Antimicrobial activity of the antibacterial peptide PMAP-36 and its analogues
Copyright © 2019 Elsevier Ltd. All rights reserved..
The growing problem of antibiotic resistance has attracted people's attention; thus, the search for new antibacterial agents is imminent. In this study, a series of antimicrobial peptides (AMPs) based on the porcine antibacterial peptide PMAP-36 were designed by amino acid substitution to develop peptide analogues as new classes of antimicrobial agents. By extending the α-helix and increasing the positive charge, two peptide analogues, PMAP-36PW and PMAP-36PK, were synthesized. The antibacterial activities of PMAP-36 and its peptide analogues were detected in vitro and in vivo. The results showed that PMAP-36PW and PMAP-36PK had a broadened antibacterial spectrum compared to that of PMAP-36. After the modification, PMAP-36PW and PMAP-36PK exhibited antibacterial activities on swine Escherichia coli K88, while PMAP-36 did not. PMAP-36, PMAP-36PW and PMAP-36PK did not have antibacterial activities against Enterococcus faecium B21. PMAP-36 PW had significant antibacterial activity against seven bacterial strains compared to PMAP-36, and PMAP-36PK had significant antibacterial activity against five bacterial strains compared to PMAP-36. Furthermore, PMAP-36PW exhibited enhanced pH stability. Moreover, in the in vivo efficacy assessment of mice infected with Salmonella choleraesuis C78-1 and Listeria monocytogenes CICC 21533, the peptide analogues exhibited an impressive therapeutic effect by reducing bacterial gene copies and decreasing inflammatory damage in mouse livers and lungs, resulting in a reduction in mouse mortality. This study provides reference data for the design of clinically effective antibacterial peptides.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2019 |
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| Erschienen: |
2019 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:136 |
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| Enthalten in: |
Microbial pathogenesis - 136(2019) vom: 15. Nov., Seite 103712 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Zhou, Jiangfei [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 10.03.2020 Date Revised 10.03.2020 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.micpath.2019.103712 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM301004943 |
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| 520 | |a Copyright © 2019 Elsevier Ltd. All rights reserved. | ||
| 520 | |a The growing problem of antibiotic resistance has attracted people's attention; thus, the search for new antibacterial agents is imminent. In this study, a series of antimicrobial peptides (AMPs) based on the porcine antibacterial peptide PMAP-36 were designed by amino acid substitution to develop peptide analogues as new classes of antimicrobial agents. By extending the α-helix and increasing the positive charge, two peptide analogues, PMAP-36PW and PMAP-36PK, were synthesized. The antibacterial activities of PMAP-36 and its peptide analogues were detected in vitro and in vivo. The results showed that PMAP-36PW and PMAP-36PK had a broadened antibacterial spectrum compared to that of PMAP-36. After the modification, PMAP-36PW and PMAP-36PK exhibited antibacterial activities on swine Escherichia coli K88, while PMAP-36 did not. PMAP-36, PMAP-36PW and PMAP-36PK did not have antibacterial activities against Enterococcus faecium B21. PMAP-36 PW had significant antibacterial activity against seven bacterial strains compared to PMAP-36, and PMAP-36PK had significant antibacterial activity against five bacterial strains compared to PMAP-36. Furthermore, PMAP-36PW exhibited enhanced pH stability. Moreover, in the in vivo efficacy assessment of mice infected with Salmonella choleraesuis C78-1 and Listeria monocytogenes CICC 21533, the peptide analogues exhibited an impressive therapeutic effect by reducing bacterial gene copies and decreasing inflammatory damage in mouse livers and lungs, resulting in a reduction in mouse mortality. This study provides reference data for the design of clinically effective antibacterial peptides | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Antibacterial activity | |
| 650 | 4 | |a Antibacterial peptide PMAP-36 | |
| 650 | 4 | |a Antibacterial peptide PMAP-36PK | |
| 650 | 4 | |a Antibacterial peptide PMAP-36PW | |
| 650 | 4 | |a Antimicrobial susceptibility testing | |
| 650 | 7 | |a Anti-Infective Agents |2 NLM | |
| 650 | 7 | |a Antimicrobial Cationic Peptides |2 NLM | |
| 650 | 7 | |a PMAP-36 |2 NLM | |
| 650 | 7 | |a Recombinant Proteins |2 NLM | |
| 700 | 1 | |a Liu, Yongqing |e verfasserin |4 aut | |
| 700 | 1 | |a Shen, Tengfei |e verfasserin |4 aut | |
| 700 | 1 | |a Chen, Liangliang |e verfasserin |4 aut | |
| 700 | 1 | |a Zhang, Cong |e verfasserin |4 aut | |
| 700 | 1 | |a Cai, Kairui |e verfasserin |4 aut | |
| 700 | 1 | |a Liao, Chengshui |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Chen |e verfasserin |4 aut | |
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