Data for β-lactoglobulin conformational analysis after (-)-epigallocatechin gallate and metal ions binding

Zhang, Liangliang; Sahu, Indra D.; Xu, Man; Wang, Yongmei

doi:10.1016/j.dib.2016.12.021

Cited by 6 publications

(2 citation statements)

References 5 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Figure 6 depicted the CD spectra of BSA in absence as well as in the presence of BrNs in various ratios. CD spectra is manifested with two significant negative peaks centered on 209 nm and 222 nm in the UV region which revealed the n → π* shift of peptide bond, characteristic of α-helix structure 47 – 50 . When BrNs is used in 1:1 ratio 209 peak abruptly vanished along with the shift of 222 nm peak towards longer wavelength.…”

Section: Resultsmentioning

confidence: 99%

Mechanistic Interaction Study of Bromo-Noscapine with Bovine Serum Albumin employing Spectroscopic and Chemoinformatics Approaches

Sood

Kumar

Rathee

et al. 2018

Sci Rep

View full text Add to dashboard Cite

Bromo-Noscapine (BrNs) is a tubulin-binding cytotoxic agent with significant activity against breast and lung cancer. The mechanistic interaction insight into the binding of bovine serum albumin (BSA) with BrNs can provide critical information about the pharmacodynamics and pharmacokinetics properties. Here, various spectroscopic techniques and computational methods were employed to understand the dynamics of BrNs and BSA interaction. The intrinsic fluorescence of BSA was quenched by BrNs through a static quenching procedure. The stoichiometry of BrNs-BSA complex was 1:1 and binding constant of the complex was in the order of 103 M−1 at 298 K. Based on thermodynamic analysis, it was deduced that binding process of the BrNs with BSA was spontaneous and exothermic, and the major forces between BrNs and BSA were van der waals forces and hydrogen bonding. Moreover, results of FT-IR, CD, UV spectra concluded significant conformational change in BSA on binding with BrNs. The in vitro findings were further confirmed by in silico assays. Molecular docking showed strong interactions with score of −8.08 kcal/mol. Molecular dynamics simulation analysis also suggested the stable binding with lower deviation in RMSD and RMSF values through persistent long simulation run. This study suggests optimal efficiency of diffusion of the BrNs into the bloodstream for the treatment of cancer.

show abstract

Section: Resultsmentioning

confidence: 99%

Mechanistic Interaction Study of Bromo-Noscapine with Bovine Serum Albumin employing Spectroscopic and Chemoinformatics Approaches

Sood

Kumar

Rathee

et al. 2018

Sci Rep

View full text Add to dashboard Cite

show abstract

“…The intermolecular and intramolecular interactions involved in the protein secondary structure stability are affected upon binding with ligands or drug molecules (Varshney et al, 2014;Thakur et al, 2017). CD spectra is established with one positive spectra on 195 nm and two significant negative peaks centered on 209 nm and 222 nm in the far-UV region due to the n → π* transition that shifts the peptide bond, which is characteristic of α-helix structure (Varlan and Hillebrand, 2010;Rogozea, 2012;Suryawashi, 2016;Zhang et at., 2016). To corroborate the fluorescence and ITC studies for kanamycin binding to TolC protein, CD measurements of TolC protein were carried out to observed the conformational behavior in the presence and absence of kanamycin.…”

Section: Measurementsmentioning

confidence: 99%

Kanamycin-Mediated Conformational Dynamics of Escherichia coli Outer Membrane Protein TolC

Pattanayak

Dehury

Priyadarshinee

et al. 2021

Front. Mol. Biosci.

View full text Add to dashboard Cite

TolC is a member of the outer membrane efflux proteins (OEPs) family and acts as an exit duct to export proteins, antibiotics, and substrate molecules across the Escherichia coli cell membrane. Export of these molecules is evidenced to be brought about through the reversible interactions and binding of substrate-specific drug molecules or antibiotics with TolC and by being open for transport, which afterward leads to cross-resistance. Hence, the binding of kanamycin with TolC was monitored through molecular docking (MD), the structural fluctuations and conformational changes to the atomic level. The results were further supported from the steady-state fluorescence binding and isothermal titration calorimetry (ITC) studies. Binding of kanamycin with TolC resulted in a concentration dependent fluorescence intensity quenching with 7 nm blue shift. ITC binding data maintains a single binding site endothermic energetic curve with binding parameters indicating an entropy driven binding process. The confirmational changes resulting from this binding were monitored by a circular dichroism (CD) study, and the results showed insignificant changes in the α-helix and β-sheets secondary structure contents, but the tertiary structure shows inclusive changes in the presence of kanamycin. The experimental data substaintially correlates the RMSD, Rg, and RMSF results. The resulting conformational changes of the TolC-kanamycin complexation was stabilized through H-bonding and other interactions.

show abstract

Effect of different doses of Co-60 gamma-ray irradiation treatment on the micro-rheological and emulsifying properties of liquid egg white

Liu

Zhang

et al. 2020

Colloids and Surfaces A: Physicochemical and Engineering Aspect

View full text Add to dashboard Cite

Data for β-lactoglobulin conformational analysis after (-)-epigallocatechin gallate and metal ions binding

Cited by 6 publications

References 5 publications

Mechanistic Interaction Study of Bromo-Noscapine with Bovine Serum Albumin employing Spectroscopic and Chemoinformatics Approaches

Mechanistic Interaction Study of Bromo-Noscapine with Bovine Serum Albumin employing Spectroscopic and Chemoinformatics Approaches

Kanamycin-Mediated Conformational Dynamics of Escherichia coli Outer Membrane Protein TolC

Effect of different doses of Co-60 gamma-ray irradiation treatment on the micro-rheological and emulsifying properties of liquid egg white

Contact Info

Product

Resources

About