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Title 

NMR structural characterization of cecropin A(1-8) - magainin 2(1-12) and cecropin A(1-8) - melittin(1-12) hybrid peptides

Authors 

D OhSong Yub ShinJoo Hyun KangKyung Soo HahmKil Lyong KimYang Mee Kim

Publisher 

Wiley-Blackwell

Issue Date 

1999

Citation 

Journal of Peptide Research, vol. 53, no. 0, pp. 578-589

Keywords 

CA(1-8)-MA(1-12)CA(1-8)-ME(1-12)hemolytic activityNMR spectroscopytertiary structure

Abstract 

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 α-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 distruption 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 α-helix on cell membrane.

ISSN 

1397-002X

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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