Study of Interaction Between Bovine Serum Albumin and Dolutegravir Intermediate: Fluorescence and Molecular Docking Analysis

Novel (4R,12aS)-7-methoxy-4-methyl-6,8-dioxo-3,4,6,8,12,12a-hexahydro-2H-pyrido-[1',2':-4,5]-pyrazino[2,1-b][1,3]oxazine-9-carboxylic acid (L) was synthesized and characterised. The interaction between bovine serum albumin (BSA) with L was scrutinized by steady-state fluorescence spectroscopy, fluorescence anisotropy, fluorescence lifetime, and molecular docking methods. The fluorescence titration experiments of BSA resulted in fluorescence quenching with the incremental addition of L. The conformational binding of L to BSA has been investigated by molecular docking analysis. The molecular probe's best conformation showed the affinity as free binding energy release of -7.93 Kcal/mol. The docking analysis confirms that ligand binds in the near vicinity of TRP-213 in the binding pocket of subdomain IIA.

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Multispectroscopic exploration and molecular docking analysis on interaction of eriocitrin with bovine serum albumin

Journal of Molecular Recognition ◽

10.1002/jmr.2779 ◽

2019 ◽

Vol 32 (7) ◽

pp. e2779 ◽

Cited By ~ 5

Author(s):

Xiangyu Cao ◽

Zhijun Yang ◽

Yonglin He ◽

Ying Xia ◽

Yin He ◽

...

Keyword(s):

Molecular Docking ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Docking Analysis ◽

Molecular Docking Analysis

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In vitro interaction of organophosphate metabolites with bovine serum albumin: A comparative 1H NMR, fluorescence and molecular docking analysis

Pesticide Biochemistry and Physiology ◽

10.1016/j.pestbp.2019.10.004 ◽

2020 ◽

Vol 163 ◽

pp. 39-50 ◽

Cited By ~ 4

Author(s):

Vandana Dahiya ◽

Bibin G. Anand ◽

Karunakar Kar ◽

Samanwita Pal

Keyword(s):

Molecular Docking ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

1H Nmr ◽

Bovine Serum ◽

Docking Analysis ◽

In Vitro Interaction ◽

Molecular Docking Analysis

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Domain-Specific Association of a Phenanthrene–Pyrene-Based Synthetic Fluorescent Probe with Bovine Serum Albumin: Spectroscopic and Molecular Docking Analysis

ACS Omega ◽

10.1021/acsomega.8b00186 ◽

2018 ◽

Vol 3 (6) ◽

pp. 6293-6304 ◽

Cited By ~ 17

Author(s):

Mihir Sasmal ◽

Rahul Bhowmick ◽

Abu Saleh Musha Islam ◽

Sutanwi Bhuiya ◽

Suman Das ◽

...

Keyword(s):

Molecular Docking ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Fluorescent Probe ◽

Bovine Serum ◽

Docking Analysis ◽

Domain Specific ◽

Specific Association ◽

Molecular Docking Analysis

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Molecular docking analysis on the interaction between bovine serum albumin and three commercial fluoroquinolones: Ciprofloxacin, enrofloxacin and pefloxacin

European Journal of Chemistry ◽

10.5155/eurjchem.12.2.192-196.2103 ◽

2021 ◽

Vol 12 (2) ◽

pp. 192-196

Author(s):

Otavio Augusto Chaves ◽

Leonardo Vazquez

Keyword(s):

Molecular Docking ◽

Amino Acid ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Protein Binding ◽

Bovine Serum ◽

Binding Pocket ◽

Molecular Features ◽

Residue Interaction ◽

The Individual

Fluoroquinolones are a family of broad spectrum, systemic antibacterial agents that have been used as therapy for infections in the respiratory and alimentary tract in animals. The pharmacodynamic of this class is widely described, predominantly to the commercial drugs ciprofloxacin (CIP), enrofloxacin (ENR), and pefloxacin (PEF). Bovine serum albumin (BSA) is the main endogenous carrier in the bovine bloodstream, being responsible for the biodistribution of different classes of molecules and drugs, including fluoroquinolones. The molecular features and interaction between BSA and fluoroquinolones are not fully described, thus, the present work enlightens the intimacy of the interaction of BSA with CIP, ENR, PEF through structural modeling and molecular docking calculation approaches. The role of key amino acid residues was assessed, indicating that the main protein binding pocket is composed by Trp-212 residue playing an important stabilization for the three fluoroquinolones through both hydrogen bonding and van der Waals forces, where reside the individual structural differences observed among the three fluoroquinolones and BSA. There is a descriptive protagonism of carboxyl group on the ENR interaction which traps the molecule and avoids the deep communication in the protein binding pocket, as well as the ligands CIP and PEF showed an interface amino acid residue interaction profile higher than 70%.

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Metal-Biosurfactant Complexes Characterization: Binding, Self-Assembly and Interaction with Bovine Serum Albumin

International Journal of Molecular Sciences ◽

10.3390/ijms20122864 ◽

2019 ◽

Vol 20 (12) ◽

pp. 2864 ◽

Cited By ~ 3

Author(s):

Tomasz Janek ◽

Lígia R. Rodrigues ◽

Eduardo J. Gudiña ◽

Żaneta Czyżnikowska

Keyword(s):

Molecular Docking ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Self Assembly ◽

Bovine Serum ◽

Peptide Antibiotics ◽

Divalent Metal Ions ◽

Docking Analysis ◽

Potential Applications ◽

Semi Empirical

Studies on the specific and nonspecific interactions of biosurfactants with proteins are broadly relevant given the potential applications of biosurfactant/protein systems in pharmaceutics and cosmetics. The aim of this study was to evaluate the interactions of divalent counterions with the biomolecular anionic biosurfactant surfactin-C15 through molecular modeling, surface tension and dynamic light scattering (DLS), with a specific focus on its effects on biotherapeutic formulations. The conformational analysis based on a semi-empirical approach revealed that Cu2+ ions can be coordinated by three amide nitrogens belonging to the surfactin-C15 cycle and one oxygen atom of the aspartic acid from the side chain of the lipopeptide. Backbone oxygen atoms mainly involve Zn2+, Ca2+ and Mg2+. Subsequently, the interactions between metal-coordinated lipopeptide complexes and bovine serum albumin (BSA) were extensively investigated by fluorescence spectroscopy and molecular docking analysis. Fluorescence results showed that metal-lipopeptide complexes interact with BSA through a static quenching mechanism. Molecular docking results indicate that the metal-lipopeptide complexes are stabilized by hydrogen bonding and van der Waals forces. The biosurfactant-protein interaction properties herein described are of significance for metal-based drug discovery hypothesizing that the association of divalent metal ions with surfactin allows its interaction with bacteria, fungi and cancer cell membranes with effects that are similar to those of the cationic peptide antibiotics.

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