Influence of the Global Charge of the Protein on the Stability of Lysozyme–AuNP Bioconjugates

Cárdenas, Betzhy; Sánchez-Obrero, Guadalupe; Madueño, Rafael; Sevilla, José Manuel; Blázquez, Manuel; Pineda, Teresa

doi:10.1021/jp505301h

Cited by 15 publications

(30 citation statements)

References 47 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The result from fluorescence lifetime measurement clearly indicates the formation of ground-state complexation between lysozyme and TBO. Furthermore, the observed results from time-resolved fluorescence studies correlate well with results from steady state emission quenching experiments (64,68,69). Equations (5) and (6) K SV * (910 5 dm 3 mol 1 ) K q * (910 13…”

Section: Fluorescence Lifetime Measurementsupporting

confidence: 74%

Elucidation of Binding Mechanism of Photodynamic Therapeutic Agent Toluidine Blue O with Chicken Egg White Lysozyme by Spectroscopic and Molecular Dynamics Studies

Shanmugaraj

Umadevi

Lakshmipathi

et al. 2017

Photochem & Photobiology

View full text Add to dashboard Cite

The nature of binding mechanism of toluidine blue O (TBO) with chicken egg white lysozyme was studied comprehensively by various spectroscopic and computational methods. Both steady state and time-resolved fluorescence studies unambiguously point to the prevalence of static quenching mechanism in lysozyme-TBO system. Thermodynamic parameters revealed that the association of TBO with lysozyme was a spontaneous process in which hydrophobic and hydrogen bond interactions played a pivotal role in the binding process. The secondary and tertiary conformational changes of lysozyme in the presence of TBO were unraveled using absorption, Fourier transform infrared spectroscopy (FT-IR) and circular dichroism (CD) techniques. Molecular docking studies of lysozyme-TBO system substantiated the findings of site marker experiment and revealed TBO adjacent to Trp-63 and Trp-108 residues of lysozyme. Molecular dynamics (MD) simulation studies of lysozyme-TBO system indicate a stable and effective complexation of TBO with lysozyme. It is hoped that the results presented here will enable further understanding of TBO toxicity.

show abstract

Section: Fluorescence Lifetime Measurementsupporting

confidence: 74%

Elucidation of Binding Mechanism of Photodynamic Therapeutic Agent Toluidine Blue O with Chicken Egg White Lysozyme by Spectroscopic and Molecular Dynamics Studies

Shanmugaraj

Umadevi

Lakshmipathi

et al. 2017

Photochem & Photobiology

View full text Add to dashboard Cite

show abstract

“…However, others have suggested that neither protein size nor charge significantly determine the protein fingerprints, confirming that electrostatic affinity alone does not constitute the major driving force regulating the silica-corona interactions. 41 …”

Section: Resultsmentioning

confidence: 99%

Protein Adsorption From Biofluids on Silica Nanoparticles: Corona Analysis as a Function of Particle Diameter and Porosity

Clemments

Botella

Landry

2015

ACS Appl. Mater. Interfaces

View full text Add to dashboard Cite

A study on the adsorption of proteins from fetal bovine serum (FBS) on spherical dense and mesoporous silica nanoparticles with a wide range of diameters, from 70 to 900 nm, is presented. Monodisperse populations of particles with a range of diameters were obtained through modifications of the Stöber method. Extensive characterization of the particles was then performed using N2 physisorption, TEM, DLS, and ζ-potential. Following serum exposure, proteomic evaluation in concert with thermogravimetric analysis revealed the associated concentrations of each protein identified in the hard corona. Small particles adsorbed the largest amount of protein, due to their larger external surface area. Proteins with low molecular weights (<50 kDa) composed the majority of the protein corona, totaling between 60 and 80 % of the total mass of adsorbed protein. Here, the higher surface curvature of small particles favors the enrichment of smaller proteins. Porosity does not promote protein adsorption, but improves deposition of the low molecular weight protein fraction due to the size exclusion effect related to pore diameter. These results have important implications for the use of dense and porous silica nanoparticles in biomedical applications.

show abstract

“…From the time-resolved fluorescence decay profiles of Lys in the absence and presence of chelerythrine (not shown) the fluorescence lifetime values and their amplitudes were calculated. [61][62][63] Steady-state fluorescence anisotropy study Steady state anisotropy data may provide valuable information on the degree of motional restriction of the fluorophore and is used as a probe to assess the extent of the flexibility or tumbling motion of small molecules after binding. After adding the maximum concentration of the chelerythrine iminium and alkanolamine forms (100 mM) to Lyz, the observed average fluorescence lifetime values were t = 1.81 ns and 2.07 ns, respectively.…”

Section: Fluorescence Lifetime Studymentioning

confidence: 99%

Chelerythrine–lysozyme interaction: spectroscopic studies, thermodynamics and molecular modeling exploration

Jash

Basu

Payghan

et al. 2015

Phys. Chem. Chem. Phys.

View full text Add to dashboard Cite

The binding of the iminium and alkanolamine forms of chelerythrine to lysozyme (Lyz) was investigated by spectroscopy and docking studies. The thermodynamics of the binding was studied by calorimetry. Spectroscopic evidence suggested that Trp-62 and Trp-63 in the β-domain of the protein are closer to the binding site; moreover, the binding site was at a distance of 2.27 and 2.00 nm from the iminium and alkanolamine forms, respectively, according to the Forster theory of non-radiation energy transfer. The equilibrium binding constants for the iminium and alkanolamine forms at 298 K were evaluated to be 1.29 × 10(5) and 7.79 × 10(5) M(-1), respectively. The binding resulted in an alteration of the secondary structure of the protein with a distinct reduction of the helical organization. The binding of iminium was endothermic, involving electrostatic and hydrophobic interactions, while that of alkanolamine form was exothermic and dominated by hydrogen bonding interactions. Docking studies provided the atomistic details pertaining to the binding of both forms of chelerythrine and supported the higher binding in favour of the alkanolamine over the iminium. Furthermore, molecular dynamics study provided accurate insights regarding the binding of both chelerythrine forms in accordance with the experimental results obtained. Chelerythrine binding pocket involves the catalytic region and aggregation prone K-peptide region, which are sandwiched between one another. Overall, these results suggest that both the forms of the alkaloid bind to the protein but the neutral form has higher affinity than the cationic form.

show abstract

Influence of the Global Charge of the Protein on the Stability of Lysozyme–AuNP Bioconjugates

Cited by 15 publications

References 47 publications

Elucidation of Binding Mechanism of Photodynamic Therapeutic Agent Toluidine Blue O with Chicken Egg White Lysozyme by Spectroscopic and Molecular Dynamics Studies

Elucidation of Binding Mechanism of Photodynamic Therapeutic Agent Toluidine Blue O with Chicken Egg White Lysozyme by Spectroscopic and Molecular Dynamics Studies

Protein Adsorption From Biofluids on Silica Nanoparticles: Corona Analysis as a Function of Particle Diameter and Porosity

Chelerythrine–lysozyme interaction: spectroscopic studies, thermodynamics and molecular modeling exploration

Contact Info

Product

Resources

About