Premium
Exploring the Antibacterial and Hemolytic Activity of Shorter‐ and Longer‐Chain β ‐, α , β ‐, and γ ‐Peptides, and of β ‐Peptides from β 2 ‐3‐Aza‐ and β 3 ‐2‐Methylidene‐amino Acids Bearing Proteinogenic Side Chains – A Survey
Author(s) -
Arvidsson Per I.,
Ryder Neil S.,
Weiss H. Markus,
Hook David F.,
Escalante Jaime,
Seebach Dieter
Publication year - 2005
Publication title -
chemistry and biodiversity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.427
H-Index - 70
eISSN - 1612-1880
pISSN - 1612-1872
DOI - 10.1002/cbdv.200590020
Subject(s) - chemistry , hemolysis , enterococcus faecalis , peptide , klebsiella pneumoniae , staphylococcus aureus , antibacterial activity , pseudomonas aeruginosa , escherichia coli , biochemistry , amphiphile , antibacterial peptide , bacteria , microbiology and biotechnology , biology , copolymer , polymer , genetics , organic chemistry , immunology , gene
The antibacterial activities of 31 different β ‐, mixed α / β ‐, and γ ‐peptides, as well as of β ‐peptides derived from β 2 ‐3‐aza‐ and β 3 ‐2‐methylidene‐amino acids were assayed against six pathogens ( Enterococcus faecalis, Staphylococcus aureus, Streptococcus pneumoniae, Escherichia coli, Klebsiella pneumoniae , and Pseudomonas aeruginosa ), and the results were compared with literature data. The interaction of these peptides with mammalian cells, as modeled by measuring the hemolysis of human erythrocytes, was also investigated. In addition to those peptides designed to fold into amphiphilic helical conformations with positive charges on one face of the helix, one new peptide with hemolytic activity was detected within the sample set. Moreover, it was demonstrated that neither cationic peptides used for membrane translocation ( β 3 ‐oligoarginines), nor mixed α / β ‐ or γ ‐peptides with somatostatin‐mimicking activities display unwanted hemolytic activity.