Evaluation of the binding behavior of olmutinib (HM61713) with model transport protein: Insights from spectroscopic and molecular docking studies

It is an effective strategy to avoid obesity by inhibiting the activity of lipase. In this study, the binding mechanism of lipase and Lentinus edodes mycelia polysaccharide (LMP) were explored with multi‐spectral methods, for example, three‐dimensional (3D) fluorescence, Fourier‐transformed infrared (FT‐IR), and Raman spectra. At 290 K, the binding constant was 2.44 × 105 L/mol, there was only one binding site between LMP and lipase. Static quenching was the quenching mechanism. The major forces were hydrogen bonding and van der Waals force. The binding of LMP to lipase impacted the microenvironment around tyrosine and tryptophan residues. The polarity around these residues was decreased and hydrophobicity was enhanced. This study not only revealed the binding mechanism of LMP on lipase but also provided scientific evidence for expanding the application of LMP in functional food industries.

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“…The number of binding sites ( n ) and the binding constant ( K b ) between lipase and LMP were calculated with the following equation 39 :

\lg ([], ((), F_{0} goodbreak- F) / F) goodbreak= \lg K_{b} goodbreak+ n \lg ({}, ([], D_{0}) goodbreak- \frac{n {[P]}_{0} ((), F_{0} goodbreak- F)}{F_{0}})

where [ P ] 0 denotes the total concentration of protein, [ D ] 0 denotes the total concentration of ligand.…”

Section: Resultsmentioning

confidence: 99%

Binding mechanism of lipase with Lentinus edodes mycelia polysaccharide by multi‐spectroscopic methods

Liu

Chen

et al. 2021

J of Molecular Recognition

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“…The enhanced absorption peak around 217 nm appeared after 20(R, S)-Rh1 were added. While the weak absorption band at 278 nm or so is mainly ascribed to Phe, Tyr, and Trp residues (Kou et al, 2021;Wang et al, 2019. The results suggested that the binding reaction between BSA and 20(R, S)-Rh1 may give rise to an alteration in BSA conformation and result in the formation of a non-fluorescent complex.…”

Section: Uv-vis Absorption Spectroscopy Of Bsa By 20(r S)-rh1mentioning

confidence: 91%

Complexation mechanism between 20(R, S)‐ginsenoside Rh1 and serum albumin: Multi‐spectroscopy, in vitro cytotoxicity, and in silico investigations

Zhao

Liang

Zhu

et al. 2022

Journal of Food Science

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As rare ginsenosides, 20(R, S)-ginsenoside Rh1 [20(R, S)-Rh1] are isomers and have been reported to exhibit multiple biological effects. However, the application of 20(R, S)-Rh1 is still limited due to their poor solubilities and low bioavailabilities. Here, the complexation mechanism between 20(R, S)-Rh1 and serum albumin (SA) was explored by a combination of multi-spectroscopy and in silico investigations. Results of spectra experiments showed that 20(R, S)-Rh1 could form complexes with bovine serum albumin (BSA) and quench its intrinsic fluorescence. In addition, the influence of BSA on the anti-cancer activity of 20(R, S)-Rh1 was also evaluated in A549 cells. The result of the MTT assay indicated that anti-cancer activity of 20(R, S)-Rh1 was enhanced when combined with BSA. The results of molecular docking and dynamics simulation demonstrated that the subtle structural differences of 20(R, S)-Rh1 at the 20-carbon atom may be responsible for their different binding capacities and binding stabilities with human serum albumin. The cytotoxicity assay for 20(R, S)-Rh1 alone and their complexes with BSA demonstrated the enhancement effect of BSA for inhibition of cell proliferation. In conclusion, this work provided insight into the complexation mechanism between 20(R, S)-Rh1 and SA.

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“…Using double log equation (▶ Eq. 4) and plot, the values of binding parameters including K b and n (which are the binding constant and number of binding sites, respectively) were found [31]:…”

Section: Determination Of Binding Parametersmentioning

confidence: 99%

Exploring The Interactions of a Natural Gamma-Oryzanol with Human Serum Albumin: Surface Plasmon Resonance, Fluorescence, and Molecular Modeling Studies

et al. 2021

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γ-oryzanol (ORY) is the vital bioactive compound, which is a mixture of ferulic acid ester and plant sterols. In the present work, the binding of ORY to human serum albumin (HSA) was investigated at the molecular level using fluorescence spectroscopy and surface plasmon resonance (SPR) as well as molecular modeling studies. Based on the fluorescence data analysis, ORY can form a non-fluorescent complex with HSA and induce static quenching of the emission intensity of HSA. Also, the high value of K SV (34.69 × 104 M−1) confirmed a high sensitivity of HSA toward ORY. The real-time monitoring of the binding of ORY to HSA was carried out using the SPR technique. The small K D value (1.23 × 10−6 M) calculated by SPR analysis indicated a high affinity of ORY toward HSA. The molecular modeling studies confirmed that ORY has only one binding site on HSA and binds HSA in a cavity between subdomain IIA and IIIA.

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Evaluation of the binding behavior of olmutinib (HM61713) with model transport protein: Insights from spectroscopic and molecular docking studies

Cited by 127 publications

References 47 publications

Binding mechanism of lipase with Lentinus edodes mycelia polysaccharide by multi‐spectroscopic methods

Binding mechanism of lipase with Lentinus edodes mycelia polysaccharide by multi‐spectroscopic methods

Complexation mechanism between 20(R, S)‐ginsenoside Rh1 and serum albumin: Multi‐spectroscopy, in vitro cytotoxicity, and in silico investigations

Exploring The Interactions of a Natural Gamma-Oryzanol with Human Serum Albumin: Surface Plasmon Resonance, Fluorescence, and Molecular Modeling Studies

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