期刊
BIOCHEMISTRY
卷 55, 期 34, 页码 4777-4786出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.biochem.6b00420
关键词
-
资金
- Consejo Nacional de Investigaciones Cientificas y Tecnicas (CONICET) [PIP 0304]
- Agencia de Promocion Cientifica y Tecnologica (ANPCyT) [PICT 2012-0508]
- Universidad Nacional de La Plata (UNLP) [X586, X712]
- CONICET
Human serum albumin (HSA) is the most abundant protein in the circulatory system. Oxidized albumin was identified'in the skin of patients suffering from vitiligo, a depigmentation disorder in which the protection against ultraviolet (UV) radiation fails because of the lack of melanin. Oxidized pterins, efficient photosensitizers under UV-A irradiation, accumulate in the skin affected by vitiligo. In this work, we have investigated the ability of pterin (Ptr), the parent compound of oxidized pterins, to induce structural and chemical changes in HSA under UV-A irradiation. Our results showed that Ptr is able to photoinduce oxidation of the protein in at least two amino acid residues: tryptophan (Trp) and tyrosine (Tyr). HSA undergoes oligomerization, yielding protein structures whose molecular weight increases with irradiation time. The protein cross-linking, due to the formation of dimers of Tyr, does not significantly affect the secondary and tertiary structures of HSA. Trp is consumed-in the photosensitized process, and N-formylkynurenine was identified as,one of its oxidation products. The photosensitization of HSA takes place via a purely dynamic process, which involves the triplet excited state of Ptr. The results presented in this work suggest that protein photodamage mediated by endogenous,photosensitizers can significantly contribute to the harmful effects of UV-A radiation on the human skin.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据