Unveiling the interaction mechanism of alogliptin benzoate with human serum albumin: Insights from spectroscopy, microcalorimetry, and molecular docking and molecular dynamics analyses

Zhang, Shuangshuang; Gan, Ruixue; Zhao, Ludan; Sun, Qiaomei; Xiang, Hongzhao; Xiang, Xi; Zhao, Gang; Li, Hui

doi:10.1016/j.saa.2020.119040

Cited by 23 publications

(6 citation statements)

References 33 publications

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“…RMSD is an important indicator for determining whether a system has reached equilibrium, particularly when monitoring displacements of molecular backbone atoms [ 68 ]. A larger and more volatile RMSD indicates intense motion.…”

Section: Resultsmentioning

confidence: 99%

Binding Affinity and Mechanism of Six PFAS with Human Serum Albumin: Insights from Multi-Spectroscopy, DFT and Molecular Dynamics Approaches

Peng,

Xu,

et al. 2024

Toxics

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Per- and Polyfluoroalkyl Substances (PFAS) bioaccumulate in the human body, presenting potential health risks and cellular toxicity. Their transport mechanisms and interactions with tissues and the circulatory system require further investigation. This study investigates the interaction mechanisms of six PFAS with Human Serum Albumin (HSA) using multi-spectroscopy, DFT and a molecular dynamics approach. Multi-spectral analysis shows that perfluorononanoic acid (PFNA) has the best binding capabilities with HSA. The order of binding constants (298 K) is as follows: “Perfluorononanoic Acid (PFNA, 7.81 × 106 L·mol−1) > Perfluoro-2,5-dimethyl-3,6-dioxanonanoic Acid (HFPO-TA, 3.70 × 106 L·mol−1) > Perfluorooctanoic Acid (PFOA, 2.27 × 105 L·mol−1) > Perfluoro-3,6,9-trioxadecanoic Acid (PFO3DA, 1.59 × 105 L·mol−1) > Perfluoroheptanoic Acid (PFHpA, 4.53 × 103 L·mol−1) > Dodecafluorosuberic Acid (DFSA, 1.52 × 103 L·mol−1)”. Thermodynamic analysis suggests that PFNA and PFO3DA’s interactions with HSA are exothermic, driven primarily by hydrogen bonds or van der Waals interactions. PFHpA, DFSA, PFOA, and HFPO-TA’s interactions with HSA, on the other hand, are endothermic processes primarily driven by hydrophobic interactions. Competitive probe results show that the main HSA–PFAS binding site is in the HSA structure’s subdomain IIA. These findings are also consistent with the findings of molecular docking. Molecular dynamics simulation (MD) analysis further shows that the lowest binding energy (−38.83 kcal/mol) is fund in the HSA–PFNA complex, indicating that PFNA binds more readily with HSA. Energy decomposition analysis also indicates that van der Waals and electrostatic interactions are the main forces for the HSA–PFAS complexes. Correlation analysis reveals that DFT quantum chemical descriptors related to electrostatic distribution and characteristics like ESP and ALIE are more representative in characterizing HSA–PFAS binding. This study sheds light on the interactions between HSA and PFAS. It guides health risk assessments and control strategies against PFAS, serving as a critical starting point for further public health research.

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Section: Resultsmentioning

confidence: 99%

Binding Affinity and Mechanism of Six PFAS with Human Serum Albumin: Insights from Multi-Spectroscopy, DFT and Molecular Dynamics Approaches

Peng,

Xu,

et al. 2024

Toxics

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“…Molecular fluorescence spectroscopy is an effective technique to establish conformational modifications and protein interactions in solution because of its good selectivity and high sensitivity. Tryptophan (Trp), tyrosine (Tyr), and phenylalanine (Phe) are the fundamental fluorophores existing in any protein [ 28 , 29 ]. Steady-state fluorescence spectroscopy analysis showed that the emission spectra of rhBMP-2 at different formulation pH showed a well-defined peak centered at 340 nm corresponding to Trp emission, which exhibited no obvious difference among the experimental groups ( Fig.…”

Section: Resultsmentioning

confidence: 99%

Regulating the bioactivity of non-glycosylated recombinant human bone morphogenetic protein-2 to enhance bone regeneration

Yu,

Chen,

Chen

et al. 2024

Bioactive Materials

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“…To further study the quenching mechanism of CQ and HCQ to the emission of serum proteins, we studied the influence of two drugs on the fluorescence lifetime of SA. Normally, the fluorescence lifetime of fluorophores during dynamic quenching will decrease with the addition of quenching agent, while in the static quenching process, it is not affected by the quenching agent [ 28 ]. The fluorescence lifetime was calculated with Eq.…”

Section: Resultsmentioning

confidence: 99%

“…Binding forces between drugs and biomacromolecules are divided into four main types: hydrogen bonding, electrostatic forces, hydrophobic forces and van der waals forces [ 28 ]. Based on the classical Ross theory, the ∆H and ∆S of the interactions between two drugs and SA were all less than zero, indicating that hydrogen bonding and van der Waals forces were the major forces of interaction [ 41 ].…”

Section: Resultsmentioning

confidence: 99%

Affinity binding of COVID-19 drug candidates (chloroquine/hydroxychloroquine) and serum albumin: Based on photochemistry and molecular docking

Yuan

Wen

et al. 2023

Journal of Photochemistry and Photobiology B: Biology

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Unveiling the interaction mechanism of alogliptin benzoate with human serum albumin: Insights from spectroscopy, microcalorimetry, and molecular docking and molecular dynamics analyses

Cited by 23 publications

References 33 publications

Binding Affinity and Mechanism of Six PFAS with Human Serum Albumin: Insights from Multi-Spectroscopy, DFT and Molecular Dynamics Approaches

Binding Affinity and Mechanism of Six PFAS with Human Serum Albumin: Insights from Multi-Spectroscopy, DFT and Molecular Dynamics Approaches

Regulating the bioactivity of non-glycosylated recombinant human bone morphogenetic protein-2 to enhance bone regeneration

Affinity binding of COVID-19 drug candidates (chloroquine/hydroxychloroquine) and serum albumin: Based on photochemistry and molecular docking

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