Probing of the binding profile of anti-hypertensive drug, captopril with bovine serum albumin: A detailed calorimetric, spectroscopic and molecular docking studies

Khatun, Samima; Riyazuddeen,

doi:10.1016/j.jct.2018.06.004

Cited by 31 publications

(8 citation statements)

References 50 publications

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“…FRET occurs due to an overlap in the emission spectrum (donor) and absorption spectrum (acceptor). e FRET e ciency is dependent on the degree of overlap and distance between the emission and absorption spectrum and is calculated as [44]…”

Section: Energy Transfermentioning

confidence: 99%

“…ϵ(λ) denotes molar absorptivity coe cient of acceptor. e value for K 2 refractive index of the medium was taken as 1.336 and ϕ D � 0.118 for BSA [43,44]. e calculated values for E, R 0 , and J(λ) are presented in Table 4.…”

Section: Energy Transfermentioning

confidence: 99%

“…Synchronous Fluorescence Studies. Synchronous fluorescence studies provide information regarding the microenvironmental changes in the amino acids responsible for fluorescence of protein [44][45][46][47]. ese studies measure the shift in the λ em, which might have occurred due to variations near the chromophores of a molecule.…”

Section: Conformational Studiesmentioning

confidence: 99%

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Evaluation of Biophysical Interaction between Newly Synthesized Pyrazoline Pyridazine Derivative and Bovine Serum Albumin by Spectroscopic and Molecular Docking Studies

Almehizia

Bakheit

Zargar

et al. 2019

Journal of Spectroscopy

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In this research, the pyrazoline pyridazine derivative 7-methyl-2-phenyl-4-(3,4,5-trimethoxyphenyl)-2H-pyrazolo[3,4-d]pyridazine (5d) was studied for its interaction with bovine serum albumin (BSA). Various spectroscopic techniques along with molecular docking analysis were utilized to understand the mechanism of interaction. The quenching of BSA fluorescence by using investigational drug 5d was the basic principle for the methodology. Spectrofluorometric methods and UV-absorption studies were conducted for exploration of the 5d and BSA binding mechanism. The fluorescence quenching mechanism involved in BSA and 5d interaction was static quenching, and a complex formation also occurred between them. Both enthalpy and entropy attained positive values suggesting involvement of hydrophobic forces in BSA and 5d interaction. The Förster distance of 2.23 nm was calculated by fluorescence resonance energy transfer (FRET). An alteration in BSA secondary structure was proven from the conformational studies of BSA-5d interaction. This binding interaction study provided a basis to comprehend the binding interaction between 5d and BSA. These results provided information about sites of BSA involved in its interaction with 5d.

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Section: Energy Transfermentioning

confidence: 99%

Section: Energy Transfermentioning

confidence: 99%

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Evaluation of Biophysical Interaction between Newly Synthesized Pyrazoline Pyridazine Derivative and Bovine Serum Albumin by Spectroscopic and Molecular Docking Studies

Almehizia

Bakheit

Zargar

et al. 2019

Journal of Spectroscopy

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“…27 In fact, the ACE inhibitor drug, captopril did bind strongly to the albumin as shown via in vivo and in silico study. 28 In this study, the ACE inhibition activity by ASP in the presence of BSA was found to be significantly reduced as much as 71.75 %.This showed that ASP could bind with the protein (albumin), causing protein precipitation, leading to its ACE inhibition activity. The ability to cause protein precipitation perhaps due to the crosslink that occurs between the phenolics in ASP with the protein.…”

Section: Discussionmentioning

confidence: 54%

Angiotensin Converting Enzyme (ACE) Inhibition Activity by Syzygium polyanthum Wight (Walp.) Leaves: Mechanism and Specificity

Ismail¹,

Anuar²,

Suffian³

et al. 2022

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Plant collection and authenticationApproximately, 3.26 kg of the plant leaves were collected from Taman Pertanian Jubli Perak, Kuantan, Pahang, Malaysia in May 2019. The plant used in this study was verified as Syzygium polyanthum (Wight) Walp by a botanist on 24th July 2019. The voucher herbarium specimen (PIIUM ABSTRACTIntroduction: One of the potential antihypertensive mechanisms include angiotensin converting enzyme (ACE) inhibition. So far, there is no in-depth study on the ACE inhibition activity of S. polyanthum, an ethnomedicinal plant used in treating hypertension. Thus, we aimed to study the ACE inhibition activity of S. polyanthum leaves by evaluating its potency, mechanism, and specificity. Methods: S. polyanthum leaves were macerated in a bath-sonicator with either water, methanol, ethyl acetate, and hexane producing aqueous (ASP), methanolic (MSP), ethyl acetate (EASP) and hexane (HSP) extracts. Each extract (100 µg/mL) were initially screened for ACE inhibition activity and then compared with standard drug, captopril (2.06 ng/mL), then the most active extract was further tested at 1 to 1000µg/ml. Inhibition mechanism was studied using zinc chloride and bovine serum albumin (BSA), while inhibition specificity was determined upon screening for α-chymotrypsin and trypsin inhibition activity. Results: ASP at 100 μg/ mL exhibited the highest inhibition activity (69.43 ± 0.60 %) compared to MSP (41.63 ± 0.15 %), EASP (9.62 ± 1.60 %), and HSP (45.40 ± 0.15 %). ASP showed dose-dependent ACE inhibition activity with IC 50 of 41 μg/mL. ASP's ACE inhibition activity was significantly reduced in the presence of BSA, but not upon the presence of zinc chloride. ASP did not significantly inhibit α-chymotrypsin and trypsin. Conclusion: This study showed that the enzyme inhibition activity by S. polyanthum leaves was specific towards ACE. The ACE inhibition possibly occurs via protein precipitation and was non-dependent to the chelation with zinc at ACE active site.

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“…11,12 The dapoxetine and ctDNA interaction was investigated with fluorescence spectroscopy, circular dichroism spectroscopy, Fourier-transform infrared spectroscopy and UV absorption spectroscopy. 13,14 The principle of fluorescence quenching of dapoxetine by ctDNA was explored for this investigation to establish the mode of binding of dapoxetine to ctDNA. The thermodynamics study at three different temperatures established the binding forces involved between them.…”

Section: Introductionmentioning

confidence: 99%

A Spectroscopic, Thermodynamic and Molecular Docking Study of the Binding Mechanism of Dapoxetine with Calf Thymus DNA

et al. 2020

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Dapoxetine is a selective serotonin reuptake inhibitor, used to treat premature ejaculation in men. Dapoxetine may interact with the DNA and hence this study investigated dapoxetine and calf thymus DNA (ctDNA) binding interaction. The interaction study of ligands to DNA is of importance in the development of molecular probes and therapeutic agents. Spectroscopic techniques including spectrofluorometry and spectrophotometry were employed to study this interaction. Fluorescence studies indicated a static quenching mechanism between dapoxetine and ctDNA. Groove binding was suggested as the mode of interaction between dapoxetine and ctDNA based on UV absorption, circular dichroism (CD) spectroscopy, iodide quenching and molecular docking studies. The studies conducted at three different temperatures 298, 303 and 310 K indicated a strong binding interaction at higher temperatures. Thermodynamic studies conducted indicated involvement of hydrophobic interaction between ctDNA and dapoxetine and were entropy-driven. Ethidium bromide probe study suggested that dapoxetine does not bind to ctDNA in an intercalative fashion. Iodide quenching studies further proved the non-intercalative binding of ctDNA with dapoxetine. Ionic strength studies conducted ruled out the electrostatic binding mechanism between ctDNA and dapoxetine. Molecular docking analysis performed for the dapoxetine with calf thymus DNA (ctDNA) interaction and confirmed minor groove binding of dapoxetine to ctDNA. The study helped to reveal the binding interaction mechanism between dapoxetine and ctDNA.

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Probing of the binding profile of anti-hypertensive drug, captopril with bovine serum albumin: A detailed calorimetric, spectroscopic and molecular docking studies

Cited by 31 publications

References 50 publications

Evaluation of Biophysical Interaction between Newly Synthesized Pyrazoline Pyridazine Derivative and Bovine Serum Albumin by Spectroscopic and Molecular Docking Studies

Evaluation of Biophysical Interaction between Newly Synthesized Pyrazoline Pyridazine Derivative and Bovine Serum Albumin by Spectroscopic and Molecular Docking Studies

Angiotensin Converting Enzyme (ACE) Inhibition Activity by Syzygium polyanthum Wight (Walp.) Leaves: Mechanism and Specificity

A Spectroscopic, Thermodynamic and Molecular Docking Study of the Binding Mechanism of Dapoxetine with Calf Thymus DNA

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