3 years ago

Antibacterial activity and cytotoxycity of gelatine-conjugated lysine-based peptides

Amram Mor, Maja Kaisersberger Vincek, Vanja Kokol, Selestina Gorgieva
The effect of the coupling approach (chemical by using carbodiimide chemistry, and enzymatic by using transglutaminase) of a hydrophilic ɛ-poly-L-lysine (ɛPL) and a structurally-hydrophobic oligo-acyl-lysyl (OAK) to a gelatine (GEL) macromolecule, and their antibacterial activity against Gram-negative E. coli and Gram-positive S. aureus bacteria, as well as cytotoxicity to human osteoblast cells was studied as potential macromolecules for biomedical applications. Different spectroscopic (ultraviolet-visible, infrared, fluorescence, and electron paramagnetic resonance) and separation (size-exclusion chromatography and capillary zone electrophoresis) techniques, as well as zeta-potential analysis were performed to confirm the ɛPL/OAK covalent coupling and to determine their amount and orientation of the immobilization. The highest and kinetically the fastest reduction of bacteria (≥77% against E. coli vs. ≥82% against S. aureus) was achieved with GEL functionalized with ɛPL/OAK by the chemical grafting-to approach being correlated with conformationally the highly-flexible ˝brush-like˝ orientation linkage of peptides, enable its targeted and rapid interactions with bacteria membrane. The up to 400-fold lower yield of OAKs being immobilized may be related also to its cationic charge and hydrophobic alkyl chain moieties, compared to more hydrophilic ɛPL easily causing random polymerization and self-conjugation. The ɛPL/OAK-functionalized GEL did not induce citotoxicity to osteoblasts, even at ∼25-fold higher concentration than bacterial minimum inhibitory (MIC) concentration of ɛPL/OAK. © 2017 Wiley Periodicals, Inc. J Biomed Mater Res Part A, 2017.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/jbm.a.36164

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