"Clicking" an Ionic Liquid to a Potent Antimicrobial Peptide: On the Route towards Improved Stability

• Published in: International journal of molecular sciences Vol. 21; no. 17; p. 6174
• Main Authors: Gomes, Ana, Bessa, Lucinda J, Correia, Patrícia, Fernandes, Iva, Ferraz, Ricardo, Gameiro, Paula, Teixeira, Cátia, Gomes, Paula
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 26-08-2020; MDPI
• Subjects: Alkynes - chemistry; antibacterial; antibiofilm; Antibiotics; Antiinfectives and antibacterials; Antimicrobial agents; Antimicrobial peptides; Azides - chemistry; Bacteria; Biofilms; Biofilms - drug effects; Biofilms - growth & development; Cell Line; Clinical isolates; Communication; Cycloaddition Reaction - methods; Drug Resistance, Multiple, Bacterial - drug effects; Enzymes; Gram-negative bacteria; Gram-Negative Bacteria - drug effects; Gram-Negative Bacteria - growth & development; Gram-positive bacteria; Humans; Investigations; ionic liquid; Ionic liquids; Ionic Liquids - chemistry; Ionic Liquids - pharmacology; Ions; Klebsiella; Microbial Sensitivity Tests; Molecular Structure; Multidrug resistance; Multidrug resistant organisms; NMR; Nuclear magnetic resonance; peptide; Peptides; Pore Forming Cytotoxic Proteins - chemistry; Pore Forming Cytotoxic Proteins - pharmacology; skin infections; Stability; Tyrosinase; Wound healing; ionic liquid; multidrug resistance; peptide; wound healing; antibiofilm; skin infections; antibacterial; tyrosinase
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms21176174

A covalent conjugate between an antibacterial ionic liquid and an antimicrobial peptide was produced via "click" chemistry, and found to retain the parent peptide's activity against multidrug-resistant clinical isolates of Gram-negative bacteria, and antibiofilm action on a resistant clinical isolate of
, while exhibiting much improved stability towards tyrosinase-mediated modifications. This unprecedented communication is a prelude for the promise held by ionic liquids -based approaches as tools to improve the action of bioactive peptides.