<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Zamojc K</submitter><funding>National Science Center</funding><pagination>41</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8744808</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>23(1)</volume><pubmed_abstract>Due to the fact that surfactant molecules are known to alter the structure (and consequently the function) of a protein, protein-surfactant interactions are very important in the biological, pharmaceutical, and cosmetic industries. Although there are numerous studies on the interactions of albumins with surfactants, the investigations are often performed at fixed environmental conditions and limited to separate surface-active agents and consequently do not present an appropriate comparison between their different types and structures. In the present paper, the interactions between selected cationic, anionic, and nonionic surfactants, namely hexadecylpyridinium chloride (CPC), hexadecyltrimethylammonium bromide (CTAB), sodium dodecyl sulfate (SDS), polyethylene glycol sorbitan monolaurate, </pubmed_abstract><journal>International journal of molecular sciences</journal><pubmed_title>On the Effect of pH, Temperature, and Surfactant Structure on Bovine Serum Albumin-Cationic/Anionic/Nonionic Surfactants Interactions in Cacodylate Buffer-Fluorescence Quenching Studies Supported by UV Spectrophotometry and CD Spectroscopy.</pubmed_title><pmcid>PMC8744808</pmcid><funding_grant_id>2016/23/D/ST4/01576</funding_grant_id><pubmed_authors>Wyrzykowski D</pubmed_authors><pubmed_authors>Zamojc K</pubmed_authors><pubmed_authors>Chmurzynski L</pubmed_authors></additional><is_claimable>false</is_claimable><name>On the Effect of pH, Temperature, and Surfactant Structure on Bovine Serum Albumin-Cationic/Anionic/Nonionic Surfactants Interactions in Cacodylate Buffer-Fluorescence Quenching Studies Supported by UV Spectrophotometry and CD Spectroscopy.</name><description>Due to the fact that surfactant molecules are known to alter the structure (and consequently the function) of a protein, protein-surfactant interactions are very important in the biological, pharmaceutical, and cosmetic industries. Although there are numerous studies on the interactions of albumins with surfactants, the investigations are often performed at fixed environmental conditions and limited to separate surface-active agents and consequently do not present an appropriate comparison between their different types and structures. In the present paper, the interactions between selected cationic, anionic, and nonionic surfactants, namely hexadecylpyridinium chloride (CPC), hexadecyltrimethylammonium bromide (CTAB), sodium dodecyl sulfate (SDS), polyethylene glycol sorbitan monolaurate, </description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Dec</publication><modification>2025-04-21T16:48:43.424Z</modification><creation>2022-02-11T15:20:02.476Z</creation></dates><accession>S-EPMC8744808</accession><cross_references><pubmed>35008466</pubmed><doi>10.3390/ijms23010041</doi></cross_references></HashMap>