Comparison of Binding Interactions of Lomefloxacin to Serum Albumin and Serum Transferrin by Resonance Light Scattering and Fluorescence Quenching Methods
作者： H. Vahedian-Movahed , M. R. Saberi , J. Chamani
DOI: 10.1080/07391102.2011.10508590
关键词:
摘要: Abstract The interaction between lomefloxacin (LMF) and two drug carrier proteins, human serum albumin (HSA) transferrin (TF), were studied compared by fluorescence quenching, resonance light scattering (RLS), circular dichroism (CD) spectroscopic along with molecular modeling. Fluorescence data show that LMF has a stronger quenching effect on HSA than TF. binding constant the number of sites calculated as 6.00 × 105 M−1 0.77 for HSA, 4.66 1.02, TF, respectively. Also, these parameters RLS data, novel approach to obtained from fluorescence. micro-environment changes Trp residues evident in both proteins. quantitative analysis secondary structure proteins further confirmed drug-induced conformational changes. distance (r) donors (HSA TF) acceptor energy transfer (FRET) theory found ...
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