Two Engineered OBPs with opposite temperature-dependent affinities towards 1-aminoanthracene
Autor(a) principal: | |
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Data de Publicação: | 2018 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/1822/56333 |
Resumo: | Engineered odorant-binding proteins (OBPs) display tunable binding affinities triggered by temperature alterations. We designed and produced two engineered proteins based on OBP-I sequence: truncated OBP (tOBP) and OBP::GQ20::SP-DS3. The binding affinity of 1-aminoanthracene (1-AMA) to these proteins revealed that tOBP presents higher affinity at 25°C (kd=0.45M) than at 37°C (kd=1.72M). OBP::GQ20::SP-DS3 showed an opposite behavior, revealing higher affinity at 37°C (kd=0.58M) than at 25°C (kd=1.17M). We set-up a system containing both proteins to evaluate their temperature-dependent binding. Our data proved the 1-AMA differential and reversible affinity towards OBPs, triggered by temperature changes. The variations of the binding pocket size with temperature, confirmed by molecular modelling studies, were determinant for the differential binding of the engineered OBPs. Herein we described for the first time a competitive temperature-dependent mechanism for this class of proteins. |
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Two Engineered OBPs with opposite temperature-dependent affinities towards 1-aminoanthraceneCiências Médicas::Biotecnologia MédicaScience & TechnologyEngineered odorant-binding proteins (OBPs) display tunable binding affinities triggered by temperature alterations. We designed and produced two engineered proteins based on OBP-I sequence: truncated OBP (tOBP) and OBP::GQ20::SP-DS3. The binding affinity of 1-aminoanthracene (1-AMA) to these proteins revealed that tOBP presents higher affinity at 25°C (kd=0.45M) than at 37°C (kd=1.72M). OBP::GQ20::SP-DS3 showed an opposite behavior, revealing higher affinity at 37°C (kd=0.58M) than at 25°C (kd=1.17M). We set-up a system containing both proteins to evaluate their temperature-dependent binding. Our data proved the 1-AMA differential and reversible affinity towards OBPs, triggered by temperature changes. The variations of the binding pocket size with temperature, confirmed by molecular modelling studies, were determinant for the differential binding of the engineered OBPs. Herein we described for the first time a competitive temperature-dependent mechanism for this class of proteins.This study was supported by the Portuguese Foundation for Science and Technology (FCT) under the scope of the strategic funding of UID/BIO/04469/2013 unit and COMPETE 2020 (POCI-01-0145-FEDER-006684). A.R. and F.G. thank FCT for funding their scholarships with the references SFRH/BPD/98388/2013 and SFRH/BD/114684/2016, respectively. T.G.C. thanks senior position funded by the European Union through the European Regional Development Fund (ERDF) under the Competitiveness Operational Program (COP-A1-A1.1.4-E nr.30/01.09.2016). C.S. thanks to the BioTecNorte operation (NORTE-01-0145-FEDER-000004) funded by European Regional Development Fund under the scope of Norte2020 - Programa Operacional Regional do Norte. Access to computing resources funded by the Project "Search-ON2: Revitalization of HPC infrastructure of UMinho" (NORTE-07-0162-FEDER-000086), co-funded by the North Portugal Regional Operational Programme (ON.2 - O Novo Norte), under the National Strategic Reference Framework (NSRF), through the European Regional Development Fund (ERDF), is also gratefully acknowledged.info:eu-repo/semantics/publishedVersionNature GroupUniversidade do MinhoGonçalves, Filipa Daniela GomesCastro, T.Azóia, Nuno G.Ribeiro, ArturSilva, Carla Manuela Pereira Marinho daCavaco-Paulo, Artur2018-10-042018-10-04T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/56333engGonçalves, Filipa D.; Castro, T.; Azoia, Nuno G.; Ribeiro, Artur; Silva, Carla; Cavaco-Paulo, Artur, Two Engineered OBPs with opposite temperature-dependent affinities towards 1-aminoanthracene. Scientific Reports, 8(14844), 20182045-23222045-232210.1038/s41598-018-33085-830287882https://www.nature.com/articles/s41598-018-33085-8info: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:RCAAP2023-07-21T12:43:35Zoai:repositorium.sdum.uminho.pt:1822/56333Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:41:06.053840Repositório 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 |
Two Engineered OBPs with opposite temperature-dependent affinities towards 1-aminoanthracene |
title |
Two Engineered OBPs with opposite temperature-dependent affinities towards 1-aminoanthracene |
spellingShingle |
Two Engineered OBPs with opposite temperature-dependent affinities towards 1-aminoanthracene Gonçalves, Filipa Daniela Gomes Ciências Médicas::Biotecnologia Médica Science & Technology |
title_short |
Two Engineered OBPs with opposite temperature-dependent affinities towards 1-aminoanthracene |
title_full |
Two Engineered OBPs with opposite temperature-dependent affinities towards 1-aminoanthracene |
title_fullStr |
Two Engineered OBPs with opposite temperature-dependent affinities towards 1-aminoanthracene |
title_full_unstemmed |
Two Engineered OBPs with opposite temperature-dependent affinities towards 1-aminoanthracene |
title_sort |
Two Engineered OBPs with opposite temperature-dependent affinities towards 1-aminoanthracene |
author |
Gonçalves, Filipa Daniela Gomes |
author_facet |
Gonçalves, Filipa Daniela Gomes Castro, T. Azóia, Nuno G. Ribeiro, Artur Silva, Carla Manuela Pereira Marinho da Cavaco-Paulo, Artur |
author_role |
author |
author2 |
Castro, T. Azóia, Nuno G. Ribeiro, Artur Silva, Carla Manuela Pereira Marinho da Cavaco-Paulo, Artur |
author2_role |
author author author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Gonçalves, Filipa Daniela Gomes Castro, T. Azóia, Nuno G. Ribeiro, Artur Silva, Carla Manuela Pereira Marinho da Cavaco-Paulo, Artur |
dc.subject.por.fl_str_mv |
Ciências Médicas::Biotecnologia Médica Science & Technology |
topic |
Ciências Médicas::Biotecnologia Médica Science & Technology |
description |
Engineered odorant-binding proteins (OBPs) display tunable binding affinities triggered by temperature alterations. We designed and produced two engineered proteins based on OBP-I sequence: truncated OBP (tOBP) and OBP::GQ20::SP-DS3. The binding affinity of 1-aminoanthracene (1-AMA) to these proteins revealed that tOBP presents higher affinity at 25°C (kd=0.45M) than at 37°C (kd=1.72M). OBP::GQ20::SP-DS3 showed an opposite behavior, revealing higher affinity at 37°C (kd=0.58M) than at 25°C (kd=1.17M). We set-up a system containing both proteins to evaluate their temperature-dependent binding. Our data proved the 1-AMA differential and reversible affinity towards OBPs, triggered by temperature changes. The variations of the binding pocket size with temperature, confirmed by molecular modelling studies, were determinant for the differential binding of the engineered OBPs. Herein we described for the first time a competitive temperature-dependent mechanism for this class of proteins. |
publishDate |
2018 |
dc.date.none.fl_str_mv |
2018-10-04 2018-10-04T00:00:00Z |
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/1822/56333 |
url |
http://hdl.handle.net/1822/56333 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Gonçalves, Filipa D.; Castro, T.; Azoia, Nuno G.; Ribeiro, Artur; Silva, Carla; Cavaco-Paulo, Artur, Two Engineered OBPs with opposite temperature-dependent affinities towards 1-aminoanthracene. Scientific Reports, 8(14844), 2018 2045-2322 2045-2322 10.1038/s41598-018-33085-8 30287882 https://www.nature.com/articles/s41598-018-33085-8 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Nature Group |
publisher.none.fl_str_mv |
Nature Group |
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 |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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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 |
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1799132958965104640 |