Determination of LMF binding site on a HSA-PPIX complex in the presence of human holo transferrin from the viewpoint of drug loading on proteins.

ABSTRACT: Holo transferrin (TF) and the natural complex of human serum albumin and protoporphyrin IX (HSA-PPIX) are two serum carrier proteins that can interact with each other. Such an interaction may alter their binding sites. In this study, fluorescence spectroscopy, as well as zeta potential and molecular modeling techniques, have been used to compare the complexes (HSA-PPIX)-LMF and [(HSA-PPIX)-TF]-LMF. The Ka1, Ka2, values of (HSA-PPIX)-LMF and [(HSA-PPIX)-TF]-LMF were 1.1×10(5) M(-1), 9.7×10(6) M(-1), and 2.0×10(4) M(-1), 1.8×10(5) M(-1), respectively, and the n1, n2 values were respectively 1.19, 1.53 and 1.17, 1.65. The second derivative of the Trp emission scan of (HSA-PPIX)-LMF exhibited one negative band at 310 nm, whereas for the [(HSA-PPIX)-TF]-LMF system, we observed one negative band

SUBMITTER: Sattar Z 

PROVIDER: S-EPMC3879261 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature