Issue 21, 2024, Issue in Progress

Lysine-based non-cytotoxic ultrashort self-assembling peptides with antimicrobial activity

Abstract

Peptide-based molecules and their hydrogels are useful materials for biomedical applications due to the reversible nature of their self-assembly as well as the diversity of nanostructures that can be created starting from low-molecular weight compounds. In this study, we have focused on comprehending the characteristics of fibrillar networks of L-lysine-based self-assembled dipeptide hydrogels with a focus on their antibacterial properties. For that purpose, L-lysine has been complemented with hydrophobic aromatic moieties coming from L-phenylalanine and benzyloxyxarbonyl N-capping. In addition, the peptide C-terminus is blocked with alkylamides of different chain lengths which introduces additional dispersive interactions and hydrophobicity. These materials were well characterized by transmission electron microscopy, scanning electron microscopy, wide-angle powder X-ray diffraction and oscillatory rheology. Finally, biocompatibility and antimicrobial tests were performed showing that these hydrogels are compatible with HEK 293 cells and present a remarkable antibacterial activity against both Gram positive (S. aureus) and Gram negative (E. coli) bacteria.

Graphical abstract: Lysine-based non-cytotoxic ultrashort self-assembling peptides with antimicrobial activity

Supplementary files

Article information

Article type
Paper
Submitted
27 Dec 2023
Accepted
01 May 2024
First published
08 May 2024
This article is Open Access
Creative Commons BY-NC license

RSC Adv., 2024,14, 15120-15128

Lysine-based non-cytotoxic ultrashort self-assembling peptides with antimicrobial activity

N. Özbek, E. L. Vilarrocha, B. V. Jover, E. F. Ventura and B. Escuder, RSC Adv., 2024, 14, 15120 DOI: 10.1039/D3RA08883A

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