CRAMP analog having potent antibiotic activity without hemolytic activity

Shin Won Kang; Gun Lee Dong; Sung Tae Yang; Yangmee Kim; Il Kim Jae; Kyung Soo Hahm; Yub Shin Song

doi:10.2174/0929866023408643

CRAMP analog having potent antibiotic activity without hemolytic activity

Shin Won Kang, Gun Lee Dong, Sung Tae Yang, Yangmee Kim, Il Kim Jae, Kyung Soo Hahm, Yub Shin Song

Chosun University

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

CRAMP-18 is an 18-residue functional region, corresponding to residues 16-33 of a mouse-derived antibiotic peptide CRAMP. To develop novel antibiotic peptides possessing strong antibiotic activity against bacterial, fungal and tumor cells without hemolytic activity, three analogs of CRAMP-18 were synthesized containing either Leu- or Lys-substitution. Leu-substitution ([L^{1, 8}]-CRAMP-18) in the hydrophobic helix face of CRAMP-18 induced a dramatic increase in antibiotic activity without a significant increase in hemolytic activity. Lys-substitution ([K^{2, 13}]-CRAMP-18 or [K^{9, 16}]-CRAMP-18) in the hydrophilic helix face produced a smaller response. Therefore, [L^{1, 8}]-CRAMP-18 may be an attractive candidate for developing novel peptide antibiotics.

Original language	English
Pages (from-to)	275-282
Number of pages	8
Journal	Protein and Peptide Letters
Volume	9
Issue number	4
DOIs	https://doi.org/10.2174/0929866023408643
State	Published - 2002

Keywords

[L]-CRAMP-18
Antibiotic activity
Antibiotic peptide
CRAMP
CRAMP-18
Hemolytic activity

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10.2174/0929866023408643

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title = "CRAMP analog having potent antibiotic activity without hemolytic activity",

abstract = "CRAMP-18 is an 18-residue functional region, corresponding to residues 16-33 of a mouse-derived antibiotic peptide CRAMP. To develop novel antibiotic peptides possessing strong antibiotic activity against bacterial, fungal and tumor cells without hemolytic activity, three analogs of CRAMP-18 were synthesized containing either Leu- or Lys-substitution. Leu-substitution ([L1, 8]-CRAMP-18) in the hydrophobic helix face of CRAMP-18 induced a dramatic increase in antibiotic activity without a significant increase in hemolytic activity. Lys-substitution ([K2, 13]-CRAMP-18 or [K9, 16]-CRAMP-18) in the hydrophilic helix face produced a smaller response. Therefore, [L1, 8]-CRAMP-18 may be an attractive candidate for developing novel peptide antibiotics.",

keywords = "[L]-CRAMP-18, Antibiotic activity, Antibiotic peptide, CRAMP, CRAMP-18, Hemolytic activity",

author = "Kang, {Shin Won} and Dong, {Gun Lee} and Yang, {Sung Tae} and Yangmee Kim and Jae, {Il Kim} and Hahm, {Kyung Soo} and Song, {Yub Shin}",

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doi = "10.2174/0929866023408643",

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journal = "Protein and Peptide Letters",

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T1 - CRAMP analog having potent antibiotic activity without hemolytic activity

AU - Kang, Shin Won

AU - Dong, Gun Lee

AU - Yang, Sung Tae

AU - Kim, Yangmee

AU - Jae, Il Kim

AU - Hahm, Kyung Soo

AU - Song, Yub Shin

PY - 2002

Y1 - 2002

N2 - CRAMP-18 is an 18-residue functional region, corresponding to residues 16-33 of a mouse-derived antibiotic peptide CRAMP. To develop novel antibiotic peptides possessing strong antibiotic activity against bacterial, fungal and tumor cells without hemolytic activity, three analogs of CRAMP-18 were synthesized containing either Leu- or Lys-substitution. Leu-substitution ([L1, 8]-CRAMP-18) in the hydrophobic helix face of CRAMP-18 induced a dramatic increase in antibiotic activity without a significant increase in hemolytic activity. Lys-substitution ([K2, 13]-CRAMP-18 or [K9, 16]-CRAMP-18) in the hydrophilic helix face produced a smaller response. Therefore, [L1, 8]-CRAMP-18 may be an attractive candidate for developing novel peptide antibiotics.

AB - CRAMP-18 is an 18-residue functional region, corresponding to residues 16-33 of a mouse-derived antibiotic peptide CRAMP. To develop novel antibiotic peptides possessing strong antibiotic activity against bacterial, fungal and tumor cells without hemolytic activity, three analogs of CRAMP-18 were synthesized containing either Leu- or Lys-substitution. Leu-substitution ([L1, 8]-CRAMP-18) in the hydrophobic helix face of CRAMP-18 induced a dramatic increase in antibiotic activity without a significant increase in hemolytic activity. Lys-substitution ([K2, 13]-CRAMP-18 or [K9, 16]-CRAMP-18) in the hydrophilic helix face produced a smaller response. Therefore, [L1, 8]-CRAMP-18 may be an attractive candidate for developing novel peptide antibiotics.

KW - [L]-CRAMP-18

KW - Antibiotic activity

KW - Antibiotic peptide

KW - CRAMP

KW - CRAMP-18

KW - Hemolytic activity

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U2 - 10.2174/0929866023408643

DO - 10.2174/0929866023408643

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VL - 9

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JO - Protein and Peptide Letters

JF - Protein and Peptide Letters

IS - 4

ER -

CRAMP analog having potent antibiotic activity without hemolytic activity

Abstract

Keywords

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