Insights into the interaction between the kusaginin and bovine serum albumin: Multi‐spectroscopic techniques and computational approaches

Abstract

Kusaginin, as a phenylethanoid glycoside, which has exhibited wide antioxidant and antimicrobial properties. The molecular mechanism underlying the broad biological activities of kusaginin has not yet been well documented. In this paper, the interaction of kusaginin with bovine serum albumin (BSA) has been explored by fluorescence spectra, UV‐vis absorption spectra, and circular dichroism (CD) spectra along with computational approaches. The fluorescence experiments showed that kusaginin could strongly quench the intrinsic fluorescence of BSA through both dynamic and static quenching mechanisms. The thermodynamic analysis suggested that hydrophobic force was the main force in stabilizing the BSA‐kusaginin complex. In addition, conformation changes of BSA were observed from three‐dimensional and synchronous fluorescence spectra, UV spectra, and CD spectra under experimental conditions. All these experimental results have been complemented and validated by the molecular docking and dynamic simulation studies, which revealed that kusaginin was bound on the hydrophobic cavity in subdomain IIA of BSA and formed a stable BSA‐kusaginin complex. Finally, density functional theory (DFT) calculation further implied that hydrogen bonds also support stabilizing the BSA‐kusaginin complex. This research may aid in understanding the pharmacological characteristics of kusaginin and provide a vital reference modeling for the design of analogues drugs.

Exploring the interaction of a potent anti‐cancer drug Selumetinib with bovine serum albumin: Spectral and computational attributes

“…Therefore, some involvement of ground state complex formation (static mechanism) can also be assumed in the quenching process. Hence, there arises a possibility of involvement of mixed quenching phenomena 34–36 . Thus, we have employed the modified Stern–Volmer equation (equations S1, S2, S3) for mixed quenching and observed that at all five temperatures (298, 303, 308, 313 and 318 K) the plots (Figure S3) result in the slope (K D .K S ) as 7.053, 12.759, 18.176, 19.351 and 22.345 × 10 8 M −2 , respectively.…”

“…The interaction affected some of the inner stabilizing forces resulting in the alteration of the secondary helical structure of BSA. These changes may be due to alteration of the hydrophobic pocket caused by disruption of hydrogen bonding upon binding with hydrophobic SEL, thus there is a change in polarity of the microenvironment of the hydrophobic cavity upon binding which resulted in a significant decrease in α ‐helix content 34,61 …”

Determination of modes of interactions of lanosterol with bovine serum albumin (BSA) using different spectroscopic techniques and molecular docking

“…Estimated values of K b were in the order of 10 7 M − 1 indicating the signi cant binding between lanosterol and BSA. Values of K b were shown to increase might be due to the enhanced stability of complex with rise in temperature [31].…”

A biophysical approach to study the impact of muscle relaxant drug tizanidine on stability and activity of serum albumins

“…The transport proteins, serum albumins, HSA and BSA, are also explored for their interactions with drugs and other molecules. Huang et al carried out BSA interaction studies with a glycoside kusaginin 21 . Similarly, Zhu et al, ascertained interaction mechanism as well as the conformational changes in the serum albumins on binding with the drugs artemisinin and dihydroartemisinin 22 .…”

“…Huang et al carried out BSA interaction studies with a glycoside kusaginin. 21 Similarly, Zhu et al, ascertained interaction mechanism as well as the conformational changes in the serum albumins on binding with the drugs artemisinin and dihydroartemisinin. 22 Khan et al studied the binding mechanism between BSA and topiramate.…”