Investigation of Conformational Changes of Bovine Serum Albumin upon Binding with Benzocaine Drug: a Spectral and Computational Analysis

Qashqoosh, Mohsen T.A.; Manea, Yahiya Kadaf; Alahdal, Faiza A.M.; Naqvi, Saba

doi:10.1007/s12668-019-00663-7

Cited by 27 publications

(17 citation statements)

References 39 publications

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“…Further, intrinsic fluorescence of BSA-arising from the two Trp residues 38 -showed a large blue shift in maximum emission wavelength (Figure 6(b)), strongly indicating a hydrophobic microenvironment around the residues and significant conformational changes to the BSA. 39,40 These results complement the findings of a previous study by Madurantakam et al, who reported loss of biological activity of BMPs following exposure to organic solvents, although a slot-blot assay did not suggest disruptions to protein structure. 8 Our study provides evidence for significant changes to protein secondary structure when BSA is directly exposed to organic solvents without a carrier phase as can possibly occur in blend electrospinning.…”

Section: Discussionsupporting

confidence: 88%

Evaluating the protective role of carrier microparticles in preserving protein secondary structure within electrospun meshes

Shaw

Dash

Samavedi

2020

J of Applied Polymer Sci

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Direct incorporation of proteins into electrospun meshes using approaches such as blend electrospinning can promote adverse interactions with hydrophobic polymers, organic solvents and high voltage, potentially leading to loss of protein activity. However, pre-encapsulation within a protective carrier phase can preserve protein conformation by avoiding exposure to harsh processing conditions. In this study, bovine serum albumin (BSA) was loaded within cellulose microparticles (MPs) and the BSA-loaded MPs were dispersed in a solution of poly(ethylene oxide) (PEO). Particle-mesh composites were created using a sacrificial fiber/co-electrospinning approach in which the BSA/MP/PEO solution was simultaneously electrospun against a poly(caprolactone) (PCL) solution. Post-fabrication, sacrificial PEO fibers were selectively dissolved by treatment with ethanol. Microscopy, weight loss analysis and FTIR spectroscopy together confirmed selective dissolution of PEO fibers and the retention of BSA-loaded MPs within the PCL network without significant loss of either the MPs or the protein. Circular dichroism spectroscopy and intrinsic fluorescence measurements on BSA extracted from the co-electrospun meshes indicated minimal disruption to secondary structure, although partial sheet induction was observed. In contrast, direct exposure of BSA to four commonly used electrospinning solvents resulted in a large decrease in helical content and significant induction of sheets, revealing significant changes to the secondary structure. In summary, our results demonstrate the protective role of MPs in minimizing adverse effects of electrospinning on the secondary structure of incorporated protein.

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Section: Discussionsupporting

confidence: 88%

Evaluating the protective role of carrier microparticles in preserving protein secondary structure within electrospun meshes

Shaw

Dash

Samavedi

2020

J of Applied Polymer Sci

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“…Fluorescence quenching is routinely used to ascertain the effect of a particular drug on the target protein. The impact of the drug on the protein can be dynamic due to collisions between the fluorophore (protein) and the quencher (drug), or it may be static, owing to the protein and the quencher forming a complex at ground-state [ 16 , 17 ]. An intense quenching of the fluorescence marked an unvarying local dielectric environment.…”

Section: Methodsmentioning

confidence: 99%

Screening and evaluation of approved drugs as inhibitors of main protease of SARS-CoV-2

Tripathi

Upadhyay

Singh³

et al. 2020

International Journal of Biological Macromolecules

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The COVID-19 pandemic caused by SARS-CoV-2 has emerged as a global catastrophe. The virus requires main protease for processing the viral polyproteins PP1A and PP1AB translated from the viral RNA. In search of a quick, safe and successful therapeutic agent; we screened various clinically approved drugs for the in-vitro inhibitory effect on 3CL Pro which may be able to halt virus replication. The methods used includes protease activity assay, fluorescence quenching, surface plasmon resonance (SPR), Thermofluor® Assay, Size exclusion chromatography and in-silico docking studies. We found that Teicoplanin as most effective drug with IC 50 ~ 1.5 μM. Additionally, through fluorescence quenching Stern–Volmer quenching constant (K SV ) for Teicoplanin was estimated as 2.5 × 10 5 L·mol −1 , which suggests a relatively high affinity between Teicoplanin and 3CL Pro protease. The SPR shows good interaction between Teicoplanin and 3CL Pro with K D ~ 1.6 μM. Our results provide critical insights into the mechanism of action of Teicoplanin as a potential therapeutic against COVID-19. We found that Teicoplanin is about 10–20 fold more potent in inhibiting protease activity than other drugs in use, such as lopinavir, hydroxychloroquine, chloroquine, azithromycin, atazanavir etc. Therefore, Teicoplanin emerged as the best inhibitor among all drug molecules we screened against 3CL Pro of SARS-CoV-2.

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“…BSA is used as a model protein to study the interaction between drugs and albumins . Indeed, due to the physiological role of serum albumin as the main drug carrier, these studies are fundamental in the elucidation of pharmacokinetic properties of developing drugs …”

Section: Introductionmentioning

confidence: 99%

Entropy‐driven binding of octyl gallate in albumin: Failure in the application of temperature effect to distinguish dynamic and static fluorescence quenching

Bertozo

Fernandes

Yoguim

et al. 2020

J of Molecular Recognition

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Fluorescence quenching is widely used to obtain association constants between proteins and ligands. This methodology is based on assumption that ground-state complex between protein and ligand is responsible for quenching. Here, we call the attention about the risk of using the temperature criterion for decision of applying or not fluorescence quenching data to measure association constants. We demonstrated that hydrophobic effect can be the major force involved in the interaction and, as such, superposes the well-established rationalization that host/guest com-

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Investigation of Conformational Changes of Bovine Serum Albumin upon Binding with Benzocaine Drug: a Spectral and Computational Analysis

Cited by 27 publications

References 39 publications

Evaluating the protective role of carrier microparticles in preserving protein secondary structure within electrospun meshes

Evaluating the protective role of carrier microparticles in preserving protein secondary structure within electrospun meshes

Screening and evaluation of approved drugs as inhibitors of main protease of SARS-CoV-2

Entropy‐driven binding of octyl gallate in albumin: Failure in the application of temperature effect to distinguish dynamic and static fluorescence quenching

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