{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["7(46)"],"submitter":["Packirisamy V"],"pubmed_abstract":["A facile synthesis of glutathione-stabilized copper nanoclusters (CuNCs) is carried out in H<sub>2</sub>O/ tetrahydrofuran medium. The photophysical and morphological studies performed with as-synthesized CuNCs revealed the formation of green-emissive, stable, and smaller nanoclusters. The precise composition of these as-synthesized CuNCs was predicted with the aid of electrospray ionization mass spectrometry analysis as Cu<sub>12</sub>(SG)<sub>9</sub>. Furthermore, the systematic studies of the interaction of synthesized CuNCs with three plasmatic proteins, namely, bovine serum albumin (BSA), lysozyme (Lys), and hemoglobin (Hb) have been performed by using a series of spectroscopic studies. The conformational changes in these proteins upon interacting with CuNCs and their binding stoichio"],"journal":["ACS omega"],"pagination":["42550-42559"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9685744"],"repository":["biostudies-literature"],"pubmed_title":["Interaction of Atomically Precise Thiolated Copper Nanoclusters with Proteins: A Comparative Study."],"pmcid":["PMC9685744"],"pubmed_authors":["Packirisamy V","Pandurangan P"],"additional_accession":[]},"is_claimable":false,"name":"Interaction of Atomically Precise Thiolated Copper Nanoclusters with Proteins: A Comparative Study.","description":"A facile synthesis of glutathione-stabilized copper nanoclusters (CuNCs) is carried out in H<sub>2</sub>O/ tetrahydrofuran medium. The photophysical and morphological studies performed with as-synthesized CuNCs revealed the formation of green-emissive, stable, and smaller nanoclusters. The precise composition of these as-synthesized CuNCs was predicted with the aid of electrospray ionization mass spectrometry analysis as Cu<sub>12</sub>(SG)<sub>9</sub>. Furthermore, the systematic studies of the interaction of synthesized CuNCs with three plasmatic proteins, namely, bovine serum albumin (BSA), lysozyme (Lys), and hemoglobin (Hb) have been performed by using a series of spectroscopic studies. The conformational changes in these proteins upon interacting with CuNCs and their binding stoichio","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Nov","modification":"2025-04-04T19:51:11.335Z","creation":"2025-04-04T19:51:11.335Z"},"accession":"S-EPMC9685744","cross_references":{"pubmed":["36440105"],"doi":["10.1021/acsomega.2c06011"]}}