Comparative studies on biophysical interactions between 4-dicyanomethylene-2,6-dimethyl-4H-pyran (DDP) with bovine serum albumin (BSA) and human serum albumin (HSA) via photophysical approaches and molecular docking techniques

Ramachandran, Thamarai Selvan; Gunasekaran, Shoba; Sreedevi, Sangeetha Murugan; Vinod, Seba Merin; Rajendran, Kumaran; Tamizhdurai, P.; Amer, M Alanazi; P.-S., Ganesh

doi:10.1016/j.jscs.2021.101364

Cited by 8 publications

(2 citation statements)

References 78 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The above parameters govern the ease of formation of the complex and play a predominant role in docking studies. This methodology has been well established in our earlier studies involving DDP dye with globular proteins − like BSA, HSA, ovalbumin, β-lactoglobulin, and myoglobin.…”

Section: Resultsmentioning

confidence: 99%

Complexity of the Role of Various Site-Specific and Selective Sudlow Binding Site Drugs in the Energetics and Stability of the Acridinedione Dye–Bovine Serum Albumin Complex: A Molecular Docking Approach

et al. 2023

Self Cite

View full text Add to dashboard Cite

Molecular docking (Mol.Doc) techniques were employed to ascertain the binding affinity of two resorcinol-based acridinedione dyes (ADR1 and ADR2) with the widely studied globular protein Bovine Serum Albumin (BSA) in the presence of site-selective binding drugs by Autodock Vina 4.2 software. Docking of various feasible conformers of ADR1 dye with BSA was found to be energetically more favored than ADR2 dye, even though both these dyes differ in the 9th position of the basic dye structure. Analysis of dyes with BSA establishes the location of dye in all of the binding sites of BSA, predominantly through conventional and nonconventional hydrogen-bonding (HB) interactions. The coexistence of hydrophobic interactions resulted in the stability of various conformers generated. The introduction of site I and site II (Sudlow site binding drugs) into ADR1−BSA and ADR2−BSA complexes effectively destabilizes the dye−protein complex; however, the drugs do not displace ADR dyes completely from their selective binding domains. Site II binding drugs effectively destabilize the binding ability of the dye−protein complex rather than site I drugs. However, docking of site I drug 3-carboxyl-4-methyl-5-propyl-2-furanpropanic acid (CMPF) largely destabilizes the ADR1−protein complex, whereas indomethacin (INDO) enhances the binding affinity of the ADR2−protein complex. Interestingly, simultaneous docking of ADR dyes to the BSA−drug complex results in larger stability of the protein−drug complex through HB interactions rather than hydrophobic interactions. Both ADR1 and ADR2 dyes predominantly occupy the Sudlow binding sites of BSA, and the introduction of either site I or site II binding drugs does not displace the dye efficiently from the corresponding binding sites, rather the drugs are effectively displaced toward other binding domains apart from their specific site-binding domains of BSA. Through Mol.Doc techniques, we authenticate that the interactions in host−guest complex systems involving competing ligands are established in depth, wherein the dye as well as the amino acid (AA) moieties in BSA act as both HB donor and acceptor sites apart from several hydrophobic interactions coexisting toward the stability.

show abstract

Section: Resultsmentioning

confidence: 99%

Complexity of the Role of Various Site-Specific and Selective Sudlow Binding Site Drugs in the Energetics and Stability of the Acridinedione Dye–Bovine Serum Albumin Complex: A Molecular Docking Approach

et al. 2023

Self Cite

View full text Add to dashboard Cite

show abstract

“…Comparative studies of HSA and BSA solutions have been carried out employing different experimental techniques [48,49]. However, there are significant open questions regarding the viability of isolating the different effects due to the delicate competition between reversible and irreversible denaturation.…”

Section: Introductionmentioning

confidence: 99%

Mechano-Chemistry across Phase Transitions in Heated Albumin Protein Solutions

et al. 2023

View full text Add to dashboard Cite

The presence of certain proteins in biofluids such as synovial fluid, blood plasma, and saliva gives these fluids non-Newtonian viscoelastic properties. The amount of these protein macromolecules in biofluids is an important biomarker for the diagnosis of various health conditions, including Alzheimer’s disease, cardiovascular disorders, and joint quality. However, existing technologies for measuring the behavior of macromolecules in biofluids have limitations, such as long turnaround times, complex protocols, and insufficient sensitivity. To address these issues, we propose non-contact, optical Brillouin and Raman spectroscopy to assess the viscoelasticity and chemistry of non-Newtonian solutions, respectively, at different temperatures in several minutes. In this work, bovine and human serum albumin solution-based biopolymers were studied to obtain both their collective dynamics and molecular chemical evolution across heat-driven phase transitions at various protein concentrations. The observed phase transitions at elevated temperatures could be fully delayed in heated biopolymers by appropriately raising the level of protein concentration. The non-contact optical monitoring of viscoelastic and chemical property evolution could represent novel potential mechano-chemical biomarkers for disease diagnosis and subsequent treatment applications, including hyperthermia.

show abstract

Molecular Docking approach on the effect of Site- Selective and Site-Specific Drugs on the Molecular Interactions of Human Serum Albumin (HSA) -Acridinedione dye complex

Sreedevi

Vinod

Krishnan

et al. 2023

Arabian Journal of Chemistry

View full text Add to dashboard Cite

Comparative studies on biophysical interactions between 4-dicyanomethylene-2,6-dimethyl-4H-pyran (DDP) with bovine serum albumin (BSA) and human serum albumin (HSA) via photophysical approaches and molecular docking techniques

Cited by 8 publications

References 78 publications

Complexity of the Role of Various Site-Specific and Selective Sudlow Binding Site Drugs in the Energetics and Stability of the Acridinedione Dye–Bovine Serum Albumin Complex: A Molecular Docking Approach

Complexity of the Role of Various Site-Specific and Selective Sudlow Binding Site Drugs in the Energetics and Stability of the Acridinedione Dye–Bovine Serum Albumin Complex: A Molecular Docking Approach

Mechano-Chemistry across Phase Transitions in Heated Albumin Protein Solutions

Molecular Docking approach on the effect of Site- Selective and Site-Specific Drugs on the Molecular Interactions of Human Serum Albumin (HSA) -Acridinedione dye complex

Contact Info

Product

Resources

About