کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1945189 | 1053255 | 2009 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Comparison of the membrane interaction mechanism of two antimicrobial RNases: RNase 3/ECP and RNase 7
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کلمات کلیدی
DOPC1,2-dioleoyl-sn-glycero-3-[phospho-rac-(1-glycerol)]8-Aminonaphthalene-1,3,6-Trisulfonic Acid Disodium SaltRNaseDOPGDPXGUV1,2-dioleoyl-sn-glycero-3-phosphocholine - 1،2-dioleoyl-sn-glycero-3-phosphocholinelarge unilamellar vesicles - بزرگ کیسه های بدون انعطاف پذیرMembrane - غشاءGiant unilamellar vesicles - غول پیکر یکپارچهFluorescence spectroscopy - فوتولومینسانس یا فلوئورسانس یا فسفرسانسLUV - لووLiposome - لیپوزوم هاAnts - مورچه، مورConfocal microscopy - میکروسکوپ کانفوکالantimicrobial protein - پروتئین ضد میکروبی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Eosinophil cationic protein (ECP/RNase 3) and the skin derived ribonuclease 7 (RNase 7) are members of the RNase A superfamily. RNase 3 is mainly expressed in eosinophils whereas RNase 7 is primarily secreted by keratinocytes. Both proteins present a broad-spectrum antimicrobial activity and their bactericidal mechanism is dependent on their membrane destabilizing capacities. Using phospholipid vesicles as membrane models, we have characterized the protein membrane association process. Confocal microscopy experiments using giant unilamellar vesicles illustrate the morphological changes of the liposome population. By labelling both lipid bilayers and proteins we have monitored the kinetic of the process. The differential protein ability to release the liposome aqueous content was evaluated together with the micellation and aggregation processes. A distinct morphology of the protein/lipid aggregates was visualized by transmission electron microscopy and the proteins overall secondary structure in a lipid microenvironment was assessed by FTIR. Interestingly, for both RNases the membrane interaction events take place in a different behaviour and timing: RNase 3 triggers first the vesicle aggregation, while RNase 7 induces leakage well before the aggregation step. Their distinct mechanism of action at the membrane level may reflect different in vivo antipathogen functions.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Biomembranes - Volume 1788, Issue 5, May 2009, Pages 1116-1125
Journal: Biochimica et Biophysica Acta (BBA) - Biomembranes - Volume 1788, Issue 5, May 2009, Pages 1116-1125
نویسندگان
Marc Torrent, Daniel Sánchez, VÃctor Buzón, M. Victòria Nogués, Josep Cladera, Ester Boix,