Convergent Evolution-Guided Design of Antimicrobial Peptides Derived from Influenza A Virus Hemagglutinin
| Autor: | Bin Gao, Shunyi Zhu, André Aumelas |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Models
Molecular Viral Hemagglutinin Magnetic Resonance Spectroscopy Molecular Sequence Data Antimicrobial peptides Hemagglutinin (influenza) Hemagglutinin Glycoproteins Influenza Virus Peptide Microbial Sensitivity Tests medicine.disease_cause Hemolysis Microbiology Mice Structure-Activity Relationship Anti-Infective Agents Drug Discovery Amphiphile Influenza A virus medicine Animals Amino Acid Sequence chemistry.chemical_classification Bacteria biology Influenza A Virus H3N2 Subtype Antimicrobial Solution structure chemistry Biochemistry Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization biology.protein Molecular Medicine Viral Fusion Proteins Antimicrobial Cationic Peptides |
| Zdroj: | Journal of Medicinal Chemistry. 54:1091-1095 |
| ISSN: | 1520-4804 0022-2623 |
| Popis: | Antimicrobial activity and solution structures of four 13-amino acid peptides derived from the fusion domain of viral hemagglutinin proteins are presented. The results show that carboxyl-terminal amidation is a key factor to switch a viral fusion domain-derived sequence into an antimicrobial peptide. Optimization of amphiphilic balance on the amidated analogue largely improves efficacy and enlarges antimicrobial spectra of these peptides. Our work indicates that viral fusion domains have potential to be engineered into potent antimicrobial peptides. |
| Databáze: | OpenAIRE |
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