Characterizing optical properties, composition of stabilizer-free copper nanoclusters and its interaction with bovine serum albumin

Sahu, Dillip Kumar; Sahu, Kalyanasis

doi:10.1016/j.jphotochem.2017.07.002

Cited by 16 publications

(12 citation statements)

References 54 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The results indicate attachment of multiple Cu NCs to BSA, conforming with the proposed binding to multiple protein pockets. This result is contrary to that reported by Sahu et al 27 However, the attachment of the Cu NCs does not change the secondary structure of BSA appreciably as can be seen from the CD spectra (Figure S8). Moreover, the results indicate that binding of the Cu NCs is not restricted only to the surface hydrophilic pockets of BSA but also extends to the inner moderate and less hydrophilic ones.…”

Section: Resultscontrasting

confidence: 99%

“…The Cu NCs were found to readily interact with BSA. Unlike D. K. Sahu and K. Sahu, who synthesized 14-atom Cu NCs and studied their interaction with BSA inferring 1:1 binding, and Das et al, who reported adsorption of HSA on glutathione-protected Cu NCs, we could identify the protein pockets. Moreover, 1:1 and 1:2 host–guest binding in BSA can be well-understood from Benesi–Hildebrand double reciprocal plots. , On contrary to the reported protein–Cu NC studies, besides mere guest–host binding, we intended to look into the characteristics of the domain specific pockets in BSA.…”

Section: Resultsmentioning

confidence: 86%

“…A number of binding pockets of various sizes are present in the structure of BSA . The challenge to find the specific characteristic of the protein pockets of various hydroaffinities seems to have remained partly explored. , Interaction of copper nanocluster (Cu NC) probes with serum albumins have been reported on the formation of protein corona over the Cu NCs , and creating energy transfer antenna using HSA or l -cysteine (Cys)-protected Cu NCs. , A previous study on interaction of Cu NCs with BSA showed minor loss in the secondary structure . However, there is hardly any report on recognition of protein pockets by electron-transfer mechanism.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Application of Photoinduced Electron Transfer with Copper Nanoclusters toward Finding Characteristics of Protein Pockets

2019

View full text Add to dashboard Cite

Proteins possess various domains and subdomain pockets with varying hydrophobicity/hydrophilicity. The local polarities of these domains play a major role in oxidation–reduction-based biological processes. Herein, we have synthesized ultrasmall fluorescent copper nanoclusters (Cu NCs) that are directed to bind to the different domain-specific pockets of the model protein bovine serum albumins (BSA). Potential electron acceptors, methyl viologen (MV) derivatives, were chosen such that they specifically reach the various domains following their hydrophobicity/hydrophilicity. Here, we have used MV 2+ , HMV + , and DHMV 2+ , possessing hydrophilic, intermediate, and hydrophobic specificities. Being electron acceptors, these derivatives draw electrons from the Cu NCs through photoinduced electron transfer (PET). The rate of PET varies at the different domains of BSA based on the local environment which has been analyzed. Here, PET is confirmed by steady state as well as time-resolved fluorescence spectroscopy. This study would provide a measurable way to identify the location of the different domains of a protein which is scalable by changing the superficial conditions without unfolding the protein.

show abstract

Section: Resultscontrasting

confidence: 99%

Section: Resultsmentioning

confidence: 86%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Application of Photoinduced Electron Transfer with Copper Nanoclusters toward Finding Characteristics of Protein Pockets

2019

View full text Add to dashboard Cite

show abstract

“…Therefore, in the present study, we have thought to determine the stoichiometry of the binding events of CuNCs with BSA. For this purpose, the fluorescence data have been analyzed based on the modified Benesi–Hildebrand (B–H) double-reciprocal plot using eq for 1:1 (BSA:NCs) complexation and eq for 2:1 (BSA:NCs) complexation. ,− where F and F m are the fluorescence intensities of CuNCs with successive addition of BSA and maximum BSA concentrations, respectively, F 0 is the fluorescence intensity in the absence of BSA, and K is the equilibrium constant related to CuNCs and BSA association.…”

Section: Resultsmentioning

confidence: 99%

“…Surface charges of those CuNCs were determined by ζ-potential measurements, which are shown in Figure S2. For determining the number of Cu atoms in the metal core (Cu n ) of those nanoclusters, a model called jellium model has been used, which is shown in the Supporting Information. , …”

Section: Experimental Sectionmentioning

confidence: 99%

Probing the Interaction of Bovine Serum Albumin with Copper Nanoclusters: Realization of Binding Pathway Different from Protein Corona

et al. 2021

View full text Add to dashboard Cite

With an aim to understand the interaction mechanism of bovine serum albumin (BSA) with copper nanoclusters (CuNCs), three different types CuNCs having chemically different surface ligands, namely, tannic acid (TA), chitosan, and cysteine (Cys), have been fabricated, and investigations are carried out in the absence and presence of protein (BSA) at ensemble-averaged and single-molecule levels. The CuNCs, capped with different surface ligands, are consciously chosen so that the role of surface ligands in the overall protein− NCs interactions is clearly understood, but, more importantly, to find whether these CuNCs can interact with protein in a new pathway without forming the "protein corona", which otherwise has been observed in relatively larger nanoparticles when they are exposed to biological fluids. Analysis of the data obtained from fluorescence, ζ-potential, and ITC measurements has clearly indicated that the BSA protein in the presence of CuNCs does not attain the binding stoichiometry (BSA/CuNCs > 1) that is required for the formation of "protein corona". This conclusion is further substantiated by the outcome of the fluorescence correlation spectroscopy (FCS) study. Further analysis of data and thermodynamic calculations have revealed that the surface ligands of the CuNCs play an important role in the protein−NCs binding events, and they can alter the mode and thermodynamics of the process. Specifically, the data have demonstrated that the binding of BSA with TA-CuNCs and Chitosan-CuNCs follows two types of binding modes; however, the same with Cys-CuNCs goes through only one type of binding mode. Circular dichroism (CD) measurements have indicated that the basic structure of BSA remains almost unaltered in the presence of CuNCs. The outcome of the present study is expected to encourage and enable better application of NCs in biological applications.

show abstract

A Simple Approach to Design Proteins for the Sustainable Synthesis of Metal Nanoclusters

et al. 2019

View full text Add to dashboard Cite

Metal nanoclusters (NCs) are considered ideal nanomaterials for biological applications owing to their strong photoluminescence (PL), excellent photostability, and good biocompatibility. This study presents a simple and versatile strategy to design proteins, via incorporation of a di‐histidine cluster coordination site, for the sustainable synthesis and stabilization of metal NCs with different metal composition. The resulting protein‐stabilized metal NCs (Prot‐NCs) of gold, silver, and copper are highly photoluminescent and photostable, have a long shelf life, and are stable under physiological conditions. The biocompatibility of the clusters was demonstrated in cell cultures in which Prot‐NCs showed efficient cell internalization without affecting cell viability or losing luminescence. Moreover, the approach is translatable to other proteins to obtain Prot‐NCs for various biomedical applications such as cell imaging or labeling.

show abstract

Characterizing optical properties, composition of stabilizer-free copper nanoclusters and its interaction with bovine serum albumin

Cited by 16 publications

References 54 publications

Application of Photoinduced Electron Transfer with Copper Nanoclusters toward Finding Characteristics of Protein Pockets

Application of Photoinduced Electron Transfer with Copper Nanoclusters toward Finding Characteristics of Protein Pockets

Probing the Interaction of Bovine Serum Albumin with Copper Nanoclusters: Realization of Binding Pathway Different from Protein Corona

A Simple Approach to Design Proteins for the Sustainable Synthesis of Metal Nanoclusters

Contact Info

Product

Resources

About