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New Fluorescence Probes for Biomolecules
Steady state fluorescence measurements have been used for the investigation of interaction between the bovine serum albumin (BSA) and fluorescence probes: 3-hydroxy-2,4-bis[(3-methyl-1,3-benzoxazol-2(3H)-ylidene)methyl]cyclobut-2-en-1-one (SQ6), 3-hydroxy-2,4-bis[(3-methyl-1,3-benzothiazol-2(3H)-yli...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6331984/ https://www.ncbi.nlm.nih.gov/pubmed/26205051 http://dx.doi.org/10.3390/molecules200713071 |
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author | Jurek, Katarzyna Kabatc, Janina Kostrzewska, Katarzyna Grabowska, Marlena |
author_facet | Jurek, Katarzyna Kabatc, Janina Kostrzewska, Katarzyna Grabowska, Marlena |
author_sort | Jurek, Katarzyna |
collection | PubMed |
description | Steady state fluorescence measurements have been used for the investigation of interaction between the bovine serum albumin (BSA) and fluorescence probes: 3-hydroxy-2,4-bis[(3-methyl-1,3-benzoxazol-2(3H)-ylidene)methyl]cyclobut-2-en-1-one (SQ6), 3-hydroxy-2,4-bis[(3-methyl-1,3-benzothiazol-2(3H)-ylidene)methyl]cyclobut-2-en-1-one (SQ7) and 3-hydroxy-2,4-bis[(1,3,3-trimethyl-1,3-dihydro-2H-indol-2-ylidene)methyl]cyclobut-2-en-1-one (SQ8). The binding constant between bovine serum albumin and squarine dyes has been determined by using both the Benesi-Hildebrand and Stern-Volmer equations. The negative value of free energy change indicates the existence of a spontaneous complexation process of BSA with squarine dyes. |
format | Online Article Text |
id | pubmed-6331984 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-63319842019-01-24 New Fluorescence Probes for Biomolecules Jurek, Katarzyna Kabatc, Janina Kostrzewska, Katarzyna Grabowska, Marlena Molecules Article Steady state fluorescence measurements have been used for the investigation of interaction between the bovine serum albumin (BSA) and fluorescence probes: 3-hydroxy-2,4-bis[(3-methyl-1,3-benzoxazol-2(3H)-ylidene)methyl]cyclobut-2-en-1-one (SQ6), 3-hydroxy-2,4-bis[(3-methyl-1,3-benzothiazol-2(3H)-ylidene)methyl]cyclobut-2-en-1-one (SQ7) and 3-hydroxy-2,4-bis[(1,3,3-trimethyl-1,3-dihydro-2H-indol-2-ylidene)methyl]cyclobut-2-en-1-one (SQ8). The binding constant between bovine serum albumin and squarine dyes has been determined by using both the Benesi-Hildebrand and Stern-Volmer equations. The negative value of free energy change indicates the existence of a spontaneous complexation process of BSA with squarine dyes. MDPI 2015-07-20 /pmc/articles/PMC6331984/ /pubmed/26205051 http://dx.doi.org/10.3390/molecules200713071 Text en © 2015 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Jurek, Katarzyna Kabatc, Janina Kostrzewska, Katarzyna Grabowska, Marlena New Fluorescence Probes for Biomolecules |
title | New Fluorescence Probes for Biomolecules |
title_full | New Fluorescence Probes for Biomolecules |
title_fullStr | New Fluorescence Probes for Biomolecules |
title_full_unstemmed | New Fluorescence Probes for Biomolecules |
title_short | New Fluorescence Probes for Biomolecules |
title_sort | new fluorescence probes for biomolecules |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6331984/ https://www.ncbi.nlm.nih.gov/pubmed/26205051 http://dx.doi.org/10.3390/molecules200713071 |
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