Molecular design, pharmacology and toxicology optimization of antimicrobial peptide from Hydrophis cyanocinctus, Hc-CATH
Based on the cathelicidin family antimicrobial peptide Hc-CATH derived from sea snake, the Hc-16 and Hc-15 of 16 and 15 amino acid residues, were designed. By using CCK8, minimal inhibitory concentration, ELISA and bio-layer interferometry assays, their cytotoxicity, antibacterial activity, anti-inflammatory activity, and LPS neutralization activity was examined. Compared with Hc-15, Hc-16 had lower cytotoxicity and better broad-spectrum antibacterial activity against pathogens including clinically resistant bacteria, with the minimum inhibitory concentration of only 4.69 μg/mL. Hc-16 inhibited the expression of inflammatory cytokines of TNF-α and IL-6 induced by LPS, so as to significantly reduce the inflammatory response induced by infection. In addition, structure-activity relationship studies have shown that the phenylalanine at the C- and N-terminals of Hc-16 played a crucial role in its antibacterial and anti-inflammatory activity. Altogether, the designed Hc-16 has an excellent prospect to be developed into a novel antibiotic.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2021 |
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| Erschienen: |
2021 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:37 |
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| Enthalten in: |
Sheng wu gong cheng xue bao = Chinese journal of biotechnology - 37(2021), 7 vom: 25. Juli, Seite 2534-2542 |
| Sprache: |
Chinesisch |
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| Beteiligte Personen: |
Gao, Jiuxiang [VerfasserIn] |
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| Links: |
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| Themen: |
Anti-Bacterial Agents |
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| Anmerkungen: |
Date Completed 02.08.2021 Date Revised 02.08.2021 published: Print Citation Status MEDLINE |
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| doi: |
10.13345/j.cjb.200583 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM32872520X |
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| 245 | 1 | 0 | |a Molecular design, pharmacology and toxicology optimization of antimicrobial peptide from Hydrophis cyanocinctus, Hc-CATH |
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| 500 | |a Date Completed 02.08.2021 | ||
| 500 | |a Date Revised 02.08.2021 | ||
| 500 | |a published: Print | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Based on the cathelicidin family antimicrobial peptide Hc-CATH derived from sea snake, the Hc-16 and Hc-15 of 16 and 15 amino acid residues, were designed. By using CCK8, minimal inhibitory concentration, ELISA and bio-layer interferometry assays, their cytotoxicity, antibacterial activity, anti-inflammatory activity, and LPS neutralization activity was examined. Compared with Hc-15, Hc-16 had lower cytotoxicity and better broad-spectrum antibacterial activity against pathogens including clinically resistant bacteria, with the minimum inhibitory concentration of only 4.69 μg/mL. Hc-16 inhibited the expression of inflammatory cytokines of TNF-α and IL-6 induced by LPS, so as to significantly reduce the inflammatory response induced by infection. In addition, structure-activity relationship studies have shown that the phenylalanine at the C- and N-terminals of Hc-16 played a crucial role in its antibacterial and anti-inflammatory activity. Altogether, the designed Hc-16 has an excellent prospect to be developed into a novel antibiotic | ||
| 650 | 4 | |a Journal Article | |
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| 650 | 7 | |a Pore Forming Cytotoxic Proteins |2 NLM | |
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| 700 | 1 | |a Yu, Haining |e verfasserin |4 aut | |
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