Antibacterial non-glycosidase activity of invertebrate destabilase-lysozyme and of its helical amphipathic peptides

BACKGROUND: Since bactericidal properties of some lysozymes are independent of their glycosidase activity, we have investigated this phenomenon for destabilase-lysozyme (DL) from medicinal leech (Hirudo medicinalis). METHODS: Glycosidase activity was determined on Micrococcus luteus, non-enzymatic antibacterial activity of heat-treated DL and of synthetic peptides alpha1, alpha2 and alpha3 (fragments of its primary structure) on M. luteus, Escherichia coli, Bacillus brevis and Streptomyces chrysomallus. RESULTS: Glycosidase activity disappeared after the heating of native DL at 100 degrees C for 40 min. Antibacterial activity of heat-treated DL for M. luteus MDMSU128 and MDMSU140 expressed as minimal inhibitory concentration was 9.8.10(-8) and 12.10(-8) M, respectively, and to E. coli MDMSU52 11.10(-8) M. Antibacterial activity of synthetic peptide alpha1 for M. luteus MDMSU128 and for E. coli MDMSU52 was 8.3.10(-5) and 4.9.10(-5) M, respectively. CONCLUSION: DL is the first invertebrate lysozyme with combined enzymatic and non-enzymatic antibacterial action.

Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.

Heat-treated destabilase retains antibacterial activity (MIC 9.8-12x10^-8 M) against M. luteus and E. coli even with glycosidase function abolished.

Leech-derived molecules this paper discusses, each with a full profile in the ASH compound registry:

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