Interaction of kaempferol with human serum albumin: A fluorescence and circular dichroism study

Spectroscopic investigation on the food components–drug interaction: The influence of flavonoids on the affinity of nifedipine to human serum albumin

“…7. In addition, the binding distance (r) between the amino acid residue of HSA and the NDP can be calculated by the following equations (Matei and Hillebrand, 2010): …”

Studies on the antagonistic action between chloramphenicol and quinolones with presence of bovine serum albumin by fluorescence spectroscopy

“…For static quenching, the relationship between the fluorescence quenching intensity and the concentration of quenchers can be described by the equation [18][19][20][21]:…”

Structure-affinity relationship of bovine serum albumin with dietary flavonoids with different C-ring substituents in the presence of Fe3+ ion

“…The study of interaction between drugs and serum albumin is not only important to provide salient information about the nature of drugs and pharmacokinetics; it is also helpful to explain the relationship between the structures and functions of drugs. Up to now, most papers have reported the binding process between flavonoids and serum albumin (Bolli et al, 2010;Matei & Hillebrand, 2010;Shi et al, 2010;Wackerbarth, Stoll, Gebken, Pelters, & Bindrich, 2009), using parameters such as binding constant, binding affinity, binding site, binding distance, and energy transfer. Only few reports focused on the structure-affinity relationship of flavonoids bound to serum albumin.…”