<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>7(46)</volume><submitter>Packirisamy V</submitter><pubmed_abstract>A facile synthesis of glutathione-stabilized copper nanoclusters (CuNCs) is carried out in H&lt;sub>2&lt;/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&lt;sub>12&lt;/sub>(SG)&lt;sub>9&lt;/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</pubmed_abstract><journal>ACS omega</journal><pagination>42550-42559</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9685744</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Interaction of Atomically Precise Thiolated Copper Nanoclusters with Proteins: A Comparative Study.</pubmed_title><pmcid>PMC9685744</pmcid><pubmed_authors>Packirisamy V</pubmed_authors><pubmed_authors>Pandurangan P</pubmed_authors></additional><is_claimable>false</is_claimable><name>Interaction of Atomically Precise Thiolated Copper Nanoclusters with Proteins: A Comparative Study.</name><description>A facile synthesis of glutathione-stabilized copper nanoclusters (CuNCs) is carried out in H&lt;sub>2&lt;/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&lt;sub>12&lt;/sub>(SG)&lt;sub>9&lt;/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</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Nov</publication><modification>2025-04-04T19:51:11.335Z</modification><creation>2025-04-04T19:51:11.335Z</creation></dates><accession>S-EPMC9685744</accession><cross_references><pubmed>36440105</pubmed><doi>10.1021/acsomega.2c06011</doi></cross_references></HashMap>