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https://hdl.handle.net/1822/25935
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Campo DC | Valor | Idioma |
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dc.contributor.author | Barros, Sandra Cerqueira | - |
dc.contributor.author | Louro, Ricardo O. | - |
dc.contributor.author | Micaelo, N. M. | - |
dc.contributor.author | Martins, José A. | - |
dc.contributor.author | Marcos, João Carlos | - |
dc.contributor.author | Paulo, Artur Cavaco | - |
dc.date.accessioned | 2013-11-01T14:49:56Z | - |
dc.date.available | 2013-11-01T14:49:56Z | - |
dc.date.issued | 2013-10 | - |
dc.identifier.issn | 1381-5148 | por |
dc.identifier.uri | https://hdl.handle.net/1822/25935 | - |
dc.description.abstract | Proteases play an important and critical role in the physiological process of wound repair. However, excessive and unregulated release of proteolytic enzymes (e.g., elastase) mediates abnormal degradation of healthy tissues, which leads to inflammatory disorders such as chronic wounds. Thus, it is of therapeutic interest to develop novel synthetic inhibitor-peptides of elastase, which can restore the balance between the free enzyme and the endogenous inhibitors in chronic wounds. In previous works, we have reported two different drug delivery systems to release novel elastase inhibitors to the wound site. In both systems synthetic peptides (KRCCPDTCGIKCL-Pep4 and KRMMPDTMGIKML-Pep4M) based on the primary structure of the endogenous elastase inhibitor, secretory leucocyte protease inhibitor, were used as active material. Phosphorylation of the reported peptides prompts significant structural differences, which reflects in distinct inhibitory capacity towards elastase. These structural modifications were prompted by electrostatic interactions and hydrogen bonds established from the peptide phosphoresidue. The current study was also extended to another synthetic peptide (WCTASVPPQCY-PepBBI) that is based on the reactive loop of another elastase inhibitor, the Bowmen-Birk inhibitor. PepBBI, phosphorylated and non-phosphorylated, displays similar behaviour to Pep4 and Pep4M. The structural modifications reported herein were evaluated by two-dimensional nuclear magnetic resonance and molecular modelling approaches. | por |
dc.description.sponsorship | The authors gratefully acknowledge the financial support of the Portuguese Foundation for Science and Technology (scholarship SFRH/BD/36522/2007 and PEst-OE/EQB/LA0004/2011), FEDER (European Fund for Regional Development)-COMPETE-QREN-EU and the European Project Lidwine - Multifunctional medical textiles for wound (e.g. Decubitus). We acknowledge CERMAX at ITQB-UNL and Rede Nacional de RMN for access to the facilities. Rede Nacional de RMN is supported with funds from FCT, Projecto de Re-equipamento Cientifico contract REDE/1517/RMN/2005, Portugal. Micaelo, N.M. acknowledges the contract research program "Compromisso corn a Ciencia" reference: C2008-UMINHO-CQ-03 and access to the Minho University GRIUM cluster. | por |
dc.language.iso | eng | por |
dc.publisher | Elsevier 1 | por |
dc.rights | openAccess | por |
dc.subject | Elastase inhibitor-peptides | por |
dc.subject | SLPI | por |
dc.subject | 2D-NMR | por |
dc.subject | Molecular docking | por |
dc.subject | Phosphorylation | por |
dc.title | NMR and molecular modelling studies on elastase inhibitor-peptides for wound management | por |
dc.type | article | eng |
dc.peerreviewed | yes | por |
sdum.publicationstatus | published | por |
oaire.citationStartPage | 1357 | por |
oaire.citationEndPage | 1365 | por |
oaire.citationIssue | 10 | por |
oaire.citationTitle | Reactive and Functional Polymers | por |
oaire.citationVolume | 73 | por |
dc.identifier.doi | 10.1016/j.reactfunctpolym.2013.02.011 | - |
dc.subject.wos | Science & Technology | por |
sdum.journal | Reactive and Functional Polymers | por |
Aparece nas coleções: | CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series |
Ficheiros deste registo:
Ficheiro | Descrição | Tamanho | Formato | |
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2013 NMR and molecular modelling studies on elastase inhibitor-peptides for wound management.pdf | NMR and molecular modelling studies on elastase inhibitor-peptides for wound management | 3,26 MB | Adobe PDF | Ver/Abrir |