Science and Technology Production
Article
Authorship
Garcia, Pablo Facundo
;
Coronel, Consuelo
;
Velo, Alejandra
;
RIVA, JULIETA SOLEDAD
;
Yudi, Lidia Mabel
;
Arguello, Gerardo
Date
2020
Publishing House and Editing Place
SPRINGER
Magazine
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS,
vol. 49
(pp. 125-132)
SPRINGER
Summary
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We report a detailed investigation of the interaction of Cr(NN)3 3+ with bovine serum albumin (BSA), an important protein for the transport of drugs in blood plasma which allows us to understand further the role of Cr(NN)3 3+ as a sensitizer in photodynamic therapy (PDT). Chromium(III) complexes, Cr(5Cl-phen)3 3+, Cr(5Me-phen)3 3+ and Cr(5Ph-phen)3 3+ (where Cl = chlorine, Me = methyl and Ph = phenyl are substituents in position 5 of the phen = 1,10-phenanthroline bidentate ligand), were used f...
We report a detailed investigation of the interaction of Cr(NN)3 3+ with bovine serum albumin (BSA), an important protein for the transport of drugs in blood plasma which allows us to understand further the role of Cr(NN)3 3+ as a sensitizer in photodynamic therapy (PDT). Chromium(III) complexes, Cr(5Cl-phen)3 3+, Cr(5Me-phen)3 3+ and Cr(5Ph-phen)3 3+ (where Cl = chlorine, Me = methyl and Ph = phenyl are substituents in position 5 of the phen = 1,10-phenanthroline bidentate ligand), were used for the present study. The interactions of BSA with Cr(NN)3 3+ were assessed employing fluorescence spectroscopy and UV–Vis absorption spectroscopy; in addition electrochemical experiments carried out at a liquid/liquid interface gave insight into the relative hydrophobicities of the complexes. We found that chromium complexes bind strongly with bovine serum albumins (BSA) with intrinsic binding constants, Kb, of (3.33 ± 0.08) × 105 M?1, (5.92 ± 0.08) × 105 M?1 and (1.64 ± 0.05) × 105 M?1 at 300.3 K. Analysis of the thermodynamic parameters ?G, ?H, and ?S indicated that hydrophobic interactions played a major role in all the BSA-Cr(NN)3 3+ association processes. The binding distances and transfer efficiencies for BSA binding reactions were calculated according to the Förster theory of non-radiation energy transfer giving distance (r) of 2.63 nm, 2.94 nm and 3.00 nm for 5Clphen, 5Mephen and 5Ph phenanthroline complexes, respectively. All these experimental results indicate that Cr(NN)3 3+ binds to serum albumins, by which these proteins could act as carriers of this complex for further applications in PDT.
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Key Words
ELECTROCHEMISTRY AT LIQUID/LIQUID INTERFACESCR(III) COMPLEXESBSAASSOCIATIONPHOTODYNAMIC THERAPY
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