Maleimido-proxyl as an EPR spin label for the evaluation of conformational changes of albumin

作者: Aleksandra Pavićević , Jinghui Luo , Ana Popović-Bijelić , Miloš Mojović

DOI: 10.1007/S00249-017-1257-Z

关键词: StereochemistryBlood proteinsElectron paramagnetic resonanceAlbuminReactive oxygen speciesSpin labelSite-directed spin labelingCysteineBovine serum albuminBiochemistryChemistry

摘要: Albumin is the most abundant plasma protein and as such has been subject of many studies using a variety techniques. One them, capable monitoring conformational changes binding capacity proteins, electron paramagnetic resonance spectroscopy (EPR) spin labeling. To date, albumin investigated number different labels, mostly spin-labeled fatty acids (SLFAs). However, can bind up to seven equivalents acids, making it difficult determine which parts molecule undergo changes. obtain information from specific site on protein, labels that free cysteine residues may be used. In this work, applicability label, 3-maleimido proxyl (5-MSL), was evaluated for bovine serum (BSA) at temperatures pH values. Also, effect ethanol, reactive oxygen species (hydrogen peroxide superoxide radical), ligands albumin, namely several drugs were evaluated. The results indicate labeling its residue (Cys-34) 5-MSL successfully used detection changes, even in case subtle alterations induced by ligand binding.

参考文章(93)
E. V. Muravskaya, A. G. Lapko, V. A. Muravskii, Modification of transport function of plasma albumin during atherosclerosis and diabetes mellitus. Bulletin of Experimental Biology and Medicine. ,vol. 135, pp. 433- 435 ,(2003) , 10.1023/A:1024903006461
Theodore Peters, Genetics: The Albumin Gene All About Albumin#R##N#Biochemistry, Genetics, and Medical Applications. pp. 133- 187 ,(1995) , 10.1016/B978-012552110-9/50006-4
JD Morrisett, HJ Pownall, AM Gotto, Bovine serum albumin. Study of the fatty acid and steroid binding sites using spin-labeled lipids. Journal of Biological Chemistry. ,vol. 250, pp. 2487- 2494 ,(1975) , 10.1016/S0021-9258(19)41627-X
Alan J. Stewart, Claudia A. Blindauer, Stephen Berezenko, Darrell Sleep, David Tooth, Peter J. Sadler, Role of Tyr84 in controlling the reactivity of Cys34 of human albumin. FEBS Journal. ,vol. 272, pp. 353- 362 ,(2005) , 10.1111/J.1742-4658.2004.04474.X
Daniel C. Carter, Joseph X. Ho, Structure of serum albumin. Advances in Protein Chemistry. ,vol. 45, pp. 153- 203 ,(1994) , 10.1016/S0065-3233(08)60640-3
C.B. Berde, B.S. Hudson, R.D. Simoni, L.A. Sklar, Human serum albumin. Spectroscopic studies of binding and proximity relationships for fatty acids and bilirubin. Journal of Biological Chemistry. ,vol. 254, pp. 391- 400 ,(1979) , 10.1016/S0021-9258(17)37930-9
Lawrence J. Berliner, Spin Labeling: Theory And Applications ,(2011)
Takamitsu Kosa, Toru Maruyama, Masaki Otagiri, Species Differences of Serum Albumins: I. Drug Binding Sites Pharmaceutical Research. ,vol. 14, pp. 1607- 1612 ,(1997) , 10.1023/A:1012138604016