Research ExplorerPublicationsModified CLEC3A-Derived Antimicrobial Peptides Lead to Enhan...

Modified CLEC3A-Derived Antimicrobial Peptides Lead to Enhanced Antimicrobial Activity against Drug-Resistant Bacteria

Standard

Modified CLEC3A-Derived Antimicrobial Peptides Lead to Enhanced Antimicrobial Activity against Drug-Resistant Bacteria. / Meinberger, Denise; Drexelius, Marco G; Grabeck, Joshua; Hermes, Gabriele; Roth, Annika; Elezagic, Dzemal; Neundorf, Ines; Streichert, Thomas; Klatt, Andreas R.

In: ANTIBIOTICS-BASEL, Vol. 12, No. 10, 11.10.2023, p. 1532.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Meinberger, D, Drexelius, MG, Grabeck, J, Hermes, G, Roth, A, Elezagic, D, Neundorf, I, Streichert, T & Klatt, AR 2023, 'Modified CLEC3A-Derived Antimicrobial Peptides Lead to Enhanced Antimicrobial Activity against Drug-Resistant Bacteria', ANTIBIOTICS-BASEL, vol. 12, no. 10, pp. 1532. https://doi.org/10.3390/antibiotics12101532

APA

Meinberger, D., Drexelius, M. G., Grabeck, J., Hermes, G., Roth, A., Elezagic, D., Neundorf, I., Streichert, T., & Klatt, A. R. (2023). Modified CLEC3A-Derived Antimicrobial Peptides Lead to Enhanced Antimicrobial Activity against Drug-Resistant Bacteria. ANTIBIOTICS-BASEL, 12(10), 1532. https://doi.org/10.3390/antibiotics12101532

Vancouver

Meinberger D, Drexelius MG, Grabeck J, Hermes G, Roth A, Elezagic D et al. Modified CLEC3A-Derived Antimicrobial Peptides Lead to Enhanced Antimicrobial Activity against Drug-Resistant Bacteria. ANTIBIOTICS-BASEL. 2023 Oct 11;12(10):1532. https://doi.org/10.3390/antibiotics12101532

Bibtex

@article{b904d71f196e46dda3ff51f7e419b441,
title = "Modified CLEC3A-Derived Antimicrobial Peptides Lead to Enhanced Antimicrobial Activity against Drug-Resistant Bacteria",
abstract = "Antimicrobial peptides (AMPs) represent a promising alternative to conventional antibiotics. Sequence changes can significantly improve the therapeutic properties of antimicrobial peptides. In our study, we apply different sequence modifications to enhance the performance of the CLEC3A-derived AMPs HT-16 and HT-47. We truncated their sequences, inserting a triple-glycine linker, adding an N-terminal tryptophan residue, and generating a D-amino acid variant, resulting in the generation of seven new peptides. We investigated their antimicrobial activity against gram-positive and gram-negative bacteria, their cytotoxicity to murine cells, and the biostability of the modified peptides in serum. We identified a novel antimicrobial peptide, WRK-30, with enhanced antimicrobial potency against S. aureus and MRSA. Additionally, WRK-30 was less cytotoxic to eukaryotic cells, allowing its application in higher concentrations in an in vivo setting. In conclusion, we identified a novel CLEC3A-derived antimicrobial peptide WRK-30 with significantly improved therapeutic properties and the potential to widen the repertoire of conventional antibiotics.",
author = "Denise Meinberger and Drexelius, {Marco G} and Joshua Grabeck and Gabriele Hermes and Annika Roth and Dzemal Elezagic and Ines Neundorf and Thomas Streichert and Klatt, {Andreas R}",
year = "2023",
month = oct,
day = "11",
doi = "10.3390/antibiotics12101532",
language = "English",
volume = "12",
pages = "1532",
journal = "ANTIBIOTICS-BASEL",
issn = "2079-6382",
publisher = "MDPI Multidisciplinary Digital Publishing Institute",
number = "10",

}

RIS

TY - JOUR

T1 - Modified CLEC3A-Derived Antimicrobial Peptides Lead to Enhanced Antimicrobial Activity against Drug-Resistant Bacteria

AU - Meinberger, Denise

AU - Drexelius, Marco G

AU - Grabeck, Joshua

AU - Hermes, Gabriele

AU - Roth, Annika

AU - Elezagic, Dzemal

AU - Neundorf, Ines

AU - Streichert, Thomas

AU - Klatt, Andreas R

PY - 2023/10/11

Y1 - 2023/10/11

N2 - Antimicrobial peptides (AMPs) represent a promising alternative to conventional antibiotics. Sequence changes can significantly improve the therapeutic properties of antimicrobial peptides. In our study, we apply different sequence modifications to enhance the performance of the CLEC3A-derived AMPs HT-16 and HT-47. We truncated their sequences, inserting a triple-glycine linker, adding an N-terminal tryptophan residue, and generating a D-amino acid variant, resulting in the generation of seven new peptides. We investigated their antimicrobial activity against gram-positive and gram-negative bacteria, their cytotoxicity to murine cells, and the biostability of the modified peptides in serum. We identified a novel antimicrobial peptide, WRK-30, with enhanced antimicrobial potency against S. aureus and MRSA. Additionally, WRK-30 was less cytotoxic to eukaryotic cells, allowing its application in higher concentrations in an in vivo setting. In conclusion, we identified a novel CLEC3A-derived antimicrobial peptide WRK-30 with significantly improved therapeutic properties and the potential to widen the repertoire of conventional antibiotics.

AB - Antimicrobial peptides (AMPs) represent a promising alternative to conventional antibiotics. Sequence changes can significantly improve the therapeutic properties of antimicrobial peptides. In our study, we apply different sequence modifications to enhance the performance of the CLEC3A-derived AMPs HT-16 and HT-47. We truncated their sequences, inserting a triple-glycine linker, adding an N-terminal tryptophan residue, and generating a D-amino acid variant, resulting in the generation of seven new peptides. We investigated their antimicrobial activity against gram-positive and gram-negative bacteria, their cytotoxicity to murine cells, and the biostability of the modified peptides in serum. We identified a novel antimicrobial peptide, WRK-30, with enhanced antimicrobial potency against S. aureus and MRSA. Additionally, WRK-30 was less cytotoxic to eukaryotic cells, allowing its application in higher concentrations in an in vivo setting. In conclusion, we identified a novel CLEC3A-derived antimicrobial peptide WRK-30 with significantly improved therapeutic properties and the potential to widen the repertoire of conventional antibiotics.

U2 - 10.3390/antibiotics12101532

DO - 10.3390/antibiotics12101532

M3 - SCORING: Journal article

C2 - 37887233

VL - 12

SP - 1532

JO - ANTIBIOTICS-BASEL

JF - ANTIBIOTICS-BASEL

SN - 2079-6382

IS - 10

ER -