NMR structural characterization of cecropin A(1-8) - magainin 2(1-12) and cecropin A (1-8) - melittin (1-12) hybrid peptides
| Autor: | D, Oh, S Y, Shin, J H, Kang, K S, Hahm, K L, Kim, Y, Kim |
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| Rok vydání: | 1999 |
| Předmět: |
Models
Molecular Erythrocytes Lung Neoplasms Magnetic Resonance Spectroscopy Protein Conformation Circular Dichroism Molecular Sequence Data Melitten Anti-Bacterial Agents Hemolysin Proteins Structure-Activity Relationship Tumor Cells Cultured Humans Amino Acid Sequence Carcinoma Small Cell Peptides Antimicrobial Cationic Peptides |
| Zdroj: | The journal of peptide research : official journal of the American Peptide Society. 53(5) |
| ISSN: | 1397-002X |
| Popis: | In order to elucidate the structure-antibiotic activity relationships of the peptides, the three-dimensional structures of two hybrid peptides, CA(1-8) - MA(1-12) and CA(1-8) - ME(1-12) in trifluoroethanol-containing aqueous solution were investigated by NMR spectroscopy. Both CA(1-8) - MA(1-12) and CA(1-8) - ME(1-12) have strong antibacterial activity but only CA(1-8) - ME(1-12) has hemolytic activity against human erythrocytes. CA(1-8) - MA(1-12) has a hydrophobic 310-helix of only two turns combined with one short helix in the N-terminus with a flexible hinge section in between. CA(1-8) - MA(1-12) has a severely bent structure in the middle of the peptide. These structural features as well as the low hydrophobicity of CA(1-8) - MA(1-12) seem to be crucial for the selective lysis against the membrane of prokaryotic cells. CA(1-8) - ME(1-12) has an alpha-helical structure of about three turns in the melittin domain and a flexible structure with one turn in the cecropin domain connected with a flexible hinge section in between, and these might be the structural features required for membrane disruption against prokaryotic and eukaryotic cells. The central hinge region (Gly9-Ile10-Gly11) in an amphipathic antibacterial peptide is considered to play an important role in providing the conformational flexibility required for ion channel formation of the C-terminal hydrophobic alpha-helix on cell membrane. |
| Databáze: | OpenAIRE |
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