scholarly journals Spectroscopic Evaluation of Chalcone Derivatives and their Zinc Metal Complexes: A Combined Experimental and Computational Approach on the Binding of the Complexes with the Serum Albumin

2020 ◽  
Author(s):  
Manos C. Vlasiou
Keyword(s):  
Molecular Docking ◽  
Serum Albumin ◽  
Electrostatic Interactions ◽  
Condensation Reaction ◽  
Dft Method ◽  
Spectroscopic Properties ◽  
Molecular Structures ◽  
Chalcone Derivatives ◽  
Vis Spectroscopy ◽  
Spectroscopy Studies

Abstract Three chalcone derivatives (L1, L2, L3) were synthesized using Claisen-Schmidt condensation reaction. Their molecular structures and spectroscopic properties (IR, UV-vis, 1HNMR), were calculated at B3LYP level. Electrostatic interactions and HOMO-LUMO properties were calculated using TD-DFT method. Molecular docking was used to compare the HSA (human serum albumin) interactions with the ligands and their Zn complexes (C1, C2, C3) which were synthesized by interaction between the ligands and the Zn (II) ion in a 2:1 M ratio. Elemental analysis, FT-IR, and UV–Vis spectroscopy studies investigated the structure of the synthesized complexes. UV–Vis, molecular docking and molecular dynamics were used to study the interactions of the Zn complexes with the BSA (bovine serum albumin). The biological activity of the Zn-Chalcone complexes was generally higher than the chalcones when evaluated spectroscopically and theoretically.

scholarly journals Probing the toxic interactions between the reactive dye Drimaren Red and Human Serum Albumin

2021 ◽  
Author(s):  
Thais Meira Menezes ◽  
Caio Rodrigo Dias de Assis ◽  
Antonio Marinho da Silva Neto ◽  
Priscila Gubert ◽  
Marcos Gomes Ghislandi ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Textile Industry ◽  
Electrostatic Interactions ◽  
Reactive Dye ◽  
Biological Macromolecules ◽  
Spectroscopic Techniques ◽  
Binding Characteristics

Azo dyes like Drimaren Red CL-5B (DR, CI Reactive Red 241) represent a class of compounds extensively used in the textile industry and are extremely dangerous to the environment and human health. Therefore, understanding the binding characteristics between such substances and biological macromolecules is essential from a toxic-kinetic perspective. The molecular interaction between DR and Human Serum Albumin (HSA) was investigated through spectroscopic techniques and molecular docking approaches. The results indicate that DR quenches HSA fluorescence following a static mechanism (corroborated by UV-Vis studies) with a moderate interaction (Ka~105 M-1), guided by electrostatic interactions (DS> 0 and DH< 0). DR is 5.52 nm distant from fluorophore residue Trp-214 (according to FRET investigations), and the interaction is mainly related to Tyr residues (as revealed by synchronous fluorescence). The Ellman assay identified a decrease in the content of HSA free thiol. The results of the RLS demonstrate that there are HSA alterations, suggesting damage to the confirmation of the protein. Molecular docking suggests the binding site of DR was located in subdomain IIB HSA, corroborating the experimental properties. Finally, the results suggest a high potential for DR toxicity triggered by contact with key proteins, which affects the biomolecule functionalities.

Synthesis, Characterization, and Application of Chalcone Derivatives as Chemosensors for Cyanide Anions

2021 ◽  
Vol 01 ◽  
Author(s):  
Ankush Gupta ◽  
Akshay Kumar ◽  
Nidhi Choudhary ◽  
Bharti Gupta ◽  
Harminder Singh ◽  
...  
Keyword(s):  
Low Cost ◽  
Condensation Reaction ◽  
High Reactivity ◽  
Water Soluble ◽  
Conjugation System ◽  
Chalcone Derivatives ◽  
Real Time Analysis ◽  
Vis Spectroscopy ◽  
Living Organisms ◽  
Interfering Ions

Research Background: The extreme toxicity of cyanide ions to living organisms encourages the researcher to develop new chemosensors for their sensitive and selective detection. Among various classes of chemosensors, chalcones are believed to be a promising candidate for designing new chemosensors for anions due to easy modification in its skeleton and conjugation system. Research Gap and Problem Statement: Despite having various medical applications and properties, the recognition ability of chalcone derivatives is not widely explored. The traditional methods known for the sensing of cyanide ions are ion chromatography or cyanide selective electrodes. However, these methods need skilled operators and are found to be expensive and time-consuming. Also, the available methods for detection of cyanide ions are not suitable for on-site monitoring and show interference from other competitive anions such as fluoride, acetate, and hydroxide ions. Hence, this encouraged us to explore the chalcone derivatives as chemical sensors that are capable of detecting the cyanide ions in presence of competitive anions such as fluoride, acetate, and hydroxide ions. Objectives of the study: The development of new chalcone analogs (1E,4E)-1,5-bis(4-chlorophenyl)penta-1,4-dien-3-one (3) and (E)-3-phenyl-1-(pyridin-2-yl)prop-2-en-1-one (6), which are particularly important for the future development of chemosensors for the detection of cyanide ions in presence of various interfering ions such as fluoride, acetate, and hydroxide ions. Methods: The sensing behavior of chalcone derivatives (1E,4E)-1,5-bis(4-chlorophenyl)penta-1,4-dien-3-one (3) and (E)-3-phenyl-1-(pyridin-2-yl)prop-2-en-1-one (6) have been investigated toward various anions (CN-, F-, Cl-, Br-, NO3-, SO42-, PO42-, OH-, OAc-) using UV-vis spectroscopy. Interestingly, among various anions tested, derivatives (1E,4E)-1,5-bis(4-chlorophenyl)penta-1,4-dien-3-one (3) and (E)-3-phenyl-1-(pyridin-2-yl)prop-2-en-1-one (6) function as highly selective chemosensors for the detection of cyanide ions. Results: We have synthesized two chalcone based derivatives (1E,4E)-1,5-bis(4-chlorophenyl)penta-1,4-dien-3-one (3) and (E)-3-phenyl-1-(pyridin-2-yl)prop-2-en-1-one (6) with simple condensation reaction for the detection of cyanide ions. The various results indicated the quick response of (1E,4E)-1,5-bis(4-chlorophenyl)penta-1,4-dien-3-one (3) and (E)-3-phenyl-1-(pyridin-2-yl)prop-2-en-1-one (6) toward cyanide anions. These two chalcone derivatives (1E,4E)-1,5-bis(4-chlorophenyl)penta-1,4-dien-3-one (3) and (E)-3-phenyl-1-(pyridin-2-yl)prop-2-en-1-one (6) showed not only spectral change with selectivity but also showed sensitivity for the detection of cyanide anions. The developed chalcone derivatives (1E,4E)-1,5-bis(4-chlorophenyl)penta-1,4-dien-3-one (3) and (E)-3-phenyl-1-(pyridin-2-yl)prop-2-en-1-one (6) detect cyanide ions in presence of various interfering ions such as fluoride, acetate, and hydroxide ions. The chemosensors (1E,4E)-1,5-bis(4-chlorophenyl)penta-1,4-dien-3-one (3) and (E)-3-phenyl-1-(pyridin-2-yl)prop-2-en-1-one (6) for the detection of cyanide ions are particularly smart due to their real-time analysis, simplicity, and low cost in comparison to other closely related processes such as fluorescence. Conclusion: The sensitivity studies show the high reactivity of derivative 1,5-bis(4-chlorophenyl)penta-1,4-dien-3-one (3) as compared to (E)-3-phenyl-1-(pyridin-2-yl)prop-2-en-1-one (6). The detection limit for derivatives (1E,4E)-1,5-bis(4-chlorophenyl)penta-1,4-dien-3-one (3) and (E)-3-phenyl-1-(pyridin-2-yl)prop-2-en-1-one (6) was 1.2 µM and 300 µM, respectively. The results of (1E,4E)-1,5-bis(4-chlorophenyl)penta-1,4-dien-3-one (3) and (E)-3-phenyl-1-(pyridin-2-yl)prop-2-en-1-one (6) for cyanide detection were satisfying and suggesting their potential application for cyanide detection. Future direction: Further research of this field is to develop water soluble chalcone based probes, which show emission in the Near Infra-Red (NIR) region to provide favorable conditions for biological applications.

scholarly journals Spectroscopic, voltammetry and molecular docking study of binding interaction of antipsychotic drug with bovine serum albumin

2016 ◽  
Vol 6 (2) ◽  
pp. 155 ◽  
Author(s):  
Mallappa Mahanthappa ◽  
Babu Giriya Gowda ◽  
Jayant I. Gowda ◽  
Raghavendran Rengaswamy
Keyword(s):  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Free Energy ◽  
Acetate Buffer ◽  
Acetate Buffer Solution ◽  
Binding Interaction ◽  
Vis Spectroscopy

<p class="PaperAbstract"><span lang="EN-GB">The interaction between perazine dimaleate (PDM) and bovine serum albumin (BSA) was investigated by voltammetry, fluorescence spectroscopy, UV–vis spectroscopy, molecular docking and viscometric methods. The study was carried out in acetate buffer solution of pH 7.2, which was prepared by using 0.1 M sodium acetate and adjusting pH using 0.1 M hydrochloric acid. The voltammetric study of PDM shows a pair of well redox peaks at 0.538 and 0.471 V (versus SCE) on a GCE in acetate buffer of pH 7.2 at <br /> 50 mV s<sup>-1</sup>. After the addition of BSA into the PDM solution, the redox peak currents decreased gradually, and peak potentials shifted towards negative direction. The results of voltammetry, fluorescence quenching and UV–vis absorption spectra experiments indicated the formation BSA–PDM complex. The binding parameters like binding con­stant and binding free energy were determined from voltammetric data. The binding constant and binding energy was also determined from UV–vis and fluorescence spectroscopy with a value quite close to that obtained from CV.</span></p>

Characterization of the interaction between human serum albumin and diazinon via spectroscopic and molecular docking methods

2018 ◽  
Vol 37 (9) ◽  
pp. 959-971
Author(s):  
S Hadichegeni ◽  
B Goliaei ◽  
M Taghizadeh ◽  
S Davoodmanesh ◽  
F Taghavi ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Blood Protein ◽  
Vis Spectroscopy ◽  
Close Relationship ◽  
Partially Unfolded ◽  
Α Helix ◽  
Toxic Concentrations

Human serum albumin (HSA) is a soluble blood protein which binds to small molecules (such as drugs and toxins) and transfers them within the blood circulation. In this research, the interaction of diazinon, as a toxic organophosphate, with HSA was investigated. Various biophysical methods such as fluorescence, ultraviolet–visible (UV-vis), Fourier transform infrared spectroscopy, and molecular docking were utilized to characterize the binding properties of diazinon to HSA under physiological-like condition. The UV-vis spectroscopy showed that the absorption increased and the fluorescence intensity of HSA decreased regularly with regard to the gradual increases of the concentrations of diazinon. Due to the binding constant of ( ka = 3.367 × 10+4 M−1), the α-helix structure for the first day and 35 days of incubation were obtained 66.09–55.4% and 59.99–46.48%, respectively, and their amounts in other secondary structures (β-sheet, β-anti, and random (r) coils) were increased. The molecular docking revealed a good binding site in HSA (Trp-214) for diazinon which was related to the considerable alterations in HSA secondary and tertiary structures. There is a close relationship between the secondary structure of protein and its biological activity and after 35 days of incubation, the high toxic concentrations of diazinon can make HSA to be partially unfolded and lose its structure.

scholarly journals Studi Teoritis Senyawa Turunan Kalkon Hidroksi Sebagai Sensor Kimia Berbagai Anion

2019 ◽  
Vol 3 (2) ◽  
pp. 95
Author(s):  
Fitra Perdana ◽  
Karna Wijaya ◽  
Ria Armunanto
Keyword(s):  
Hydrogen Bond ◽  
Geometry Optimization ◽  
Dft Method ◽  
Molecular Structures ◽  
Energy Change ◽  
Lumo Energy ◽  
Interaction Models ◽  
Chalcone Derivatives ◽  
The Difference ◽  
Homo Lumo

AbstrakStudi secara teoritis telah dilakukan untuk mempelajari interaksi senyawa turunan kalkon hidroksi (CH) sebagai sensor kimia dengan anion F-, Cl-, Br-, CN-, CH3COO-, dan NO3-. Penelitian ini bertujuan untuk memodelkan struktur molekul senyawa turunan kalkon hidroksi (CH) dan sifat sensornya serta model interaksinya dengan anion dengan metode DFT. Hasil optimasi geometri menunjukkan terjadinya pemanjangan ikatan O-H sebesar 0,63-0,85 Å dengan adanya anion F-, CN-, and CH3COO-. Hal ini mengindikasikan terjadinya deprotonasi sensor kalkon hidroksi (CH) oleh anion. Sedangkan interaksi sensor kalkon hidroksi (CH) dengan anion Cl-, Br-, dan NO3- hanya berupa ikatan hidrogen dengan pemanjangan ikatan O-H sebesar 0,08-0,46 Å. Sensor kalkon hidroksi (CH) yang mengalami deprotonasi memiliki energi interaksi yang lebih besar yaitu -209,37 – -424,06 kJ/mol dibandingkan sensor yang hanya membentuk ikatan hidrogen yaitu -98,60 – -125,59 kJ/mol. Sensor yang mengalami deprotonasi mengakibatkan turunnya selisih energi HOMO-LUMO dari -3,94 – -4,06 eV menjadi -2,62 – -2,75 eV.Kata kunci: sensor kimia, kalkon hidroksi, anion, DFT  AbstractTheoretical study had been carried out to investigate interaction between hydroxy chalcone derivatives (CH) as chemosensors with F-, Cl-, Br-, CN-, CH3COO-, and NO3- anions. This study was aimed to design molecular structures of chemosensor hydroxy chalcone (CH) properties for the anions and their interaction models with DFT method. The result of geometry optimization showed 0,63-0,85 Å O-H bond elongation of the hydroxy chalcone was occured by F-, CN-, and CH3COO-. It was indicated deprotonation of sensor hydroxy chalcone (CH) by anions. Where as the interaction of the hydroxy chalcone (CH) with Cl-, Br-, and NO3- just formed an hydrogen bond with 0,08-0,46 Å O-H bond elongation. Deprotonized sensor hydroxy chalcone (CH) had more energy change of interaction -209,37– -424,06 kJ/mol than sensor which just formed the hydrogen bond -98,60 – -125,59 kJ/mol. Deprotonized sensor caused reduction of the difference of HOMO-LUMO energy from - 3,94 – -4,06 eV to -2,62 – -2,75 eV.Keywords: chemosensor, hydroxy chalcone, anion, DFT

scholarly journals A Diversified Spectrometric and Molecular Docking Technique to Biophysical Study of Interaction between Bovine Serum Albumin and Sodium Salt of Risedronic Acid, a Bisphosphonate for Skeletal Disorders

2018 ◽  
Vol 2018 ◽  
pp. 1-13 ◽  
Author(s):  
M. Manjushree ◽  
Hosakere D. Revanasiddappa
Keyword(s):  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Sodium Salt ◽  
Bovine Serum ◽  
Biologically Active ◽  
Risedronic Acid ◽  
Binding Interaction ◽  
Vis Spectroscopy ◽  
Ft Ir

The binding interaction between bovine serum albumin (BSA) and sodium salt of risedronic acid (RSN) was studied by using the FT-IR (Fourier transform infrared), UV-Vis (ultraviolet–visible), fluorescence (emission and synchronous), CD (circular dichroism) spectrometric, and computational (molecular docking) techniques at 289, 297, and 305 K temperatures with physiological buffer of pH 7.40. The conformational and secondary structural changes observed for BSA from CD spectra and by curve fitting procedure were applied to Fourier self-deconvolution in FT-IR spectra. The formation of a BSA-RSN complex was confirmed from UV-Vis spectroscopy. The static type of quenching shown for RSN to BSA was verified from Stern–Volmer and modified Stern–Volmer equations. The binding constant of order 105 was obtained to be confirming that there exists a strong binding interaction between BSA and RSN. Synchronous fluorescence shows that the microenvironment of tryptophan was altered, not tyrosine of BSA; in addition to this, the distance between tryptophan of BSA and RSN was found out from Forster’s theory of nonradiation energy transfer. The interaction between BSA and RSN mainly occurred as a result of hydrogen bonds and van der Waals forces, the process is exothermic and spontaneous, and it was achieved through van ’t Hoff equation. This interaction was affected by the presence of biologically active Fe2+, Ni2+, Ca2+, Mg2+, and Cd2+ ions and was also studied. The subdomain IIIA of BSA involved with RSN interaction was authenticated from molecular docking analysis.

scholarly journals Dihydro-alpha-lipoic acid binds to human serum albumin at Sudlow I binding site

2020 ◽  
Author(s):  
Nikola Gligorijević ◽  
Vladimir Šukalović ◽  
Goran Miljuš ◽  
Olgica Nedić ◽  
Ana Penezić
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Lipoic Acid ◽  
Electrostatic Interactions ◽  
Dietary Intervention ◽  
Alpha Lipoic Acid ◽  
Preferential Binding

ABSTRACTBinding of dihydro-alpha-lipoic acid (DHLA) to human serum albumin (HSA) was characterised in detail in this study. Binding process was monitored by spectroscopic methods and molecular docking approach. HSA binds DHLA with moderate affinity, 0.80 ± 0.007 × 104 M−1. Spectroscopic data demonstrated that the preferential binding site for DHLA on HSA is IIA (Sudlow I). Hydrogen bonds and electrostatic interactions were identified as the key binding interactions. DHLA binding thermally stabilized HSA, yet it had no effect on HSA structure and its susceptibility to trypsin digestion. Molecular docking confirmed that Sudlow I site accommodated DHLA in a certain conformation in order for binding to occur. Molecular dynamic simulation showed that formed complex is stable. Reported results offer future perspectives for investigations regarding the use of DHLA as a dietary intervention but also raise concerns about the effectiveness of alpha-lipoic acid and DHLA in treatment of patients with COVID-19.

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