کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5210078 | 1382873 | 2013 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
NMR and molecular modelling studies on elastase inhibitor-peptides for wound management
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کلمات کلیدی
2D total correlated spectroscopyMmpsRMSD2D-NMRPep4SLPIPPETOCSYNOESYNOE2D NMR - NMR 2Dnuclear Overhauser enhancement and exchange spectroscopy - افزایش انرژی هسته ای و طیف سنجی مبادلهPorcine pancreatic elastase - الاستاز پانکراس گوشت خوکtwo-dimensional nuclear magnetic resonance - رزونانس مغناطیسی هسته ای دو بعدیphosphothreonine - فسفاترونینPhosphorylation - فسفریلاسیونMatrix metalloproteinases - متالوپروتئیناز ماتریکسsecretory leukocyte protease inhibitor - مهار کننده پروتئاز لکوستیک ترشحیroot mean square deviation - میانگین انحراف مربع ریشهMolecular docking - پیوندهای بین مولکولیCOSY - کثیف
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آلی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: NMR and molecular modelling studies on elastase inhibitor-peptides for wound management NMR and molecular modelling studies on elastase inhibitor-peptides for wound management](/preview/png/5210078.png)
چکیده انگلیسی
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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Reactive and Functional Polymers - Volume 73, Issue 10, October 2013, Pages 1357-1365
Journal: Reactive and Functional Polymers - Volume 73, Issue 10, October 2013, Pages 1357-1365
نویسندگان
Sandra Cerqueira Barros, Ricardo O. Louro, Nuno M. Micaêlo, José Alberto Martins, João Carlos Marcos, Artur Cavaco-Paulo,