XXII. BIOCHEMICKÝ ZJAZD - Jesseniova lekárska fakulta

Posters
17.
CLONING, EXPrESSION aND aNTIMICrOBIal aCTIvITY of THE HUMan
caTHELICIDIN LL-37
Csaba Tóth 1 , Roland Pálffy 1 , Juraj Gašperík 2 , Stanislav Stuchlík 1 and Ján Turňa 1
1
Department of molecular biology, Faculty of Natural Sciences, Comenius University,
2
Institute of Molecular Biology, SAS Bratislava
Antimicrobial peptides are short polypeptides involved in the innate immunity system
and they can be found among all classes of life. They demonstrate antimicrobial activity
against Gram-negative and Gram-positive bacteria, viruses, fungal pathogens and cancerous
cells. LL-37 is a multifunctional peptide and the only antimicrobial peptide from
the cathelicidin family found in human. It is mainly expressed in myeloid cells, where it
is located in specific granules, but it was also described in inflamed skin, testis, wound
fluid, lung epithelia, sweat and saliva. Apart from its’ wide spectrum of bactericidal activity,
LL-37 also plays an important role in the regulation of the inflammatory response,
neutralization of LPS and the promotion of wound healing.
As the therapeutical and commercial importance of these peptides is rising, simple
expression and purification systems will be needed for their large-scale production.
We have designed and prepared a cost-effective and efficient expression system for
the production of LL-37 in fusion with ketosteroid isomerase in E. coli cells. After the
purification and activation of the peptide, we have tested its’ biological activity against
various bacterial pathogens.
132 XXII. Biochemistry Congress, Martin