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- W4205979191 abstract "Antimicrobial peptides (AMPs) are found in nearly all living organisms, show broad spectrum antibacterial activity, and can modulate the immune system. Furthermore, they have a very low level of resistance induction in bacteria, which makes them an ideal target for drug development and for targeting multi-drug resistant bacteria 'Superbugs'. Despite this promise, AMP therapeutic use is hampered as typically they are toxic to mammalian cells, less active under physiological conditions and are susceptible to proteolytic degradation. Research has focused on addressing these limitations by modifying natural AMP sequences by including e.g., d-amino acids and N-terminal and amino acid side chain modifications to alter structure, hydrophobicity, amphipathicity, and charge of the AMP to improve antimicrobial activity and specificity and at the same time reduce mammalian cell toxicity. Recently, multimerisation (dimers, oligomer conjugates, dendrimers, polymers and self-assembly) of natural and modified AMPs has further been used to address these limitations and has created compounds that have improved activity and biocompatibility compared to their linear counterparts. This review investigates how modifying and multimerising AMPs impacts their activity against bacteria in planktonic and biofilm states of growth." @default.
- W4205979191 created "2022-01-25" @default.
- W4205979191 creator A5027806957 @default.
- W4205979191 creator A5044751208 @default.
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- W4205979191 creator A5047172005 @default.
- W4205979191 creator A5053411244 @default.
- W4205979191 creator A5091489953 @default.
- W4205979191 date "2022-01-10" @default.
- W4205979191 modified "2023-09-30" @default.
- W4205979191 title "The Potential of Modified and Multimeric Antimicrobial Peptide Materials as Superbug Killers" @default.
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