An insight into the inhibition of fibrillation process verses disaggregation of preformed fibrils of bovine serum albumin by isoprenaline hydrochloride

Serum albumin is the most abundant protein in blood plasma; among its functions is the transport of a high variety of drugs in the body. Quinones show several biological and pharmacological activities, such as anti-malarial, antitumor, anti-microbial, anti-inflammatory and anti-parasitic. We report fluorescence and circular dichroism (CD) spectroscopic studies to try to understand the interaction process between Î±-lapachone (Î±-LAP) and bovine serum albumin (BSA). Studies using computational methods, such as molecular docking, were performed to identify the main cavity in which this interaction occurs as well as the type of intermolecular interactions between the amino acid residues from albumin and the ligand. The BSA fluorescence quenching by added Î±-LAP is a static process, indicating an initial association BSA: Î±-LAP. The Ka and Kb values for the interaction BSA: Î±-LAP are in the range 105-104 Lâˆ™mol-1, indicating a strong binding between these two species. CD data show that there is no significant perturbation on the secondary structure of the protein with binding. The negative Î”Go values are consistent with spontaneous binding occurring endothermically (Î”Ho = 127 kJâˆ™mol-1), and possibly driven by hydrophobic factors (Î”So = 0.526 kJâˆ™mol-1âˆ™s-1). The number of binding sites (n) indicates the existence of just one main binding site in BSA for Î±-LAP, with molecular docking results showing that it binds preferentially to the albumin in the domain IIA, where the Trp-212 residue is located. The ligand interacts via hydrogen bond with Arg-259 and Tyr-149 residues and via T-stacking with the fluorophore Trp-212 residue.

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Molecular level insight into the effect of triethyloctylammonium bromide on the structure, thermal stability, and activity of Bovine serum albumin

International Journal of Biological Macromolecules ◽

10.1016/j.ijbiomac.2017.08.157 ◽

2018 ◽

Vol 107 ◽

pp. 186-193 ◽

Cited By ~ 6

Author(s):

Lakkoji Satish ◽

Sabera Millan ◽

Visakh Vijayalekshmi Sasidharan ◽

Harekrushna Sahoo

Keyword(s):

Thermal Stability ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Molecular Level ◽

Insight Into

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Construing the interactions between MnO2 nanoparticle and bovine serum albumin: insight into the structure and stability of a protein–nanoparticle complex

New Journal of Chemistry ◽

10.1039/c7nj01227f ◽

2017 ◽

Vol 41 (16) ◽

pp. 8130-8139 ◽

Cited By ~ 20

Author(s):

Ayonbala Baral ◽

Lakkoji Satish ◽

Dipti P. Das ◽

Harekrushna Sahoo ◽

Malay K. Ghosh

Keyword(s):

Experimental Investigation ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Structure And Stability ◽

Insight Into ◽

Nanoparticle Complex

Systematic experimental investigation of MnO2–BSA complexes in terms of the structure and stability of the protein as well as the aggregation of the nanoparticle.

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