دورية أكاديمية
New insight into the mechanism of action of the temporin antimicrobial peptides.
| العنوان: | New insight into the mechanism of action of the temporin antimicrobial peptides. |
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| المؤلفون: | Saviello MR; Department of Pharmaceutical and Toxicological Chemistry, University of Naples Federico II, I-80131 Naples, Italy., Malfi S, Campiglia P, Cavalli A, Grieco P, Novellino E, Carotenuto A |
| المصدر: | Biochemistry [Biochemistry] 2010 Feb 23; Vol. 49 (7), pp. 1477-85. |
| نوع المنشور: | Comparative Study; Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Chemical Society Country of Publication: United States NLM ID: 0370623 Publication Model: Print Cited Medium: Internet ISSN: 1520-4995 (Electronic) Linking ISSN: 00062960 NLM ISO Abbreviation: Biochemistry Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Washington, American Chemical Society. |
| مواضيع طبية MeSH: | Anti-Bacterial Agents/*chemistry , Antimicrobial Cationic Peptides/*chemistry , Peptides/*chemistry , Proteins/*chemistry, Animals ; Anti-Bacterial Agents/pharmacology ; Anti-Bacterial Agents/toxicity ; Antimicrobial Cationic Peptides/physiology ; Antimicrobial Cationic Peptides/toxicity ; Glutamine/chemistry ; Gram-Positive Bacteria/drug effects ; Hemolysis/drug effects ; Magnetic Resonance Spectroscopy ; Membranes, Artificial ; Micelles ; Peptides/physiology ; Peptides/toxicity ; Proline/chemistry ; Protein Conformation ; Protein Structure, Secondary ; Proteins/physiology ; Proteins/toxicity ; Rana temporaria ; Structure-Activity Relationship |
| مستخلص: | Temporins constitute a family of amphipathic alpha-helical antimicrobial peptides (AMPs) and contain some of the shortest cytotoxic peptides, comprised of only 10-14 residues. We have recently investigated two members of this family, temporin A (TA) and temporin L (TL), because of their different spectra of antimicrobial activity and toxicity. Consequently, we developed new analogues with promising biological activities named Pro(3)-TL and Gln(3)-TA. In this work, we performed a detailed NMR analysis of the new analogues in SDS and DPC micelles, which mimic bacterial and mammalian membranes, respectively. NMR studies reveal that strongly hemolytic Gln(3)-TA was in a stable helical conformation along the entire sequence, while weakly hemolytic but antimicrobial Pro(3)-TL showed conformational averaging at the N-terminus. Furthermore, molecular dynamics (MD) simulations on TL and Pro(3)-TL were performed in explicit water and DPC micelles. Simulations indicated that both peptides prefer a location at the micelle-water interface; however, Phe(1) of strongly hemolytic TL was embedded more in depth into DPC, and only TL caused a significant distortion of the micelle shape. By combining NMR and computational analyses, we obtained a molecular-level resolution of the interactions between TL and its analogues with membrane mimicking micelles. |
| المشرفين على المادة: | 0 (Anti-Bacterial Agents) 0 (Antimicrobial Cationic Peptides) 0 (Membranes, Artificial) 0 (Micelles) 0 (Peptides) 0 (Proteins) 0 (temporin) 0 (temporin L, Rana temporaria) 0RH81L854J (Glutamine) 9DLQ4CIU6V (Proline) |
| تواريخ الأحداث: | Date Created: 20100120 Date Completed: 20100414 Latest Revision: 20131121 |
| رمز التحديث: | 20240628 |
| DOI: | 10.1021/bi902166d |
| PMID: | 20082523 |
| قاعدة البيانات: | MEDLINE |
Find this issue from the American Chemical Society | تدمد: | 1520-4995 |
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| DOI: | 10.1021/bi902166d |