Underlying the Mechanism of Vancomycin and Human Serum Albumin Interaction: A Biophysical Study

Abstract

In the present study, the binding mechanism of vancomycin with human serum albumin (HSA) was determined. Upon addition of vancomycin to HSA, the fluorescence emission was quenched and the binding constant of vancomycin with HSA was found to be 6.05 × 10(3) M(-1) at 295 K, which corresponds to -2.16 × 10(4) J·mol(-1) of free energy. The conformation of HSA was altered upon binding of vancomycin with a decrease in α helix and an increase in β sheets and random coils, suggesting partial unfolding of the secondary structure. Molecular docking experiments found that vancomycin binds strongly with HSA at the hydrophobic pocket through hydrogen bonding and van der Waals interactions. An average binding distance of 4.71 nm has been determined on the basis of the Förster resonance energy theory. It was demonstrated that vancomycin binding to HSA causes protein structural changes.

Interaction rule and mechanism of perfluoroalkyl sulfonates containing different carbon chains with human serum albumin

“…48 The soware CD Pro was used to estimate the secondary structure contents of HSA via analyzing the CD spectra (Tables 1 to 3). 25 It proved that PFASs caused some alteration in the HSA secondary structure. With the addition of PFOS, the a-helix content of HSA slightly increased ($1.4%), whereas the content of b-sheet showed an opposite trend ($4.1%).…”

“…Therefore, CD spectroscopy is used to investigate the structural changes in proteins. 25,47 CD spectra performed in the presence and absence of different PFASs are shown in Fig. S5.…”

“…21,22 Therefore, HSA is usually used as a model protein for studies to investigate the interaction between the ligands and proteins. [23][24][25][26] Former studies have simultaneously evaluated the toxicity of PFOS, PFHS, and PFBS at both animal and cell level. For Xenopus embryo, the acute embryo toxicity of PFHS and PFBS was lower than that of PFOS.…”

Investigation on the Interaction of Hydroxyethyl Starch 130/0.4 (Voluven) and Serum Albumin for Pharmacokinetic and Toxicological Implications

“…It can be seen from Figure A that HSA exhibited two main amide bands around 1652 cm −1 (C=O stretch) and 1548 cm −1 (C–N stretch, N–H bending mode) related with the secondary structure of proteins. Meanwhile, Voluven exhibited two main absorption bands around 1568 cm −1 (C=O stretch) and 1390 cm −1 (C–H stretch) . In comparing with the absorption spectrum of HSA and the summed absorption spectrum between HSA and Voluven, the absorption spectrum of Voluven–HSA system exhibited a tiny wavelength blueshift (from 1652 to 1649 cm −1 ).…”

Prediction of Unbound Vancomycin Levels in Intensive Care Unit and Nonintensive Care Unit Patients: Total Bilirubin May Play an Important Role

“…Similar to previous observations, 18 , 25 significant correlations between the unbound vancomycin level and total protein level and albumin in our study population could not be demonstrated. This is puzzling since the PPB characteristics of vancomycin were also believed to be correlated predominantly with albumin, 15 , 19 , 29 total protein 14 and IgA 11 , 15 , 19 , 30 levels in previous studies. Although we included a relatively large study population, we were still unable to correlate the unbound vancomycin level and the albumin level.…”