Interaction of adrenocorticotropin peptides with microheterogeneous systems : a fluorescence study.
Autor(a) principal: | |
---|---|
Data de Publicação: | 2009 |
Outros Autores: | |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UFOP |
Texto Completo: | http://www.repositorio.ufop.br/handle/123456789/4877 https://doi.org/10.1016/j.bpc.2008.10.009 |
Resumo: | Adrenocorticotropin (ACTH) and α-melanocyte stimulating hormone (α-MSH) are peptides which present many physiological effects related to pigmentation, motor and sexual behavior, learning and memory, analgesia, anti-inflammatory and antipyretic processes. The 13 amino acid residues of α-MSH are the same initial sequence of ACTH and due to the presence of a tryptophan residue in position 9 of the peptide chain, fluorescence techniques could be used to investigate the conformational properties of the hormones in different environments and the mechanisms of interaction with biomimetic systems like sodium dodecyl sulphate (SDS) micelles, sodium dodecyl sulphate-poly(ethylene oxide) (SDS-PEO) aggregates and neutral polymeric micelles. In buffer solution, fluorescence parameters were typical of peptides containing tryptophan exposed to the aqueous medium and upon addition of surfactant and polymer molecules, the gradual change of those parameters demonstrated the interaction of the peptides with the microheterogeneous systems. From time-resolved experiments it was shown that the interaction proceeded with conformational changes in both peptides, and further information was obtained from quenching of Trp fluorescence by a family of N-alkylpyridinium ions, which possess affinity to the microheterogeneous systems dependent on the length of the alkyl chain. The quenching of Trp fluorescence was enhanced in the presence of charged micelles, compared to the buffer solution and the accessibility of the fluorophore to the quencher was dependent on the peptide and the alkylpyridinium: in ACTH(1–21) highest collisional constants were obtained using ethylpyridinium as quencher, indicating a location of the residue in the surface of the micelle, while in α-MSH the best quencher was hexylpyridinium, indicating insertion of the residue into the non-polar region of the micelles. The results had shown that the interaction between the peptides and the biomimetic systems where driven by combined electrostatic and hydrophobic effects: in ACTH(1–24) the electrostatic interaction between highly positively charged C-terminal and negatively charged surface of micelles and aggregates predominates over hydrophobic interactions involving residues in the central region of the peptide; in α-MSH, which presents one residual positive charge, the hydrophobic interactions are relevant to position the Trp residue in the non-polar region of the microheterogeneous systems. |
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Romani, Ana PaulaIto, Amando Siuiti2015-04-01T17:20:30Z2015-04-01T17:20:30Z2009ROMANI, A. P.; ITO, A. S. Interaction of adrenocorticotropin peptides with microheterogeneous systems: a fluorescence study. Biophysical Chemistry, v. 139, p. 92-98, 2009. Disponível em: <http://www.sciencedirect.com/science/article/pii/S0301462208002251>. Acesso em: 02 fev. 2015.0301-4622http://www.repositorio.ufop.br/handle/123456789/4877https://doi.org/10.1016/j.bpc.2008.10.009Adrenocorticotropin (ACTH) and α-melanocyte stimulating hormone (α-MSH) are peptides which present many physiological effects related to pigmentation, motor and sexual behavior, learning and memory, analgesia, anti-inflammatory and antipyretic processes. The 13 amino acid residues of α-MSH are the same initial sequence of ACTH and due to the presence of a tryptophan residue in position 9 of the peptide chain, fluorescence techniques could be used to investigate the conformational properties of the hormones in different environments and the mechanisms of interaction with biomimetic systems like sodium dodecyl sulphate (SDS) micelles, sodium dodecyl sulphate-poly(ethylene oxide) (SDS-PEO) aggregates and neutral polymeric micelles. In buffer solution, fluorescence parameters were typical of peptides containing tryptophan exposed to the aqueous medium and upon addition of surfactant and polymer molecules, the gradual change of those parameters demonstrated the interaction of the peptides with the microheterogeneous systems. From time-resolved experiments it was shown that the interaction proceeded with conformational changes in both peptides, and further information was obtained from quenching of Trp fluorescence by a family of N-alkylpyridinium ions, which possess affinity to the microheterogeneous systems dependent on the length of the alkyl chain. The quenching of Trp fluorescence was enhanced in the presence of charged micelles, compared to the buffer solution and the accessibility of the fluorophore to the quencher was dependent on the peptide and the alkylpyridinium: in ACTH(1–21) highest collisional constants were obtained using ethylpyridinium as quencher, indicating a location of the residue in the surface of the micelle, while in α-MSH the best quencher was hexylpyridinium, indicating insertion of the residue into the non-polar region of the micelles. The results had shown that the interaction between the peptides and the biomimetic systems where driven by combined electrostatic and hydrophobic effects: in ACTH(1–24) the electrostatic interaction between highly positively charged C-terminal and negatively charged surface of micelles and aggregates predominates over hydrophobic interactions involving residues in the central region of the peptide; in α-MSH, which presents one residual positive charge, the hydrophobic interactions are relevant to position the Trp residue in the non-polar region of the microheterogeneous systems.Tryptophan fluorescenceDetergent and polymeric micelleAlkylpyridinium quencherInteraction of adrenocorticotropin peptides with microheterogeneous systems : a fluorescence study.info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleO periódico Biophysical Chemistry concede permissão para depósito deste artigo no Repositório Institucional da UFOP. Número da licença: 3577170779614.info:eu-repo/semantics/openAccessengreponame:Repositório Institucional da UFOPinstname:Universidade Federal de Ouro Preto (UFOP)instacron:UFOPLICENSElicense.txtlicense.txttext/plain; charset=utf-82636http://www.repositorio.ufop.br/bitstream/123456789/4877/2/license.txtc2ffdd99e58acf69202dff00d361f23aMD52ORIGINALARTIGO_InteractionAdrenocorticotropinPeptides.pdfARTIGO_InteractionAdrenocorticotropinPeptides.pdfapplication/pdf546664http://www.repositorio.ufop.br/bitstream/123456789/4877/1/ARTIGO_InteractionAdrenocorticotropinPeptides.pdf93d942ecbbcbb32b8d646fe4a8327893MD51123456789/48772019-07-03 12:09:34.552oai:localhost: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Repositório InstitucionalPUBhttp://www.repositorio.ufop.br/oai/requestrepositorio@ufop.edu.bropendoar:32332019-07-03T16:09:34Repositório Institucional da UFOP - Universidade Federal de Ouro Preto (UFOP)false |
dc.title.pt_BR.fl_str_mv |
Interaction of adrenocorticotropin peptides with microheterogeneous systems : a fluorescence study. |
title |
Interaction of adrenocorticotropin peptides with microheterogeneous systems : a fluorescence study. |
spellingShingle |
Interaction of adrenocorticotropin peptides with microheterogeneous systems : a fluorescence study. Romani, Ana Paula Tryptophan fluorescence Detergent and polymeric micelle Alkylpyridinium quencher |
title_short |
Interaction of adrenocorticotropin peptides with microheterogeneous systems : a fluorescence study. |
title_full |
Interaction of adrenocorticotropin peptides with microheterogeneous systems : a fluorescence study. |
title_fullStr |
Interaction of adrenocorticotropin peptides with microheterogeneous systems : a fluorescence study. |
title_full_unstemmed |
Interaction of adrenocorticotropin peptides with microheterogeneous systems : a fluorescence study. |
title_sort |
Interaction of adrenocorticotropin peptides with microheterogeneous systems : a fluorescence study. |
author |
Romani, Ana Paula |
author_facet |
Romani, Ana Paula Ito, Amando Siuiti |
author_role |
author |
author2 |
Ito, Amando Siuiti |
author2_role |
author |
dc.contributor.author.fl_str_mv |
Romani, Ana Paula Ito, Amando Siuiti |
dc.subject.por.fl_str_mv |
Tryptophan fluorescence Detergent and polymeric micelle Alkylpyridinium quencher |
topic |
Tryptophan fluorescence Detergent and polymeric micelle Alkylpyridinium quencher |
description |
Adrenocorticotropin (ACTH) and α-melanocyte stimulating hormone (α-MSH) are peptides which present many physiological effects related to pigmentation, motor and sexual behavior, learning and memory, analgesia, anti-inflammatory and antipyretic processes. The 13 amino acid residues of α-MSH are the same initial sequence of ACTH and due to the presence of a tryptophan residue in position 9 of the peptide chain, fluorescence techniques could be used to investigate the conformational properties of the hormones in different environments and the mechanisms of interaction with biomimetic systems like sodium dodecyl sulphate (SDS) micelles, sodium dodecyl sulphate-poly(ethylene oxide) (SDS-PEO) aggregates and neutral polymeric micelles. In buffer solution, fluorescence parameters were typical of peptides containing tryptophan exposed to the aqueous medium and upon addition of surfactant and polymer molecules, the gradual change of those parameters demonstrated the interaction of the peptides with the microheterogeneous systems. From time-resolved experiments it was shown that the interaction proceeded with conformational changes in both peptides, and further information was obtained from quenching of Trp fluorescence by a family of N-alkylpyridinium ions, which possess affinity to the microheterogeneous systems dependent on the length of the alkyl chain. The quenching of Trp fluorescence was enhanced in the presence of charged micelles, compared to the buffer solution and the accessibility of the fluorophore to the quencher was dependent on the peptide and the alkylpyridinium: in ACTH(1–21) highest collisional constants were obtained using ethylpyridinium as quencher, indicating a location of the residue in the surface of the micelle, while in α-MSH the best quencher was hexylpyridinium, indicating insertion of the residue into the non-polar region of the micelles. The results had shown that the interaction between the peptides and the biomimetic systems where driven by combined electrostatic and hydrophobic effects: in ACTH(1–24) the electrostatic interaction between highly positively charged C-terminal and negatively charged surface of micelles and aggregates predominates over hydrophobic interactions involving residues in the central region of the peptide; in α-MSH, which presents one residual positive charge, the hydrophobic interactions are relevant to position the Trp residue in the non-polar region of the microheterogeneous systems. |
publishDate |
2009 |
dc.date.issued.fl_str_mv |
2009 |
dc.date.accessioned.fl_str_mv |
2015-04-01T17:20:30Z |
dc.date.available.fl_str_mv |
2015-04-01T17:20:30Z |
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.citation.fl_str_mv |
ROMANI, A. P.; ITO, A. S. Interaction of adrenocorticotropin peptides with microheterogeneous systems: a fluorescence study. Biophysical Chemistry, v. 139, p. 92-98, 2009. Disponível em: <http://www.sciencedirect.com/science/article/pii/S0301462208002251>. Acesso em: 02 fev. 2015. |
dc.identifier.uri.fl_str_mv |
http://www.repositorio.ufop.br/handle/123456789/4877 |
dc.identifier.issn.none.fl_str_mv |
0301-4622 |
dc.identifier.doi.none.fl_str_mv |
https://doi.org/10.1016/j.bpc.2008.10.009 |
identifier_str_mv |
ROMANI, A. P.; ITO, A. S. Interaction of adrenocorticotropin peptides with microheterogeneous systems: a fluorescence study. Biophysical Chemistry, v. 139, p. 92-98, 2009. Disponível em: <http://www.sciencedirect.com/science/article/pii/S0301462208002251>. Acesso em: 02 fev. 2015. 0301-4622 |
url |
http://www.repositorio.ufop.br/handle/123456789/4877 https://doi.org/10.1016/j.bpc.2008.10.009 |
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eng |
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