@article{fdi:010063130,
  title = {{I}nteraction between antimalarial 2-{A}ryl-3{H}-indol-3-one derivatives and human serum albumin},
  author = {{R}akotoarivelo, {N}. {V}. and {P}erio, {P}ierre and {N}ajahi, {E}. and {N}epveu, {F}.},
  editor = {},
  language = {{ENG}},
  abstract = {{B}inding of drugs to plasma proteins, such as albumin, is a major factor which determines their pharmacokinetics and pharmacological effects. {T}herefore, the interactions between human serum albumin ({HSA}) and four antimalarial compounds selected in the 2-aryl-3{H}-indol-3-one series have been investigated using {UV}-visible, fluorescence and circular dichroism ({CD}) spectroscopies. {C}ompounds produced a static quenching of the intrinsic fluorescence of {HSA}. {T}he thermodynamic parameters have shown that the binding reaction is endothermic for three compounds while exothermic for the 2-phenyl-3{H}-indol-3-one, 3. {T}he interaction is entropically driven with predominant hydrophobic forces with binding affinities of the order of 104 {M}-1. {T}he highest binding constant is observed for 3 ({K}-lambda=280nm = 4.53 x 10(4) {M}-1) which is also the less active compound against {P}lasmodium falciparum. {S}ynchronous fluorescence gave qualitative information on the conformational changes of {HSA} while quantitative data were obtained with {CD}. {D}isplacement experiments with site markers indicated that drugs bind to {HSA} at site {I} (subdomain {IIA}). {I}n addition, the apparent binding constant and the binding site number were calculated in the presence of different ions.},
  keywords = {},
  booktitle = {},
  journal = {{J}ournal of {P}hysical {C}hemistry {B}},
  volume = {118},
  numero = {47},
  pages = {13477--13485},
  ISSN = {1520-6106},
  year = {2014},
  DOI = {10.1021/jp507569e},
  URL = {https://www.documentation.ird.fr/hor/fdi:010063130},
}