Comparison on effect of hydrophobicity on the antibacterial and antifungal activities of α-helical antimicrobial peptides : = Comparison on effect of hydrophobicity on the antibacterial and antifungal activities of α-helical antimicrobial peptides
HPRP-A1, a 15-mer α-helical cationic peptide, was derived from N-terminus of ribosomal protein L1 (RpL1) of Helicobacter pylori. In this study, HPRP-A1 was used as a framework to obtain a series of peptide analogs with different hydrophobicity by single amino acid substitutions in the center of nonpolar face of the amphipathic helix in order to systematically study the effect of hydrophobicity on biological activities of -helical antimicrobial peptides. Hydrophobicity and net charge of peptides played key roles in the biological activities of these peptide analogs; HPRP-A1 and peptide analogs with relative higher hydrophobicity exerted broad spectrum antimicrobial activity against Gram-negative bacteria, Gram-positive bacteria and pathogenic fungi, but also showed stronger hemolytic activity; the change of hydrophobicity and net charge of peptides had similar effects with close trend and extent on antibacterial activities and antifungal activities. This indicated that there were certain correlations between the antibacterial mode of action and the antifungal mode of action of these peptides in this study. The peptides exhibited antimicrobial specificity for bacteria and fungi, which provided potentials to develop new antimicrobial drugs for clinical practices..
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2013-09-01 2013 |
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| Erschienen: |
2013-09-01 |
| Enthalten in: |
Zur Gesamtaufnahme - year:2013 |
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| Enthalten in: |
Science China / Chemistry - (2013), 09 vom: 01. Sept., Seite 1307-1314 Original Letters: Enthalten in (DE-576)322441951 (DE-576)322441951 |
| Reihe: |
China Academic Journals (CAJ), A, 理工A(数学物理力学天地生) = Mathematics/ Physics/ Mechanics/ Astronomy |
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| Sprache: |
Chinesisch |
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| Weiterer Titel: |
Comparison on effect of hydrophobicity on the antibacterial and antifungal activities of α-helical antimicrobial peptides |
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| Beteiligte Personen: |
ZHAO LianJing [VerfasserIn] |
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| Links: |
oversea.cnki.net [lizenzpflichtig] |
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| Anmerkungen: |
Author info:ZHAO LianJing 1 , HUANG YiBing 1 , GAO Song 2 , CUI Yan 2 , HE Dan 2 , WANG Li 2* & CHEN YuXin 1* 1 Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, Jilin University, Changchun 130012, China 2 Department of Pathogenobiology, Norman Bethune College of Medicine, Jilin University Mycology Research Center, Jilin University, Changchun 130021, China |
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| Förderinstitution / Projekttitel: |
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CAJ407178120 |
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| 520 | |a HPRP-A1, a 15-mer α-helical cationic peptide, was derived from N-terminus of ribosomal protein L1 (RpL1) of Helicobacter pylori. In this study, HPRP-A1 was used as a framework to obtain a series of peptide analogs with different hydrophobicity by single amino acid substitutions in the center of nonpolar face of the amphipathic helix in order to systematically study the effect of hydrophobicity on biological activities of -helical antimicrobial peptides. Hydrophobicity and net charge of peptides played key roles in the biological activities of these peptide analogs; HPRP-A1 and peptide analogs with relative higher hydrophobicity exerted broad spectrum antimicrobial activity against Gram-negative bacteria, Gram-positive bacteria and pathogenic fungi, but also showed stronger hemolytic activity; the change of hydrophobicity and net charge of peptides had similar effects with close trend and extent on antibacterial activities and antifungal activities. This indicated that there were certain correlations between the antibacterial mode of action and the antifungal mode of action of these peptides in this study. The peptides exhibited antimicrobial specificity for bacteria and fungi, which provided potentials to develop new antimicrobial drugs for clinical practices. | ||
| 610 | 2 | 4 | |a Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education,Jilin University |
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