Fostering protein-calixarene interactions: from molecular recognition to sensing

Bibliographic Details
Main Author: Prata, José Virgílio
Publication Date: 2016
Other Authors: D. Barata, Patrícia
Format: Article
Language: eng
Source: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Download full: http://hdl.handle.net/10400.21/7270
Summary: Two isomeric bis-calixarene-carbazole conjugates (CCC-1 and CCC-2) endowed with carboxylic acid functions at their lower rims have been found to display a high sensing ability (KSV up to 6 x 10(7) M-1) and selectivity toward cytochrome c, a multi-functional protein, in an aqueous-based medium. After targeting basic amino acid residues on the protein surface residing near the prosthetic heme group through electrostatic and hydrophobic interactions, a rapid photoinduced electron transfer ensues between the integrated transduction element (aryleneethynylene chromophore) of CCCs and the iron-oxidized heme of cytochrome c, enabling direct detection of the protein at nanomolar levels. Our results show that CCCs are capable of efficiently discriminating heme proteins (cytochrome c vs. myoglobin) and non-heme proteins (lysozyme) in an aqueous medium. Studies performed in two solvent systems (organic and aqueous) strongly suggest that in an organic medium a Forster-type resonance energy transfer is responsible for the observed reduction in CCCs emission upon contact with heme proteins while in an aqueous medium a specific photoinduced electron transfer mechanism prevails.
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spelling Fostering protein-calixarene interactions: from molecular recognition to sensingTwo isomeric bis-calixarene-carbazole conjugates (CCC-1 and CCC-2) endowed with carboxylic acid functions at their lower rims have been found to display a high sensing ability (KSV up to 6 x 10(7) M-1) and selectivity toward cytochrome c, a multi-functional protein, in an aqueous-based medium. After targeting basic amino acid residues on the protein surface residing near the prosthetic heme group through electrostatic and hydrophobic interactions, a rapid photoinduced electron transfer ensues between the integrated transduction element (aryleneethynylene chromophore) of CCCs and the iron-oxidized heme of cytochrome c, enabling direct detection of the protein at nanomolar levels. Our results show that CCCs are capable of efficiently discriminating heme proteins (cytochrome c vs. myoglobin) and non-heme proteins (lysozyme) in an aqueous medium. Studies performed in two solvent systems (organic and aqueous) strongly suggest that in an organic medium a Forster-type resonance energy transfer is responsible for the observed reduction in CCCs emission upon contact with heme proteins while in an aqueous medium a specific photoinduced electron transfer mechanism prevails.RCIPLPrata, José VirgílioD. Barata, Patrícia2017-07-13T11:09:28Z20162016-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.21/7270engPRATA, José V.; BARATA, Patrícia D. - Fostering protein-calixarene interactions: from molecular recognition to sensing. RSC ADVANCES. ISSN 2046-2069. Vol. 6, N.º 2, (2016), pp. 1659-16692046-206910.1039/c5ra19887metadata only accessinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-08-03T09:53:06Zoai:repositorio.ipl.pt:10400.21/7270Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:16:15.175216Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Fostering protein-calixarene interactions: from molecular recognition to sensing
title Fostering protein-calixarene interactions: from molecular recognition to sensing
spellingShingle Fostering protein-calixarene interactions: from molecular recognition to sensing
Prata, José Virgílio
title_short Fostering protein-calixarene interactions: from molecular recognition to sensing
title_full Fostering protein-calixarene interactions: from molecular recognition to sensing
title_fullStr Fostering protein-calixarene interactions: from molecular recognition to sensing
title_full_unstemmed Fostering protein-calixarene interactions: from molecular recognition to sensing
title_sort Fostering protein-calixarene interactions: from molecular recognition to sensing
author Prata, José Virgílio
author_facet Prata, José Virgílio
D. Barata, Patrícia
author_role author
author2 D. Barata, Patrícia
author2_role author
dc.contributor.none.fl_str_mv RCIPL
dc.contributor.author.fl_str_mv Prata, José Virgílio
D. Barata, Patrícia
description Two isomeric bis-calixarene-carbazole conjugates (CCC-1 and CCC-2) endowed with carboxylic acid functions at their lower rims have been found to display a high sensing ability (KSV up to 6 x 10(7) M-1) and selectivity toward cytochrome c, a multi-functional protein, in an aqueous-based medium. After targeting basic amino acid residues on the protein surface residing near the prosthetic heme group through electrostatic and hydrophobic interactions, a rapid photoinduced electron transfer ensues between the integrated transduction element (aryleneethynylene chromophore) of CCCs and the iron-oxidized heme of cytochrome c, enabling direct detection of the protein at nanomolar levels. Our results show that CCCs are capable of efficiently discriminating heme proteins (cytochrome c vs. myoglobin) and non-heme proteins (lysozyme) in an aqueous medium. Studies performed in two solvent systems (organic and aqueous) strongly suggest that in an organic medium a Forster-type resonance energy transfer is responsible for the observed reduction in CCCs emission upon contact with heme proteins while in an aqueous medium a specific photoinduced electron transfer mechanism prevails.
publishDate 2016
dc.date.none.fl_str_mv 2016
2016-01-01T00:00:00Z
2017-07-13T11:09:28Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10400.21/7270
url http://hdl.handle.net/10400.21/7270
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv PRATA, José V.; BARATA, Patrícia D. - Fostering protein-calixarene interactions: from molecular recognition to sensing. RSC ADVANCES. ISSN 2046-2069. Vol. 6, N.º 2, (2016), pp. 1659-1669
2046-2069
10.1039/c5ra19887
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