和变化是由阴离子和胶原蛋白的胺官能团之间的静电相互作用促成的。
