Fostering protein-calixarene interactions: from molecular recognition to sensing
Main Author: | |
---|---|
Publication Date: | 2016 |
Other Authors: | |
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. |
id |
RCAP_18eab3c2b15eafc925a8bed6806be973 |
---|---|
oai_identifier_str |
oai:repositorio.ipl.pt:10400.21/7270 |
network_acronym_str |
RCAP |
network_name_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository_id_str |
7160 |
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 |
dc.rights.driver.fl_str_mv |
metadata only access info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
metadata only access |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
|
_version_ |
1799133421993197568 |