Influence of secretory leukocyte protease inhibitor (SLPI) basedeptides on elastase activity and their incorporation into hyaluronic acid hydrogels for chronic wound terapy
Autor(a) principal: | |
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Data de Publicação: | 2012 |
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/1822/22157 |
Resumo: | Chronic nonhealing skin wounds, such as leg ulcers and pressure sores, represent a major clinical problem and a financial burden for the health care systems. Chronic wounds are characterized by prolonged inflammatory phase that results in high levels of elastase, reactive oxygen species (ROS), and diminished growth factor activity. Under normal physiological conditions, elastase is a powerful host defence and its activity is regulated by endogenous inhibitors. The unrestrained elastase activity in chronic wounds may be tuned by exogenous active materials that inhibit elastase. Secretory leucocyte protease inhibitor, SLPI, is a potent endogenous inhibitor of elastase. Peptide fragments, KRCCPDTCGIKCL (Pep4) and KRMMPDTMGIKML (Pep4M), selected from SLPI primary structure were studied as potential elastase inhibitors. Kinetic studies performed for human neutrophil elastase (HNE) and porcine pancreatic elastase (PPE) in presence of these peptides revealed that both behave as uncompetitive and noncompetitive inhibitors of HNE and PPE, respectively. The influence of ROS and albumin on Pep4 and Pep4M inhibitory activity toward elastase reveals that this mixture increases the inhibitory activity of both peptides. These peptides were incorporated in hyaluronic acid hydrogels to evaluate the possibility of being used as active compounds in a drug delivery system. Assessment of HNE and PPE activity in the presence of these hydrogels formulations revealed a considerable decrease in enzyme activity. Although, only moderated elastase inhibition was observed, these peptides represent potential candidates for chronic wound applications, as there is no need for complete elastase inhibition in the normal wound healing process |
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Influence of secretory leukocyte protease inhibitor (SLPI) basedeptides on elastase activity and their incorporation into hyaluronic acid hydrogels for chronic wound terapyElastaseInhibitor-peptidesKinetic parametersReactive oxygen speciesHyaluronic acid hydrogelsScience & TechnologyChronic nonhealing skin wounds, such as leg ulcers and pressure sores, represent a major clinical problem and a financial burden for the health care systems. Chronic wounds are characterized by prolonged inflammatory phase that results in high levels of elastase, reactive oxygen species (ROS), and diminished growth factor activity. Under normal physiological conditions, elastase is a powerful host defence and its activity is regulated by endogenous inhibitors. The unrestrained elastase activity in chronic wounds may be tuned by exogenous active materials that inhibit elastase. Secretory leucocyte protease inhibitor, SLPI, is a potent endogenous inhibitor of elastase. Peptide fragments, KRCCPDTCGIKCL (Pep4) and KRMMPDTMGIKML (Pep4M), selected from SLPI primary structure were studied as potential elastase inhibitors. Kinetic studies performed for human neutrophil elastase (HNE) and porcine pancreatic elastase (PPE) in presence of these peptides revealed that both behave as uncompetitive and noncompetitive inhibitors of HNE and PPE, respectively. The influence of ROS and albumin on Pep4 and Pep4M inhibitory activity toward elastase reveals that this mixture increases the inhibitory activity of both peptides. These peptides were incorporated in hyaluronic acid hydrogels to evaluate the possibility of being used as active compounds in a drug delivery system. Assessment of HNE and PPE activity in the presence of these hydrogels formulations revealed a considerable decrease in enzyme activity. Although, only moderated elastase inhibition was observed, these peptides represent potential candidates for chronic wound applications, as there is no need for complete elastase inhibition in the normal wound healing processContract grant sponsor: Portuguese Foundation for Science and TechnologyContract grant number: SFRH/BD/36522/2007Contract grant sponsors: FEDER (European Fund for Regional Development)-COMPETE-QREN-EUContract grant sponsors: COST Action 868The authors greatly acknowledge the European Project Lidwine-Multifunctional medical textiles for wound (e.g., Decubitus) prevention and improved wound healing. The financial support for the Research Centre was given by CQ/UM [PEst-C/QUI/UI0686/2011(FCOMP-01-0124-FEDER-022716]. The divulgation of these results, as an oral communication, was supported by the COST Action 868. The authors thank Professor Ana Campos (Chemistry Department, Minho University, Portugal) for supplying the hyaluronic acid used in this study.WileyUniversidade do MinhoBarros, Sandra CerqueiraMartins, J. A. R.Marcos, João CarlosPaulo, Artur Cavaco2012-11-122012-11-12T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/22157eng0006-352510.1002/bip.2216623203763http://onlinelibrary.wiley.com/doi/10.1002/bip.22166/fullinfo: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:RCAAP2023-07-21T12:39:26Zoai:repositorium.sdum.uminho.pt:1822/22157Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:36:03.196205Repositório 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 |
Influence of secretory leukocyte protease inhibitor (SLPI) basedeptides on elastase activity and their incorporation into hyaluronic acid hydrogels for chronic wound terapy |
title |
Influence of secretory leukocyte protease inhibitor (SLPI) basedeptides on elastase activity and their incorporation into hyaluronic acid hydrogels for chronic wound terapy |
spellingShingle |
Influence of secretory leukocyte protease inhibitor (SLPI) basedeptides on elastase activity and their incorporation into hyaluronic acid hydrogels for chronic wound terapy Barros, Sandra Cerqueira Elastase Inhibitor-peptides Kinetic parameters Reactive oxygen species Hyaluronic acid hydrogels Science & Technology |
title_short |
Influence of secretory leukocyte protease inhibitor (SLPI) basedeptides on elastase activity and their incorporation into hyaluronic acid hydrogels for chronic wound terapy |
title_full |
Influence of secretory leukocyte protease inhibitor (SLPI) basedeptides on elastase activity and their incorporation into hyaluronic acid hydrogels for chronic wound terapy |
title_fullStr |
Influence of secretory leukocyte protease inhibitor (SLPI) basedeptides on elastase activity and their incorporation into hyaluronic acid hydrogels for chronic wound terapy |
title_full_unstemmed |
Influence of secretory leukocyte protease inhibitor (SLPI) basedeptides on elastase activity and their incorporation into hyaluronic acid hydrogels for chronic wound terapy |
title_sort |
Influence of secretory leukocyte protease inhibitor (SLPI) basedeptides on elastase activity and their incorporation into hyaluronic acid hydrogels for chronic wound terapy |
author |
Barros, Sandra Cerqueira |
author_facet |
Barros, Sandra Cerqueira Martins, J. A. R. Marcos, João Carlos Paulo, Artur Cavaco |
author_role |
author |
author2 |
Martins, J. A. R. Marcos, João Carlos Paulo, Artur Cavaco |
author2_role |
author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Barros, Sandra Cerqueira Martins, J. A. R. Marcos, João Carlos Paulo, Artur Cavaco |
dc.subject.por.fl_str_mv |
Elastase Inhibitor-peptides Kinetic parameters Reactive oxygen species Hyaluronic acid hydrogels Science & Technology |
topic |
Elastase Inhibitor-peptides Kinetic parameters Reactive oxygen species Hyaluronic acid hydrogels Science & Technology |
description |
Chronic nonhealing skin wounds, such as leg ulcers and pressure sores, represent a major clinical problem and a financial burden for the health care systems. Chronic wounds are characterized by prolonged inflammatory phase that results in high levels of elastase, reactive oxygen species (ROS), and diminished growth factor activity. Under normal physiological conditions, elastase is a powerful host defence and its activity is regulated by endogenous inhibitors. The unrestrained elastase activity in chronic wounds may be tuned by exogenous active materials that inhibit elastase. Secretory leucocyte protease inhibitor, SLPI, is a potent endogenous inhibitor of elastase. Peptide fragments, KRCCPDTCGIKCL (Pep4) and KRMMPDTMGIKML (Pep4M), selected from SLPI primary structure were studied as potential elastase inhibitors. Kinetic studies performed for human neutrophil elastase (HNE) and porcine pancreatic elastase (PPE) in presence of these peptides revealed that both behave as uncompetitive and noncompetitive inhibitors of HNE and PPE, respectively. The influence of ROS and albumin on Pep4 and Pep4M inhibitory activity toward elastase reveals that this mixture increases the inhibitory activity of both peptides. These peptides were incorporated in hyaluronic acid hydrogels to evaluate the possibility of being used as active compounds in a drug delivery system. Assessment of HNE and PPE activity in the presence of these hydrogels formulations revealed a considerable decrease in enzyme activity. Although, only moderated elastase inhibition was observed, these peptides represent potential candidates for chronic wound applications, as there is no need for complete elastase inhibition in the normal wound healing process |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-11-12 2012-11-12T00:00:00Z |
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/1822/22157 |
url |
http://hdl.handle.net/1822/22157 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0006-3525 10.1002/bip.22166 23203763 http://onlinelibrary.wiley.com/doi/10.1002/bip.22166/full |
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 |
Wiley |
publisher.none.fl_str_mv |
Wiley |
dc.source.none.fl_str_mv |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
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RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799132888531206144 |