Interaction of singlet oxygen with bovine serum albumin and the role of the protein nano-compartmentalization
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F16%3A00471969" target="_blank" >RIV/68081707:_____/16:00471969 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1016/j.freeradbiomed.2016.02.014" target="_blank" >http://dx.doi.org/10.1016/j.freeradbiomed.2016.02.014</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.freeradbiomed.2016.02.014" target="_blank" >10.1016/j.freeradbiomed.2016.02.014</a>
Alternative languages
Result language
angličtina
Original language name
Interaction of singlet oxygen with bovine serum albumin and the role of the protein nano-compartmentalization
Original language description
Singlet molecular oxygen (O-1(2)) contributes to protein damage triggering biophysical and biochemical changes that can be related with aging and oxidative stress. Serum albumins, such as bovine serum albumin (BSA), are abundant proteins in blood plasma with different biological functions. This paper presents a kinetic and spectroscopic study of the O-1(2)-mediated oxidation of BSA using the tris(2,2'-bipyridine)ruthenium(II) cation [Ru(bpy)(3)](2+) as sensitizer. BSA quenches efficiently O-1(2) with a total (chemical + physical interaction) rate constant k(t)(BSA)=7.3(+/- 0.4) x 108 M-1 s(-1), where the chemical pathway represented 37% of the interaction. This efficient quenching by BSA indicates the participation of several reactive residues. MALDI-TOF MS analysis of intact BSA confirmed that after oxidation by O-1(2), the mass protein increased the equivalent of 13 oxygen atoms. Time-resolved emission spectra analysis of BSA established that Trp residues were oxidized to N'-formylkynurenine, being the solvent-accessible W134 preferentially oxidized by O-1(2) as compared with the buried W213. MS confirmed oxidation of at least two Tyr residues to form dihydroxyphenylalanine, with a global reactivity towards O-1(2) six-times lower than for Trp residues. Despite the lack of MS evidences, kinetic and chemical analysis also suggested that residues other than Trp and Tyr, e.g. Met, must react with O-1(2). Modeling of the 3D-structure of BSA indicated that the oxidation pattern involves a random distribution of O-1(2) into BSA; allowing also the interaction of O-1(2) with buried residues by its diffusion from the bulk solvent through interconnected internal hydrophilic and hydrophobic grooves. (C) 2016 Elsevier Inc. All rights reserved.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
BO - Biophysics
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GBP206%2F12%2FG151" target="_blank" >GBP206/12/G151: Center of novel approaches to bioanalysis and molecular diagnostics</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Free Radical Biology and Medicine
ISSN
0891-5849
e-ISSN
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Volume of the periodical
94
Issue of the periodical within the volume
MAY2016
Country of publishing house
US - UNITED STATES
Number of pages
11
Pages from-to
99-109
UT code for WoS article
000374644100010
EID of the result in the Scopus database
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