Exploring the interaction of l-cysteine capped CuS nanoparticles with bovine serum albumin (BSA): a spectroscopic study

Abstract

The interactions between nanoparticles and proteins have prime importance in nanomedicine and nanotoxicology. L-cysteine capped copper sulfide (Cy-CuS) nanoparticles having average particle size of 6 nm have been synthesized using chemical coprecipitation method and their interactions with Bovine Serum Albumin (BSA) were explored using various spectroscopic techniques. A ground state complex is formed between BSA and Cy-CuS nanoparticles in solution. The number of binding sites, binding constant, quenching constant and the binding distance between Cy-CuS nanoparticles and BSA were determined. The overall conformation of BSA in the complex was unaltered, however the α-helical content of BSA was marginally reduced.

Newly synthesized Cu(II) pyrazino[2,3‐f][1,10]phenanthroline complexes as potential anticancer candidates

“…But a reasonable estimate of the binding position could be made from the FRET study which indicates that the distance between the complexes and protein is about 1.46 nm for complex 1 , 1.66 nm for complex 2 and 1.78 nm for complex 3 . This indicates that the lower r value means a closer distance between BSA and complexes 1 – 3 and therefore we can suggest that these complexes bind near BSA …”

Enzymatic biomineralization of biocompatible CuInS2, (CuInZn)S2and CuInS2/ZnS core/shell nanocrystals for bioimaging

“…This process is analogous to the chemical route to aqueous phase sulfide mineralization whereby reactive Na2S is added to induce mineralization of, for example, Cu2−xS. 37 The formation of nanoparticles, as opposed to bulk materials, is due to (i) the presence of the L-cysteine which can act as a capping agent, 38,39 and (ii) the templating ability of the CSE enzyme itself. 28 Unfortunately, no corresponding fluorescence peak could be observed due to a very low fluorescence inten-sity.…”

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

“…In this perspective, it is relevant to mention that there are several studies reported on the interaction between proteins and nanomaterials, such as quantum dots, − metal nanoparticles, ,− metal nanoclusters, − graphene quantum dots, and carbon-based nanoparticles. , In these works, it has been demonstrated that protein–NPs interaction mainly mediated through the formation of either protein–NPs complex or “protein corona”. ,,,,, The observation of the above studies is interpreted by analyzing binding constants, number of binding sites, protein conformational change, hydrodynamic size alteration, etc. ,, Interestingly, some studies have also shown that the size of nanoparticle and surface ligands can have a profound influence on the protein–NPs interaction event. In this context, Nyokong and co-workers while working on the interaction between different CdTe QDs capped with various thiol ligands with protein have found that the binding affinity of those QDs with protein can vary significantly with a change in the nature of thiol ligands, signifying the important role of surface chemistry in these interactions.…”

“…26,30,31,34,35,37 The observation of the above studies is interpreted by analyzing binding constants, number of binding sites, protein conformational change, hydrodynamic size alteration, etc. 29,31,33 Interestingly, some studies have also shown that the size of nanoparticle and surface ligands can have a profound influence on the protein− NPs interaction event. In this context, Nyokong and coworkers 27 while working on the interaction between different CdTe QDs capped with various thiol ligands with protein have found that the binding affinity of those QDs with protein can vary significantly with a change in the nature of thiol ligands, signifying the important role of surface chemistry in these interactions.…”