scholarly journals In vitro Interactions of Secnidazole and Its Iron (II), Copper (II) Complexes with Bovine Serum Albumin by Fluorescence Quenching Method

2020 ◽  
Vol 23 (1) ◽  
pp. 1-9
Author(s):  
Md Jamal Hossain ◽  
Md Zakir Sultan ◽  
Mohammad A Rashid ◽  
Md Ruhul Kuddus
Keyword(s):  
Bovine Serum Albumin ◽  
Transition Metal ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Metal Complexes ◽  
Transition Metal Complexes ◽  
Bovine Serum ◽  
Spectroscopic Method ◽  
Van Der Waals Interactions

The current study was designed to investigate the interactions of an antimicrobial drug secnidazole and its two transition metal complexes with bovine serum albumin (BSA). The interactions of secnidazole and its both transition metal complexes were confirmed by the extingushing of fluorescence intensity of the protein. The fluorescence quenching of BSA by the drug and its both metal complexes showed a static quenching process and the reactions followed exothermic mechanism. The fluorescence spectroscopic method was utilized to evaluate the thermodynamic parameters like change of enthalpy (ΔH), entropy (ΔS) and Gibb’s free energy (ΔG) which indicated the bindings of the antimicrobial agent and its both metal chelates were hydrogen bonding and van der Waals interactions. The binding constant and the number of binding sites were also measured by double log plot that indicated the drug or its metal complexes bound with BSA at 1:1 ratio. Bangladesh Pharmaceutical Journal 23(1): 1-9, 2020

Study on the interaction characteristics of dexamethasone sodium phosphate with bovine serum albumin by spectroscopic technique

2014 ◽  
Vol 38 (9) ◽  
pp. 4092-4098 ◽  
Author(s):  
Qian Wang ◽  
Xuyang Liu ◽  
Ming Su ◽  
Zhihong Shi ◽  
Hanwen Sun
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Sodium Phosphate ◽  
Spectroscopic Method ◽  
Spectroscopic Technique ◽  
Physiological Conditions ◽  
Dexamethasone Sodium Phosphate

The interaction of dexamethasone sodium phosphate (DEX-P) with bovine serum albumin (BSA) was studied by fluorescence quenching in combination with UV-Vis spectroscopic method under near physiological conditions.

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

2015 ◽  
Vol 17 (1) ◽  
pp. 92-98 ◽  
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

scholarly journals In-vitro Fluorescence Spectroscopic Analysis of the Interaction of Glimepiride with Bovine Serum Albumin (BSA)

2019 ◽  
pp. 1-8
Author(s):  
Kanij Nahar Deepa ◽  
Sabia Nawsheen ◽  
Md. Abu Sufian ◽  
S. M. Ashraful Islam
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Thermodynamic Parameters ◽  
Bovine Serum ◽  
Spectroscopic Analysis ◽  
Spectroscopic Technique ◽  
Different Temperatures ◽  
Quenching Method

Background: The significant study was made to investigate the interaction of an antidiabetic drug, glimepiride with bovine serum albumin (BSA) by fluorescence quenching method in two different temperatures (298K and 308K). Methods: The study was carried out through fluorescence spectroscopic analysis. Stern-Volmer equation determined the fluorescence quenching constant. The various thermodynamic parameters such as free energy (ΔG), enthalpy (ΔH), and entropy (ΔS) was found out by Van’t Hoff equation. Results: The data revealed that glimepiride interact with BSA and both tryptophan and tyrosine residues of BSA are responsible for interactions with glimepiride. BSA undergo static quenching in presence of glimepiride, a quencher. The hydrophobic forces participated in chief roles for BSA-glimepiride complexation and this was indicated by the values of thermodynamic parameters. The binding number (n) obtained was ≈1 pointed out that glimepiride and BSA has bound with 1:1 ratio. Conclusions: Through fluorescence spectroscopic technique we revealed the nature of interaction of glimepiride with BSA, quenching mechanism for the interaction and associated thermodynamic parameters.

Synthesis, Characterization and in vitro Biological Evaluation of a New Schiff Base Derived from Drug and its Complexes with Transition Metal Ions

2018 ◽  
Vol 69 (7) ◽  
pp. 1678-1681
Author(s):  
Amina Mumtaz ◽  
Tariq Mahmud ◽  
M. R. J. Elsegood ◽  
G. W. Weaver
Keyword(s):  
Schiff Base ◽  
Transition Metal ◽  
Metal Ions ◽  
Metal Complexes ◽  
Transition Metal Complexes ◽  
Free Ligand ◽  
Transition Metal Ions ◽  
Biological Evaluation ◽  
Pyridoxal Hydrochloride

New series of copper (II), cobalt (II), zinc (II), nickel (II), manganese (II), iron (II) complexes of a novel Schiff base were prepared by the condensation of sulphadizine and pyridoxal hydrochloride. The ligand and metal complexes were characterized by utilizing different instrumental procedures like microanalysis, thermogravimetric examination and spectroscopy. The integrated ligand and transition metal complexes were screened against various bacteria and fungus. The studies demonstrated the enhanced activity of metal complexes against reported microbes when compared with free ligand.

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

1969 ◽  
Vol 26 (5) ◽  
pp. 1392-1397 ◽  
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.

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

2006 ◽  
Vol 16 (9) ◽  
pp. 2450-2453 ◽  
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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