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Title 

Structure and antibiotic activity of a porcine myeloid antibacterial peptide, PMAP-23 and its analogues

Authors 

Song Yub ShinJoo Hyun KangSo Yun JangKil Lyong KimKyung Soo Hahm

Publisher 

Springer Verlag (Germany)

Issue Date 

2000

Citation 

Journal of Biochemistry and Molecular Biology, vol. 33, no. 1, pp. 49-53

Keywords 

antibacterial activityantitumor activityphospholipid vesicle-disrupting activityPMAP-23secondary structure

Abstract 

PMAP-23 is a 23-residue antimicrobial peptide derived from porcine myloid cells. In order to investigate the effects of two Pro residues at positions 12 and 15 of PMAP-23 on antibiotic activity, two analogues in which Ala was substituted for Pro residue at position 12 or 15 were synthesized. Pro12→Ala (PMAP1) or Pro15→Ala (PMAP2) substitution in PMAP-23 caused a significant reduction on antitumor and phospholipid vesicle-disrupting activities, but did not cause a significant effect on antibacterial activity. PMAP-23 displayed the type I β-turn structure with a negative ellipticity at near 205 nm in SDS micelle, whereas PMAP1 and PMAP2 had a somewhat α-helical propensity in TFE solution, as compared to PMAP-23. These results suggest that two Pro residues of positions 12 and 15 in PMAP-23 play important roles in the formation of β-turn structure on lipid membrane and its β-turn structure may be essential for antibiotic activity including phospholipid vesicle-disrupting property.

ISSN 

1225-8687

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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