CRAMP analogues having potent antibiotic activity against bacterial, fungal, and tumor cells without hemolytic activity.

Abstract:

:CRAMP-18 (GEKLKKIGQKIKNFFQKL) is the antibacterial 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 (K(2)-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 alpha-helical structure of the peptides plays an important role in killing bacterial and fungal cells, but the increase of alpha-helical content is less connected with the enhanced antibiotic activity.

authors

Shin SY,Kang SW,Lee DG,Eom SH,Song WK,Kim JI

doi

10.1006/bbrc.2000.3269

subject

Has Abstract

pub_date

2000-09-07 00:00:00

pages

904-9

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(00)93269-8

journal_volume

275

pub_type

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