دورية أكاديمية
Structure-activity relationship, conformational and biological studies of temporin L analogues.
| العنوان: | Structure-activity relationship, conformational and biological studies of temporin L analogues. |
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| المؤلفون: | Mangoni ML; Department of Pharmaceutical and Toxicological Chemistry, University of Naples Federico II, Via D Montesano 49, I-80131 Naples, Italy., Carotenuto A, Auriemma L, Saviello MR, Campiglia P, Gomez-Monterrey I, Malfi S, Marcellini L, Barra D, Novellino E, Grieco P |
| المصدر: | Journal of medicinal chemistry [J Med Chem] 2011 Mar 10; Vol. 54 (5), pp. 1298-307. Date of Electronic Publication: 2011 Feb 14. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Chemical Society Country of Publication: United States NLM ID: 9716531 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-4804 (Electronic) Linking ISSN: 00222623 NLM ISO Abbreviation: J Med Chem Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Washington Dc : American Chemical Society Original Publication: [Easton, Pa.] : American Chemical Society, [c1963- |
| مواضيع طبية MeSH: | Amphibian Proteins/*chemical synthesis , Antimicrobial Cationic Peptides/*chemical synthesis , Peptides/*chemical synthesis, Amino Acid Sequence ; Amphibian Proteins/chemistry ; Amphibian Proteins/pharmacology ; Anti-Bacterial Agents/chemical synthesis ; Anti-Bacterial Agents/chemistry ; Anti-Bacterial Agents/pharmacology ; Antifungal Agents/chemical synthesis ; Antifungal Agents/chemistry ; Antifungal Agents/pharmacology ; Antimicrobial Cationic Peptides/chemistry ; Antimicrobial Cationic Peptides/pharmacology ; Cell Membrane Permeability ; Circular Dichroism ; Hemolysis ; Humans ; Hydrophobic and Hydrophilic Interactions ; In Vitro Techniques ; Microbial Sensitivity Tests ; Peptides/chemistry ; Peptides/pharmacology ; Protein Structure, Secondary ; Structure-Activity Relationship |
| مستخلص: | Temporins are naturally occurring peptides with promising features, which could lead to the development of new drugs. Temporin-1Tl (TL) is the strongest antimicrobial peptide, but it is toxic on human erythrocytes and this fact makes the design of synthetic analogues with a higher therapeutic index vital.We studied the structure-activity relationships of a library of TL derivatives focusing on the correlation between the α-helix content of the peptides, the nature of their cationic residues, and their antibacterial/antiyeast/hemolytic activities. We found that the percentage of helicity of TL analogues is directly correlated to their hemolytic activity but not to their antimicrobial activity. In addition, we found that the nature of positively charged residues can affect the biological properties of TL without changing the peptide's helicity. It is noteworthy that a single amino acid substitution can prevent the antimicrobial activity of TL, making it a lytic peptide presumably due to its self-association. Last, we identified a novel analogue with properties that make it an attractive topic for future research. |
| المشرفين على المادة: | 0 (Amphibian Proteins) 0 (Anti-Bacterial Agents) 0 (Antifungal Agents) 0 (Antimicrobial Cationic Peptides) 0 (Peptides) 0 (temporin L, Rana temporaria) |
| تواريخ الأحداث: | Date Created: 20110216 Date Completed: 20110606 Latest Revision: 20141120 |
| رمز التحديث: | 20231215 |
| DOI: | 10.1021/jm1012853 |
| PMID: | 21319749 |
| قاعدة البيانات: | MEDLINE |
Find this issue from the American Chemical Society | تدمد: | 1520-4804 |
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| DOI: | 10.1021/jm1012853 |