Effect of chain elongation on biological properties of the toxin paralysin β-alanyl-tyrosine
Jazyk angličtina Země Anglie, Velká Británie Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
24168419
DOI
10.1111/cbdd.12257
Knihovny.cz E-zdroje
- Klíčová slova
- Neobellieria bullata, fleshfly, metamorphosis, sarcophagin, solid phase peptide synthesis,
- MeSH
- aminokyselinové motivy MeSH
- antiinfekční látky chemie farmakologie MeSH
- biologické toxiny chemie farmakologie MeSH
- buňky Hep G2 MeSH
- dipeptidy chemie farmakologie MeSH
- houby účinky léků MeSH
- lidé MeSH
- mikrobiální testy citlivosti MeSH
- proliferace buněk účinky léků MeSH
- Staphylococcus aureus účinky léků MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- alanyltyrosine MeSH Prohlížeč
- antiinfekční látky MeSH
- biologické toxiny MeSH
- dipeptidy MeSH
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 kDa. 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 HepG2. 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 mM for 2xβ-AY, 0.4 mM for 4xβ-AY and 0.25 mM for 6xβ-AY.
Citace poskytuje Crossref.org
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