In silico and multi-spectroscopic analyses on the interaction of 5-amino-8-hydroxyquinoline and bovine serum albumin as a potential anticancer agent

Abstract5-Amino-8-hydroxyquinoline (5A8HQ), an amino derivative of 8-hydroxyquinoline, has become a potential anticancer candidate because of its promising proteasome inhibitory activity to overcome and yet synergize bortezomib for fighting cancers. Therefore, in this study, its physicochemical properties and interaction activities with serum protein have extensively been elucidated by both in vitro and in silico approaches to fulfill the pharmacokinetic and pharmacodynamic gaps. 5A8HQ exhibited the drug-likeness properties, where oral administration seems to be a route of choice owing to its high-water solubility and intestinal absorptivity. Multi-spectroscopic investigations suggested that 5A8HQ tended to associate with bovine serum albumin (BSA), a representative of serum protein, via the ground-state complexation. It apparently bound in a protein cleft between subdomains IIA and IIIA of BSA as suggested by the molecular docking and molecular dynamics simulations. The binding was mainly driven by hydrogen bonding and electrostatic interactions with a moderate binding constant at 104 M−1, conforming with the predicted free fraction in serum at 0.484. Therefore, 5A8HQ seems to display a good bioavailability in plasma to reach target sites and exerts its potent pharmacological activity. Likewise, serum albumin is a good candidate to be reservoir and transporter of 5A8HQ in the circulatory system.

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In Vitro Investigation on Behavior of Pyriproxyfen Binding onto Bovine Serum Albumin by Mean of Various Spectroscopic Methodologies and In Silico

ChemistrySelect ◽

10.1002/slct.201902688 ◽

2019 ◽

Vol 4 (40) ◽

pp. 11626-11635 ◽

Cited By ~ 1

Author(s):

Jia‐Fei Feng ◽

Meng Wu ◽

Bao‐Li Wang ◽

Song‐Bo Kou ◽

Zhen‐Yi Lin ◽

...

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

In Silico ◽

Bovine Serum ◽

In Vitro Investigation

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Synthesis, Molecular Docking, BSA, and in-vitro reactivation study of imidazopyridine oxime against paraoxon inhibited acetylcholinesterase

Medicinal Chemistry ◽

10.2174/1573406417666210208223240 ◽

2021 ◽

Vol 17 ◽

Author(s):

Ashima Thakur ◽

Jayant Patwa ◽

Abha Sharma ◽

Swaran Jeet Flora

Keyword(s):

Molecular Docking ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

In Silico ◽

Bovine Serum ◽

Enzymatic Assay ◽

Acid Dissociation ◽

Acid Dissociation Constant ◽

Spectroscopic Techniques

Aim: To synthesize and evaluate the fused heterocyclic imidazopyridine oxime as a reactivator against paraoxon inhibited acetylcholinesterase. Background: Organophosphorus compounds (OPs) include parathion, malathion, chlorpyrifos, monocrotophos, and diazinon which are commonly used in agriculture for enhancing agricultural productivity via killing crop-damaging pests. However, people may get exposed to OPs pesticides unintentionally/intentionally via ingestion, inhalation or dermal. The current treatment regimen includes reactivator such as mono or bis-pyridinium oximes along with anticholinergic and an anticonvulsant drugs are recommended for the treatment of OP poisoning. Unfortunately, the drawback of the existing reactivator is that owing to the permanent charge present on the pyridinium makes them inefficient to cross the blood-brain barrier (BBB) and reactivate OP-inhibited central nervous system (CNS) acetylcholinesterase. Therefore, there is a need of reactivator that could cross the BBB and reactivate the OP inhibited acetylcholinesterase. Objective: The objectives of the study were synthesis, molecular docking, BSA binding and in-vitro estimation of oximes of various substituted imidazo [1,2-a]pyridine against paraoxon inhibited acetylcholinesterase. Method: The reactivators were synthesized in three steps and characterized using various spectroscopic techniques. Molecular docking study was performed on 2WHP and 3ZLV PDB using Autodock tool. The acid dissociation constant (pKa) of oximes was calculated experimentally and drug-likeness properties of the oximes were calculated In silico using mole inspiration and Swiss ADME software. The binding of oximes with bovine serum albumin (BSA) was also investigated by UV-Vis spectrophotometer. The reactivation potential of the oximes was determined by in vitro enzymatic assay. Result: in-silico study inferred that synthesized molecules fulfilled the parameters that required for a successful CNS drug candidate. Further, in-vitro enzymatic assay indicated reasonable reactivation potential of the oximes against paraoxon-inhibited AChE. The binding of oximes with bovine serum albumin (BSA) revealed static quenching of intrinsic fluorescence of BSA by oxime. The binding constant value and number of binding sites were found 0.24 mol-1 and 1 respectively. Conclusion: The results of study concluded that this scaffold could be used for further designing of more efficient uncharged reactivators.

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In vitro Model for Studying Interactions between Ketorolac and Omeprazole with Bovine Serum Albumin by UV-Spectroscopic Method

Bangladesh Pharmaceutical Journal ◽

10.3329/bpj.v17i1.22323 ◽

2015 ◽

Vol 17 (1) ◽

pp. 92-98 ◽

Cited By ~ 1

Author(s):

Kanij Nahar Deepa ◽

Md Khalid Hossain ◽

Md Shah Amran ◽

Shaila Kabir

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Binding Site ◽

Bovine Serum ◽

Association Constant ◽

Spectroscopic Method ◽

Free Fraction ◽

In Vivo Model ◽

Specific Probe

The binding of Ketorolac and Omeprazole to bovine serum albumin (BSA) was studied by equilibrium dialysis method followed by UV spectroscopy. Warfarin and Diazepam were used as site-I and site-II specific probe, respectively. The binding of Ketorolac and Omeprazole was characterized by two sets of association constant: high affinity association constant (K1) with low capacity binding site (n1) and low affinity association constant (K1) with high capacity binding site (n1). In this study, n1 and n1 values were found to be 0.25 ± 0.006 and 1.8 ± 0.025 for Ketorolac and 0.22 ± 0.030 and 1.3±0.035 for Omeprazole at pH 7.4 and 37°C, respectively. At the same condition, the values of K1 and K1 for Ketorolac were found to be 0.624 ± 0.033 ?M-1 and 0.133 ± 0.023 ?M-1 and that of Omeprazole were 0.51 ± 0.001 ?M-1 and 0.28 ± 0.005 ?M-1, respectively. Site specific probe displacement studies implied that both Ketorolac and Omeprazole bind predominantly to site-II, the Diazepam site. In the present study, both Ketorolac and Omeprazole increased the free fraction of each other when they simultaneously bound to BSA. They compete for a common binding site on the albumin molecule, thereby free fraction of both the drugs was increased as compared to the level obtained when the drugs were given individually. We, thus, conclude that during concurrent administration of Ketorolac and Omeprazole adequate precautions should be taken. However, further studies are needed on in-vivo model to substantiate the findings from in-vitro experiments. DOI: http://dx.doi.org/10.3329/bpj.v17i1.22323 Bangladesh Pharmaceutical Journal 17(1): 92-98, 2014

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Biophysical insight into the binding mechanism of doxofylline to bovine serum albumin: An in vitro and in silico approach

Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy ◽

10.1016/j.saa.2020.119296 ◽

2021 ◽

Vol 249 ◽

pp. 119296

Author(s):

Sharmin Siddiqui ◽

Faisal Ameen ◽

Tasneem Kausar ◽

Shahid M. Nayeem ◽

Sayeed Ur Rehman ◽

...

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

In Silico ◽

Bovine Serum ◽

Binding Mechanism ◽

Insight Into

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In silico and experimental studies of bovine serum albumin-encapsulated carbenoxolone nanoparticles with reduced cytotoxicity

Colloids and Surfaces B Biointerfaces ◽

10.1016/j.colsurfb.2021.111670 ◽

2021 ◽

pp. 111670

Author(s):

Subhashini Bharathala ◽

Lakshmi Kanth Kotarkonda ◽

Vijay Pal Singh ◽

Rajni Singh ◽

Pankaj Sharma

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

In Silico ◽

Bovine Serum ◽

Experimental Studies

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A Precipitin-like Reaction of the Hemolymph of the Lobster Homarus americanus

Journal of the Fisheries Research Board of Canada ◽

10.1139/f69-127 ◽

1969 ◽

Vol 26 (5) ◽

pp. 1392-1397 ◽

Cited By ~ 10

Author(s):

James E. Stewart ◽

Diane M. Foley

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Serum Proteins ◽

Homarus Americanus ◽

Test Period ◽

Fluorescent Material

The levels of fluorescent material in the hemolymph of lobsters injected with serum proteins from lobster hemolymph labelled with fluorescein remained relatively constant over a 6-day test period; the levels in lobsters injected with bovine serum albumin labelled with fluorescein declined rapidly. A precipitin-like reaction was observed when lobster hemolymph serum was titrated with bovine serum albumin in vitro.

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Preparation and in vitro photodynamic activities of novel axially substituted silicon (IV) phthalocyanines and their bovine serum albumin conjugates

Bioorganic & Medicinal Chemistry Letters ◽

10.1016/j.bmcl.2006.01.075 ◽

2006 ◽

Vol 16 (9) ◽

pp. 2450-2453 ◽

Cited By ~ 42

Author(s):

Xiong-Jie Jiang ◽

Jian-Dong Huang ◽

Yu-Jiao Zhu ◽

Fen-Xiang Tang ◽

Dennis K.P. Ng ◽

...

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum

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Amuchina Gel Xgerm hand rub in vitro virucidal activity against SARS-CoV-2

Future Microbiology ◽

10.2217/fmb-2021-0128 ◽

2021 ◽

Author(s):

Alessandra Capezzone de Joannon ◽

Angela Testa ◽

Natalie Falsetto ◽

Michela Procaccini ◽

Lorella Ragni

Keyword(s):

Detection Limit ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Virucidal Activity ◽

European Standard ◽

Enveloped Viruses ◽

Prevention Measure ◽

Study Product

Aim: Ethanol is highly effective at inactivating enveloped viruses, including SARS-CoV-2. The aim of this study is to evaluate the virucidal activity of Amuchina Gel Xgerm (74% ethanol) against SARS-CoV-2, according to the European Standard EN14476:2013+A2:2019. Materials & methods: Virucidal activity of the study product was evaluated against SARS-CoV-2 strain USAWA1/2020 in suspension, in the presence of 0.3 g/l of bovine serum albumin. Results: The log10 reduction of SARS-CoV-2 in the presence of bovine serum albumin was ≥4.11 ± 0.12 after 30 s of exposure to the study product (80% dilution). Cytotoxicity was observed in the 100 dilution, affecting the detection limit by 1 log10. Conclusion: Virucidal activity against SARS-CoV-2 supports the effectiveness of this alcohol-based formulation as a prevention measure for COVID-19 illness.

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