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Effect of Chain Elongation on Biological Properties of the Toxin Paralysin β ‐Alanyl‐tyrosine
Author(s) -
Macurkova Anna,
Neubauerova Tereza,
Poncova Kristyna,
Jezek Rudolf,
Lovecka Petra,
Spiwok Vojtech,
Mackova Martina,
Macek Tomas
Publication year - 2014
Publication title -
chemical biology and drug design
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.59
H-Index - 77
eISSN - 1747-0285
pISSN - 1747-0277
DOI - 10.1111/cbdd.12257
Subject(s) - antimicrobial , tyrosine , hemolymph , biological activity , biochemistry , bacteria , escherichia coli , chemistry , biology , molecular mass , stereochemistry , microbiology and biotechnology , in vitro , enzyme , genetics , gene
In hemolymph of insect species, compounds with remarkable properties for pharmaceutical industry are present. At the first line, there were found compounds of low molecular mass, less than 1 kD a. One of such compounds, β ‐alanyl‐tyrosine (252 Da), was isolated from larval hemolymph of some species of holometabolous insects (e.g. Neobellieria bullata ). Its paralytic activity and antimicrobial properties were described until now. In this study, we present the effect of elongation of β ‐alanyl‐tyrosine by repeating of this motive on the biological and physical properties of prepared analogues. For assessment of antimicrobial properties of these new compounds strains of Gram‐positive, Gram‐negative bacteria and fungi were used, we also followed the haemolytic activity and toxic effect on human cell culture H ep G 2. On the base of ECD spectroscopy measurement, subsequent molecular modelling and known secondary structure of original β ‐alanyl‐tyrosine dipeptide, the secondary structures of repeating sequences of β ‐AY were specified. The repeating structures of β ‐alanyl‐tyrosine show increase in antimicrobial activity; for Escherichia coli , Staphylococcus aureus and Pseudomonas aeruginosa, minimal inhibitory concentration was decreased from 30 to 15 m m for 2x β ‐AY, 0.4 m m for 4x β ‐AY and 0.25 m m for 6x β ‐AY.