Interaction of folic acid and some matrix metalloproteinase (MMP) inhibitor folate-γ-hydroxamate derivatives with Zn(II) and human serum albumin.

@article{Enyedy2011InteractionOF,
  title={Interaction of folic acid and some matrix metalloproteinase (MMP) inhibitor folate-γ-hydroxamate derivatives with Zn(II) and human serum albumin.},
  author={{\'E}va A Enyedy and E. J. Farkas and Orsolya D{\"o}m{\"o}t{\"o}r and M. Am{\'e}lia Santos},
  journal={Journal of inorganic biochemistry},
  year={2011},
  volume={105 3},
  pages={444-53}
}
Human serum albumin binding of folic acid and its γ-hydroxamate/carboxylate derivatives was studied by ultrafiltration and spectrofluorimetry, and it was found that the ligands exhibit a moderate binding (K(D) ~2-50 μM), and the folate-γ-phenylalanine represents the highest conditional binding constant towards albumin. This feature may have importance in the serum transport processes of these ligands. Interaction of folic acid and its derivatives with Zn(II) was investigated in aqueous solution… CONTINUE READING