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

[Image: see text] 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 N...

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Autores principales: Bhunia, Soumyadip, Kumar, Sumit, Purkayastha, Pradipta
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2019
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6648241/
https://www.ncbi.nlm.nih.gov/pubmed/31459491
http://dx.doi.org/10.1021/acsomega.8b03213
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author Bhunia, Soumyadip
Kumar, Sumit
Purkayastha, Pradipta
author_facet Bhunia, Soumyadip
Kumar, Sumit
Purkayastha, Pradipta
author_sort Bhunia, Soumyadip
collection PubMed
description [Image: see text] 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.
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spelling pubmed-66482412019-08-27 Application of Photoinduced Electron Transfer with Copper Nanoclusters toward Finding Characteristics of Protein Pockets Bhunia, Soumyadip Kumar, Sumit Purkayastha, Pradipta ACS Omega [Image: see text] 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. American Chemical Society 2019-02-01 /pmc/articles/PMC6648241/ /pubmed/31459491 http://dx.doi.org/10.1021/acsomega.8b03213 Text en Copyright © 2019 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Bhunia, Soumyadip
Kumar, Sumit
Purkayastha, Pradipta
Application of Photoinduced Electron Transfer with Copper Nanoclusters toward Finding Characteristics of Protein Pockets
title Application of Photoinduced Electron Transfer with Copper Nanoclusters toward Finding Characteristics of Protein Pockets
title_full Application of Photoinduced Electron Transfer with Copper Nanoclusters toward Finding Characteristics of Protein Pockets
title_fullStr Application of Photoinduced Electron Transfer with Copper Nanoclusters toward Finding Characteristics of Protein Pockets
title_full_unstemmed Application of Photoinduced Electron Transfer with Copper Nanoclusters toward Finding Characteristics of Protein Pockets
title_short Application of Photoinduced Electron Transfer with Copper Nanoclusters toward Finding Characteristics of Protein Pockets
title_sort application of photoinduced electron transfer with copper nanoclusters toward finding characteristics of protein pockets
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6648241/
https://www.ncbi.nlm.nih.gov/pubmed/31459491
http://dx.doi.org/10.1021/acsomega.8b03213
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