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）的相互作用中，阴离子起着重要的作用。在这项工作中，已选择了具有不同阴离子的咪唑基ILs（IILs），即双氰胺（DCA），硫酸氢盐（HS），磷酸二甲酯（DP），乙酸盐（A），硫酸盐（S）和磷酸二氢盐（DHP）目的是基于离子的同质性和离液性，了解阴离子在对胶原蛋白产生去稳定作用中的作用。基于咪唑鎓的IL破坏了胶原蛋白的三螺旋结构，从而证明它是胶原蛋白的强变性剂，这已通过各种光谱技术（例如CD，FT-IR，粘度和阻抗测量）得到了证实。解决方案的研究是根据RTT胶原纤维在原纤维水平的尺寸稳定性的变化进行的。具有不同阴离子的咪唑鎓阳离子对胶原蛋白表现出去稳定作用，按霍夫迈斯特系列中的离子顺序排列。IDP <IDHP <IA <IDCA <IS <IHS。据推测，这些显着的作用和变化是由于阴离子与胶原的胺官能团之间的静电相互作用而促进的。