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利用离子液体功能化氧化铈纳米粒子稳定胶原。

Collagen stabilization using ionic liquid functionalised cerium oxide nanoparticle.

机构信息

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.

出版信息

Int J Biol Macromol. 2020 Mar 15;147:24-28. doi: 10.1016/j.ijbiomac.2019.12.271. Epub 2020 Jan 3.

DOI:10.1016/j.ijbiomac.2019.12.271
PMID:31904464
Abstract

Nanoparticles owing to their size have a substantial influence on the biological behavior of collagen, thereby opening new channels to unfold the propensity of nanoparticles in terms of collagen stabilization. The present study aims to synthesize and characterize cerium oxide nanoparticles and to investigate their crosslinking efficiency on collagen. Cerium oxide nanoparticles, known biocatalysts, form an effective oxidation system due to their variable oxidation state. Ionic liquid functionalizes cerium oxide nanoparticles (IL-CONP) have been synthesis by the sonication method and characterizes using techniques such as Dynamic Light Scattering, and X-ray Diffraction. The hydrodynamic diameter, Zeta potential and polydispersity index of nanoparticles is 192.3 ± 2.14 nm, -13.76 ± 1.5 mV and 0.387, respectively. Changes in the secondary structure of collagen upon treatment with increasing concentration of IL-CONP indicate conformational modifications at the molecular level. Differential scanning calorimetry studies on rat tail tendon collagen fibers with IL-CONP indicate an increase in thermal stability of collagen from 61 to 87 °C. Thus, cerium oxide-based nanoparticle crosslinking invokes a considerable array of interest as a potential crosslinking agent for collagen.

摘要

由于纳米颗粒的尺寸,它们对胶原蛋白的生物行为有很大的影响,从而为研究纳米颗粒在胶原蛋白稳定方面的特性开辟了新的途径。本研究旨在合成和表征氧化铈纳米颗粒,并研究其对胶原蛋白的交联效率。氧化铈纳米颗粒是已知的生物催化剂,由于其可变的氧化态,形成了有效的氧化体系。通过超声法合成了离子液体功能化氧化铈纳米颗粒(IL-CONP),并通过动态光散射和 X 射线衍射等技术对其进行了表征。纳米颗粒的水动力直径、Zeta 电位和多分散指数分别为 192.3 ± 2.14nm、-13.76 ± 1.5mV 和 0.387。随着 IL-CONP 浓度的增加,胶原蛋白二级结构的变化表明在分子水平上发生了构象修饰。用 IL-CONP 对大鼠尾腱胶原纤维进行差示扫描量热法研究表明,胶原的热稳定性从 61°C 增加到 87°C。因此,基于氧化铈的纳米颗粒交联作为潜在的胶原蛋白交联剂引起了广泛的关注。

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