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Open AccessArticle

All d-Lysine Analogues of the Antimicrobial Peptide HPA3NT3-A2 Increased Serum Stability and without Drug Resistance

by Jong-Kook Lee 1,2 and Yoonkyung Park 1,2,*
1
Department of Biomedical Science, Chosun University, Gwangju 501-759, Korea
2
Research Center for Proteinaceous Materials (RCPM), Chosun University, Gwangju 501-759, Korea
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2020, 21(16), 5632; https://doi.org/10.3390/ijms21165632
Received: 17 June 2020 / Revised: 4 August 2020 / Accepted: 5 August 2020 / Published: 6 August 2020
Novel antibiotic drugs are urgently needed because of the increase in drug-resistant bacteria. The use of antimicrobial peptides has been suggested to replace antibiotics as they have strong antimicrobial activity and can be extracted from living organisms such as insects, marine organisms, and mammals. HPA3NT3-A2 ([Ala1,8] HPA3NT3) is an antimicrobial peptide that is an analogue of the HP (2–20) peptide derived from Helicobacter pylori ribosomal protein L1. Although this peptide was shown to have strong antimicrobial activity against drug-resistant bacteria, it also showed lower toxicity against sheep red blood cells (RBCs) and HaCaT cells compared to HPA3NT3. The l-Lys residues of HPA3NT3-A2 was substituted with d-Lys residues (HPA3NT3-A2D; [d-Lys2,5,6,9,10,15] HPA3NT3-A2) to prevent the cleavage of peptide bonds by proteolytic enzymes under physiological conditions. This peptide showed an increased half-life and maintained its antimicrobial activity in the serum against Escherichia coli (E. coli) and Staphylococcus aureus (S. aureus) (pathogen). Furthermore, the antimicrobial activity of HPA3NT3-A2D was not significantly affected in the presence of mono- or divalent ions (Na+, Mg2+, Ca2+). Finally, l- or d-HPA3NT3-A2 peptides exhibited the strongest antimicrobial activity against antibiotic-resistant bacteria and failed to induce resistance in Staphylococcus aureus after 12 passages. View Full-Text
Keywords: drug-resistant bacteria; sheep RBCs; d-enantiomer; antimicrobial peptide; physiological condition drug-resistant bacteria; sheep RBCs; d-enantiomer; antimicrobial peptide; physiological condition
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Lee, J.-K.; Park, Y. All d-Lysine Analogues of the Antimicrobial Peptide HPA3NT3-A2 Increased Serum Stability and without Drug Resistance. Int. J. Mol. Sci. 2020, 21, 5632.

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