Pipaón Sergio, Gragera Marcos, Bueno-Carrasco M Teresa, García-Bernalt Diego Juan, Cantero Miguel, Cuéllar Jorge, Fernández-Fernández María Rosario, Valpuesta José María
Centro Nacional de Biotecnología (CNB-CSIC). Darwin, 3. 28049 Madrid, Spain.
Unidad Asociada de Nanobiotecnología (IMDEA Nanociencia), 28049 Madrid, Spain.
Nanomaterials (Basel). 2021 Feb 17;11(2):503. doi: 10.3390/nano11020503.
Chaperonins are molecular chaperones found in all kingdoms of life, and as such they assist in the folding of other proteins. Structurally, chaperonins are cylinders composed of two back-to-back rings, each of which is an oligomer of ~60-kDa proteins. Chaperonins are found in two main conformations, one in which the cavity is open and ready to recognise and trap unfolded client proteins, and a "closed" form in which folding takes place. The conspicuous properties of this structure (a cylinder containing a cavity that allows confinement) and the potential to control its closure and aperture have inspired a number of nanotechnological applications that will be described in this review.
伴侣蛋白是存在于所有生命王国中的分子伴侣,因此它们协助其他蛋白质的折叠。从结构上看,伴侣蛋白是由两个背靠背的环组成的圆柱体,每个环都是由约60 kDa蛋白质组成的寡聚体。伴侣蛋白有两种主要构象,一种是空腔开放,准备识别并捕获未折叠的客户蛋白;另一种是“封闭”形式,蛋白质在其中进行折叠。这种结构的显著特性(一个包含可限制空间的空腔的圆柱体)以及控制其封闭和开口的潜力激发了许多纳米技术应用,本文将对此进行描述。