丙二醛
氧化磷酸化
化学
氧化损伤
氧化应激
生物化学
作者
Vendula Paculová,Ankush Prasad,Michaela Sedlářová,Pavel Pospı́šil
标识
DOI:10.1016/j.abb.2023.109850
摘要
Human skin is exposed to various physical and chemical stress factors, which commonly cause the oxidation of lipids and proteins. In this study, azo initiator AAPH [2,2′ -azobis(2-methylpropionamidine) dihydrochloride] was employed to initiate lipid peroxidation in porcine skin as an ex vivo model for human skin. We demonstrate that malondialdehyde (MDA), a secondary product of lipid peroxidation, is covalently bound to collagen in the dermis, forming MDA-collagen adducts. The binding of MDA to collagen results in an unfolding of the collagen triple helix, formation of the dimer of α-chains of collagen, and fragmentation of the collagen α-chain. It is proposed here that the MDA is bound to the lysine residues of α-chain collagen, which are involved in electrostatic interaction and hydrogen bonding with the glutamate and aspartate of other α-chains of the triple helix. Our data provide crucial information about the MDA binding topology in the skin, which is necessary to understand better the various types of skin-related diseases and the aging process in the skin under stress.
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