Inorganic and Physical Chemistry Laboratory, CSIR-Central Leather Research Institute, Adyar, Chennai 600020, India.
Inorganic and Physical Chemistry Laboratory, CSIR-Central Leather Research Institute, Adyar, Chennai 600020, India.
Int J Biol Macromol. 2017 Aug;101:179-186. doi: 10.1016/j.ijbiomac.2017.03.050. Epub 2017 Mar 12.
Collagen fibrils accumulate in excessive amounts and impair the normal functioning of the organ; therefore it stimulates the interest for identifying the compounds that could prevent the formation of fibrils. Herein, inhibition of self-assembly of collagen using oleuropein has been studied. The changes in the physico-chemical characteristics of collagen on interaction with increasing concentration of oleuropein has been studied using techniques like viscosity, UV-vis, CD and FT-IR. The inhibitory effect of oleuropein on fibril formation of collagen was proved using SEM. Circular dichroism and FT-IR spectra elucidates the alterations in the secondary structure of collagen suggesting non-covalent interactions between oleuropein and collagen. The decreased rate of collagen fibril formation also confirms the inhibition in the self-assembly of collagen. Hence, our study suggests that inhibition of the self-assembly process using oleuropein may unfold new avenues to treat fibrotic diseases.
胶原纤维过度积累,损害器官的正常功能;因此,人们对寻找能阻止纤维形成的化合物产生了浓厚的兴趣。本文研究了橄榄苦苷对胶原自组装的抑制作用。采用粘度、紫外-可见、圆二色和傅里叶变换红外等技术研究了胶原与橄榄苦苷浓度增加时相互作用时物理化学特性的变化。用 SEM 证明了橄榄苦苷对胶原纤维形成的抑制作用。圆二色和傅里叶变换红外光谱阐明了胶原二级结构的变化,表明橄榄苦苷与胶原之间存在非共价相互作用。胶原纤维形成速度的降低也证实了对胶原自组装的抑制。因此,我们的研究表明,使用橄榄苦苷抑制自组装过程可能为治疗纤维化疾病开辟新途径。