Department of Biomedical Sciences, Panum Institute, University of Copenhagen, 2200 Copenhagen, Denmark.
Departamento de Química Física, Facultad de Química y de Farmacia, Pontificia Universidad Catolica de Chile, Santiago 7820436, Chile.
Molecules. 2021 Dec 21;27(1):15. doi: 10.3390/molecules27010015.
Covalent crosslinks within or between proteins play a key role in determining the structure and function of proteins. Some of these are formed intentionally by either enzymatic or molecular reactions and are critical to normal physiological function. Others are generated as a consequence of exposure to oxidants (radicals, excited states or two-electron species) and other endogenous or external stimuli, or as a result of the actions of a number of enzymes (e.g., oxidases and peroxidases). Increasing evidence indicates that the accumulation of unwanted crosslinks, as is seen in ageing and multiple pathologies, has adverse effects on biological function. In this article, we review the spectrum of crosslinks, both reducible and non-reducible, currently known to be formed on proteins; the mechanisms of their formation; and experimental approaches to the detection, identification and characterization of these species.
蛋白质内部或之间的共价交联在决定蛋白质的结构和功能方面起着关键作用。其中一些是通过酶促或分子反应有意形成的，对于正常的生理功能至关重要。另一些则是由于暴露于氧化剂（自由基、激发态或双电子物质）和其他内源性或外源性刺激物，或者由于许多酶（如氧化酶和过氧化物酶）的作用而产生的。越来越多的证据表明，在衰老和多种病理情况下积累的不需要的交联会对生物功能产生不利影响。在本文中，我们综述了目前已知在蛋白质上形成的可还原和不可还原的交联的种类；它们形成的机制；以及检测、鉴定和表征这些物质的实验方法。
