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Chemical changes in bovine serum albumin photoinduced by pterin

Paper ID Volume ID Publish Year Pages File Format Full-Text
29863 44444 2014 7 PDF Available
Title
Chemical changes in bovine serum albumin photoinduced by pterin
Abstract

•Bovine serum albumin (BSA) is photodamaged by pterin by a purely dynamic process.•Photosensitized reactions involve tryptophan and tyrosine residues.•Pterin photoinduces cross-linking of BSA through dimerization of tyrosine residues.

The exposure to UV-A radiation of bovine serum albumin (BSA) in aerated aqueous solution in the presence of pterin (Ptr), results in chemical and conformational modifications of the protein. Ptr belongs to a family of heterocyclic compounds that are well-known type I (electron-transfer) and type II (singlet oxygen) photosensitizers. The evolution of the photosensitized processes was followed by UV/vis spectrophotometry and fluorescence spectroscopy indicating that tryptophan (Trp) and tyrosine (Tyr) residues were affected. Additionally, conformational changes were evaluated by electrophoresis (SDS-PAGE) and size exclusion chromatography coupled with dynamic light scattering detection, showing that BSA undergoes dimerization, via the formation of Tyr radicals. The degradation of Trp residues takes place faster than the oligomerization of the protein. The photosensitized process is initiated by an electron transfer from BSA to the triplet excited stated of Ptr, being a purely dynamic mechanism.

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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 141, December 2014, Pages 262–268
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
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Price was $35.95
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