A one-enzyme strategy to release an antimicrobial peptide from the LFampin-domain of bovine lactoferrin |
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Authors: | Bolscher Jan G M van der Kraan Marieke I A Nazmi Kamran Kalay Hakan Grün Christian H Van't Hof Wim Veerman Enno C I Nieuw Amerongen Arie V |
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Institution: | Department of Oral Biochemistry, Academic Centre for Dentistry Amsterdam (ACTA), Vrije Universiteit and Universiteit van Amsterdam, Van der Boechorststraat 7, NL-1081BT Amsterdam, The Netherlands. jgm.bolscher@vumc.nl |
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Abstract: | Antimicrobial peptides have been found throughout living nature, yet antimicrobial sequences may still lie hidden within a wide variety of proteins. A rational strategy was developed to select interesting domains, based on the presumed common features of antimicrobial peptides, and to release these from accessible and safe proteins. In silico proteolysis simulations of bovine lactoferrin (bLF) with selected endoproteinases predicted the liberation of peptides that encompasses a cationic amphipathic alpha-helix. Three predicted peptides were synthesized and tested for their biological activity, demonstrating that one single enzyme was sufficient to obtain an antimicrobial peptide. The proof of principle demonstrated that a 32-mer fragment isolated from the endoproteinase AspN digestion of bLF possessed strong antimicrobial activity. Moreover, desalted crude digest had improved activity over native bLF. Hence, selective digestion of bLF increases its antimicrobial activity by release of antimicrobial stretches. |
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