Biomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, Christchurch 8140, New Zealand.
Nanoscale. 2014 Nov 7;6(21):13169-78. doi: 10.1039/c4nr04624b.
Previous work has identified crystallin proteins extracted from fish eye lenses as a cheap and readily available source for the self-assembly of amyloid nanofibrils. However, before exploring potential applications, the biophysical aspects and safety of this bionanomaterial need to be assessed so as to ensure that it can be effectively and safely used. In this study, crude crystallin amyloid fibrils are shown to be stable across a wide pH range, in a number of industrially relevant solvents, at both low and high temperatures, and in the presence of proteases. Crystallin nanofibrils were compared to well characterised insulin and whey protein fibrils using Thioflavin T assays and TEM imaging. Cell cytotoxicity assays suggest no adverse impact of both mature and fragmented crystallin fibrils on cell viability of Hec-1a endometrial cells. An IR microspectroscopy study supports long-term structural integrity of crystallin nanofibrils.
先前的工作已经确定，从鱼眼晶状体中提取的晶状体蛋白是一种廉价且易于获得的用于组装淀粉样纳米原纤维的来源。然而，在探索潜在应用之前，需要评估这种生物纳米材料的生物物理特性和安全性，以确保其能够被有效且安全地使用。在这项研究中，粗制的晶状体蛋白原纤维在很宽的 pH 值范围内、在许多工业相关的溶剂中、在低温和高温下以及在蛋白酶存在的情况下都是稳定的。利用噻唑蓝 T 检测法和 TEM 成像，将晶状体纳米原纤维与经过充分表征的胰岛素和乳清蛋白原纤维进行了比较。细胞毒性检测实验表明，成熟的和碎片化的晶状体原纤维对子宫内膜细胞 Hec-1a 的存活率没有不良影响。红外微光谱学研究支持晶状体纳米原纤维具有长期的结构完整性。
