Copper(I) oxide nanoparticle and tryptophan as its biological conjugate: a modulation of cytotoxic effects

Maity, Mritunjoy; Pramanik, Sumit Kumar; Pal, Uttam; Banerji, Biswadip; Maiti, Nakul C.

doi:10.1007/s11051-013-2179-z

Cited by 12 publications

(10 citation statements)

References 46 publications

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“…1-2 and Table-1) implies minor conformational changes induced by CeO2 nanoparticles on the structure of BSA. Conformational changes were observed when CeO2 nanoparticles interacted with BSA [37], HSA [38], heme protein [39], BSA interacted with cerium [40], copper(I) oxide nanoparticles [41], Al2O3 nanoparticles [26], ZnO nanoparticles [20], CdO nanoparticles [42], TiO2 nanoparticles [36] and tin oxide nanoparticles [35].…”

Section: Resultsmentioning

confidence: 99%

Spectroscopic Studies of Interaction of Protein with Cerium Oxide Nanoparticles

Abraham¹

2018

Asian J. Chem.

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Section: Resultsmentioning

confidence: 99%

Spectroscopic Studies of Interaction of Protein with Cerium Oxide Nanoparticles

Abraham¹

2018

Asian J. Chem.

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“…Increased concentrations of Copper (I) oxide NPs and gold NPs in BSA resulted in a decrease in fluorescence intensity due to quenching [22,13]. Quenching of the intrinsic fluorescence of BSA with a blue shift in emission maximum was reported during the interaction studies of BSA with increasing concentrations of ZnO NPs [23], Cu NPs [24,25], silver NPs [26] and colloidal capped CdS NPs [27].…”

Section: Tem Studymentioning

confidence: 96%

Interaction of Copper Oxide Nanoparticles With Bovine Serum Albumin by Spectroscopic Studies

Abraham

Parthasarathy

2018

Int J Pharm Pharm Sci

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Objective: Since structural changes of adsorbed protein are necessary for cellular uptake of nanoparticles (NPs) it is of prime importance to know about structural changes of bovine serum albumin (BSA) when it interacts with CuO NPs-a potential new antitumor drug.Methods: CuO NPs prepared by sol-gel technique were characterized by x-ray diffraction (XRD) and tunneling electron microscope (TEM) techniques. The conformational changes induced by CuO NPs on BSA were studied by various spectroscopic techniques such as steady state and time-resolved fluorescence measurements. The changes in fluorescence emission parameters such as fluorescence intensity, fluorescence emission maximum and lifetimes of fluorescent residues in BSA were studied.Results: XRD analysis showed the average particle size as 32 nm. The TEM micrograph showed particles of different size varying from 10 to 45 nm. Fluorescence quenching was confirmed due to a decrease in fluorescence intensity of CuO NPs-BSA complex. The analysis of lifetime measurements indicated BSA contained two tryptophan (trp) residues that fluoresced in different environments. Static quenching mechanism was confirmed by time-resolved measurements when BSA interacted with CuO NPs. Conclusion:Minor structural changes of BSA protein were observed during the interaction studies.

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“…Some reports used shaped controlled nanoparticles (Maity et al 2014, prepared by using PVP as CA (Zhang et al (111) face. It was observed that the amine groups are responsible for the bonding of the L-Trp because the bands in FTIR spectra related to -NH 2 modes were shifted (Maity et al 2014).…”

Section: Amino Acid Interaction With Cu 2 Omentioning

confidence: 99%

“…It was observed that the amine groups are responsible for the bonding of the L-Trp because the bands in FTIR spectra related to -NH 2 modes were shifted (Maity et al 2014). In the case of L-Tyr , impedance measurements were performed, and Nyquist plots were interpreted as an indication of the amino acid adsorption, and octahedra were found to be more electroactive than spherical nanoparticles.…”

Section: Amino Acid Interaction With Cu 2 Omentioning

confidence: 99%

The long and successful journey of electrochemically active amino acids. From fundamental adsorption studies to potential surface engineering tools.

Dourado

Pastrián

Torresi

2018

An. Acad. Bras. Ciênc.

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Proteins have been the subject of electrochemical studies. It is possible to apply electrochemical techniques to obtain information about their structure due to the presence of five electroactive amino acids that can be oriented to the outside of the peptidic chain. These amino acids are L-and L-Cysteine (L-Cys); their electrochemical behavior being subject of extensive research, but it is still controversial. No spectroscopic investigations have been reported on L-Trp, and due to the short life time of the intermediates, ex situ techniques cannot be employed, leading to a never-ending discussion about possible intermediates. In the L-Tyr and L-His cases, spectroelectrochemical studies were performed and different intermediates were observed, suggesting that some intermediates may be observed under specific conditions, as proposed for L-Cys. This amino acid is the most interesting among the electroactive ones because of the presence of a thiol moiety at its side chain, leading to a wide range of oxidation states. It can adsorb onto surfaces of different crystallographic orientation in stereoselective conformation, modifying the surface for different applications.as a surface engineering tool since it plays the role of as an anchor for the growing of nanocrystals inside proteic templates.

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Copper(I) oxide nanoparticle and tryptophan as its biological conjugate: a modulation of cytotoxic effects

Cited by 12 publications

References 46 publications

Spectroscopic Studies of Interaction of Protein with Cerium Oxide Nanoparticles

Spectroscopic Studies of Interaction of Protein with Cerium Oxide Nanoparticles

Interaction of Copper Oxide Nanoparticles With Bovine Serum Albumin by Spectroscopic Studies

The long and successful journey of electrochemically active amino acids. From fundamental adsorption studies to potential surface engineering tools.

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