dc.creator | Jameson, Laramie P. | |
dc.creator | Smith, Nicholas W. | |
dc.creator | Annunziata, Onofrio | |
dc.creator | Dzyuba, Sergei V. | |
dc.date.accessioned | 2016-08-03T21:49:55Z | |
dc.date.available | 2016-08-03T21:49:55Z | |
dc.date.issued | 2016-05-09 | |
dc.identifier.uri | https://doi.org/10.1039/C6CP00420B | |
dc.identifier.uri | https://repository.tcu.edu/handle/116099117/11220 | |
dc.identifier.uri | https://pubs.rsc.org/en/Content/ArticleLanding/2016/CP/C6CP00420B | |
dc.description.abstract | The fluorescence of BODIPY and click-BODIPY dyes was found to substantially increase in the presence of bovine serum albumin (BSA). BSA acted as a solubilizer for dye aggregates, in addition to being a conventional binding scaffold for the click-BODIPY dyes, indicating that disaggregation of fluorophores should be considered when evaluating dye-protein interactions. | |
dc.language.iso | en | en_US |
dc.publisher | The Royal Society of Chemistry | |
dc.rights.uri | https://creativecommons.org/licenses/by/3.0/ | |
dc.source | Physical Chemistry Chemical Physics | |
dc.subject | design | |
dc.subject | probes | |
dc.title | Interaction of BODIPY dyes with bovine serum albumin: a case study on the aggregation of a click-BODIPY dye | |
dc.type | Article | |
dc.rights.holder | Jameson et al. | |
dc.rights.license | CC BY 3.0 | |
local.college | College of Science and Engineering | |
local.department | Chemistry and Biochemistry | |
local.persons | All (CHEM) | |