Antibiotic and hemolytic activity of a β2/β3 peptide capable of folding into a 12/10-helical secondary structure

被引：97

作者：

Arvidsson, PI

Ryder, NS

Weiss, HM

Gross, G

Kretz, O

Woessner, R

Seebach, D ^{[1
]}

机构：

[1] ETH Honggerberg, Organ Chem Lab, CH-8093 Zurich, Switzerland

[2] Uppsala Univ, Inst Chem, Dept Organ Chem, S-75124 Uppsala, Sweden

[3] Novartis Inst Biomed Res Inc, Infect Dis Biol, Cambridge, MA 02139 USA

[4] Novartis Pharma AG, Preclin Safety RW Exploratory Clin Dev, CH-4002 Basel, Switzerland

来源：

CHEMBIOCHEM | 2003年 / 4卷 / 12期

关键词：

amphiphiles; antibiotics; helical structures; peptides; peptidomimetics;

D O I：

10.1002/cbic.200300698

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Active peptide helices: The β-nonapeptide H-β 3HPhe-β2HVal-β3H Phe-β 2HLeu-β3HLys-β2HLeu-β 3HLys-β2HLeu-β3HPhe-OH with alternating β2- and β3-amino-acid residues has been tested for antibiotic and hemolytic activities. This represents the first case of biomimetic activity of a mixed" β3/β 2-peptide."

引用

页码：1345 / 1347

页数：3

共 48 条

[1] Syntheses and CD-spectroscopic investigations of longer-chain β-peptides:: Preparation by solid-phase couplings of single amino acids, dipeptides, and tripeptides [J].