Multi-spectroscopic approaches and molecular simulation research of the intermolecular interaction between the angiotensin-converting enzyme inhibitor (ACE inhibitor) benazepril and bovine serum albumin (BSA)

Wang, Baoli; Pan, Dong-Qi; Zhou, Kai; Lou, Yan‐Yue; Shi, Jie‐Hua

doi:10.1016/j.saa.2018.12.040

Cited by 172 publications

(46 citation statements)

References 36 publications

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“…From Table 1, it can be found that the K SV increased with increasing temperature, suggesting that the quenching process is initiated by dynamic quenching. What's more, we observed that the values for k q are greater than the maximum diffusion collision quenching rate constant (2.0 Â 10 10 M À1 s À1 ), 7,36 indicating that the static quenching effect may exist in the system of Yb-complex and DNA. That is to say, the quenching mechanism of Yb-complex by FS-DNA is initiated by a combined quenching process (including dynamic and static quenching).…”

Section: The F-f Transition Of Ytterbium Complexmentioning

confidence: 74%

“…That is to say, the quenching mechanism of Yb-complex by FS-DNA is initiated by a combined quenching process (including dynamic and static quenching). K b and the number of binding sites (n) for interaction DNA with the Yb-complex were analysed by eqn (6) using the data obtained from uorescence titration: The binding constant (K b ), the number of the binding sites (n), the biomolecular quenching rate constant k q , the Stern-Volmer constant (K SV ), and thermodynamic parameters (DS , DH , and DG ) for the interaction of DNA with ytterbium complex at various temperatures (7) and (8)) by the plotting of ln K b against 1/ T (Fig. 2(C…”

Section: The F-f Transition Of Ytterbium Complexmentioning

confidence: 99%

“…Their three-dimensional structure is like the shape of the heart and consists of three homologous domains and each domain comprises two subdomains (A and B). 7,8 In this context, binding toward serum proteins that may perform a transport function for metal complexes appears to be the most important issue because such interactions determine also the overall drug distribution and excretion and differences in efficacy, activity, and toxicity. [8][9][10][11] The coordination chemistry of lanthanides (Ln) has disclosed considerable development in several decades because of its various applications.…”

Section: Introductionmentioning

confidence: 99%

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Parent and nano-encapsulated ytterbium(iii) complex toward binding with biological macromolecules, in vitro cytotoxicity, cleavage and antimicrobial activity studies

et al. 2020

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Section: The F-f Transition Of Ytterbium Complexmentioning

confidence: 74%

Section: The F-f Transition Of Ytterbium Complexmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Parent and nano-encapsulated ytterbium(iii) complex toward binding with biological macromolecules, in vitro cytotoxicity, cleavage and antimicrobial activity studies

et al. 2020

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“…The quenching process has been divided into three types: (i) dynamic quenching, (ii) static quenching, and (iii) combined quenching. [ 36–39 ] Dynamic quenching occurs due to the collision between fluorophore and quencher molecule, while in static quenching a ground‐state complex is formed between fluorophore and quencher. The third type arises as a result of both static and dynamic quenching.…”

Section: Resultsmentioning

confidence: 99%

Effect of quercetin on the amiloride–bovine serum albumin interaction using spectroscopic methods, molecular docking and chemometric approaches

et al. 2020

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The effect of quercetin flavonoid (QUE), on the binding interaction of antihypertensive drug, amiloride (AMI) with bovine serum albumin (BSA) was investigated in this study. Spectroscopic methods such as steady‐state, synchronous, three‐dimensional fluorescence, and circular dichroism spectroscopy were employed to study the interaction. Fluorescence data were analyzed using the Stern–Volmer equation and a static quenching process was found to be involved in the formation of AMI–BSA and QUE–BSA complexes and were in good agreement with the thermodynamic study. The thermodynamic parameters illustrated that the process is spontaneous and enthalpy driven. Hydrophobicity is acting as the primary force in the binding interaction. Fluorescence spectral data were resolved using a multivariate curve resolution‐alternating least squares method (MCR–ALS). Site marker and molecular docking studies confirmed the binding site of AMI on BSA, i.e. site II. The binding distance between amino acid of BSA and AMI was calculated and found to be 2.18 nm which indicated that energy transfer has occurred from an amino acid of BSA to AMI. The binding affinity of AMI to BSA was found to be reduced in the presence of QUE, which may lead to the poor distribution of AMI at the desired site.

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“…Angiotensin converting enzyme (ACE) inhibitors play a key role in the regulation of peripheral blood pressure, mainly through the renin-angiotensin and kallikrain-kin in systems 1 . ACE has been considered as a target in the prevention and treatment of hypertensive diseases 2 .…”

Section: Introductionmentioning

confidence: 99%

QSAR studies of angiotensin converting enzyme inhibitors using CoMFA, CoMSIA and molecular docking

Tong

Tian-Hao

Feng

et al. 2021

JSCS

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In order to better understand the biochemical interactions governing their activities in lowering blood pressure, multiple quantitative structure-activity relationship (QSAR) models were developed from a data set of 58 angiotensin converting enzyme (ACE) inhibitors. The models were built by using comparative molecular field analysis (CoMFA) and comparative molecular similarity indices analysis (CoMSIA) techniques. The best CoMFA model had a cross-validation q2 value of 0.940, a non cross-validation r2 value of 0.952 and an external validation statistic Qext2 value of 0.920. For the best CoMSIA model the values were with q2 = 0.872, r2 = 0.926 and Qext2 = 0.868. Based on the contour maps, eight new ACE inhibitors were designed. Molecular docking was employed to further explore the binding requirements between the ligands and the receptor protein which included several hydrogen bonds between the ACE inhibitors and active site residues. This study showed extensive interactions between ACE inhibitors and residues of HIS383, GLU384, HIS513, TYR520 and LYS511 in the active site of ACE. The design of potent new inhibitors of ACE can get useful insights from these results.

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Multi-spectroscopic approaches and molecular simulation research of the intermolecular interaction between the angiotensin-converting enzyme inhibitor (ACE inhibitor) benazepril and bovine serum albumin (BSA)

Cited by 172 publications

References 36 publications

Parent and nano-encapsulated ytterbium(iii) complex toward binding with biological macromolecules, in vitro cytotoxicity, cleavage and antimicrobial activity studies

Parent and nano-encapsulated ytterbium(iii) complex toward binding with biological macromolecules, in vitro cytotoxicity, cleavage and antimicrobial activity studies

Effect of quercetin on the amiloride–bovine serum albumin interaction using spectroscopic methods, molecular docking and chemometric approaches

QSAR studies of angiotensin converting enzyme inhibitors using CoMFA, CoMSIA and molecular docking

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