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Title 

CRAMP Analogues Having Potent Antibiotic Activity against Bacterial, Fungal, and Tumor Cells without Hemolytic Activity

Authors 

Song Yub ShinShin Won KangDong Gun LeeSoo Hyun EomWoo Keun SongJae Il Kim

Publisher 

Elsevier

Issue Date 

2000

Citation 

Biochemical and Biophysical Research Communications, vol. 275, no. 3, pp. 904-909

Keywords 

cathelicidin-derived antimicrobial peptideCRAMP-18hemolytic activitylys-substitutioncramp 18polypeptide antibiotic agentantineoplastic activitybactericidal activityfungicidal activityhuman cell

Abstract 

CRAMP-18 (GEKLKKIGQKIKNFFQKL) is the anti-bacterial sequence derived from CRMAP, a member of cathelicidin-derived antimicrobial peptides. To develop the novel antibiotic peptides useful as therapeutic drugs requires strong antibiotic activity against bacterial and fungal cells without hemolytic effect. To this goal, the analogues were designed to increase only net positively charge by Lys-substitution of positions 2, 9, 13, or 16 at the hydrophilic helix face of CRAMP-18 without any change at the hydrophobic helix face. In particular, Lys-substitution (K2-CRAMP-18) of position 2 in CRAMP-18 induced the enhanced antibiotic activity without any increase in hemolysis. Thus, this peptide may provide a useful template for the design novel antibiotic peptides for the treatment of infectious diseases. Additional CD spectra studies suggested that the α-helical structure of the peptides plays an important role in killing bacterial and fungal cells, but the increase of α-helical content is less connected with the enhanced antibiotic activity.

ISSN 

0006-291X

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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