Interaction of singlet oxygen with bovine serum albumin and the role of the protein nano-compartmentalization

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

Interaction of singlet oxygen with bovine serum albumin and the role of the protein nano-compartmentalization

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Interaction of singlet oxygen with bovine serum albumin and the role of the protein nano-compartmentalization

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

BO - Biofyzika

OECD FORD obor

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Projekt

<a href="/cs/project/GBP206%2F12%2FG151" target="_blank" >GBP206/12/G151: Centrum nových přístupů k bioanalýze a molekulární diagnostice</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2016

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Free Radical Biology and Medicine

ISSN

0891-5849

e-ISSN

—

Svazek periodika

94

Číslo periodika v rámci svazku

MAY2016

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

11

Strana od-do

99-109

Kód UT WoS článku

000374644100010

EID výsledku v databázi Scopus

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