| Novel β-Hairpin Antimicrobial Peptide Containing the β-Turn Sequence of -NG- and the Tryptophan Zippers Facilitate Self-Assembly into Nanofibers, Exhibiting Excellent Antimicrobial Performance | |
| 2024-03-04 | |
| Online publication date | 2024-03 |
| Source Publication | JOURNAL OF MEDICINAL CHEMISTRY Impact Factor & Quartile Of Published Year The Latest Impact Factor & Quartile |
| ISSN | 0022-2623 |
| EISSN | 1520-4804 |
| page numbers | 19 |
| Abstract | Antimicrobial peptides (AMPs) have emerged as promising agents to combat the antibiotic resistance crisis due to their rapid bactericidal activity and low propensity for drug resistance. However, AMPs face challenges in terms of balancing enhanced antimicrobial efficacy with increased toxicity during modification processes. In this study, de novo d-type beta-hairpin AMPs are designed. The conformational transformation of self-assembling peptide W-4 in the environment of the bacterial membrane and the erythrocyte membrane affected its antibacterial activity and hemolytic activity and finally showed a high antibacterial effect and low toxicity. Furthermore, W-4 displays remarkable stability, minimal occurrence of drug resistance, and synergistic effects when combined with antibiotics. The in vivo studies confirm its high safety and potent wound-healing properties at the sites infected by bacteria. This study substantiates that nanostructured AMPs possess enhanced biocompatibility. These advances reveal the superiority of self-assembled AMPs and contribute to the development of nanoantibacterial materials. |
| Publisher | AMER CHEMICAL SOC |
| DOI | 10.1021/acs.jmedchem.3c02339 |
| Indexed By | SCIE |
| Language | 英语 |
| WOS Research Area | Pharmacology & Pharmacy |
| WOS Subject | Chemistry, Medicinal |
| WOS ID | WOS:001179769000001 |
| Original Document Type | Article ; Early Access |
| PMID | 38436574 |
| Citation statistics | |
| Document Type | 期刊论文 |
| Identifier | https://ir.lzu.edu.cn/handle/262010/585130 |
| Collection | 基础医学院 |
| Affiliation | 1.Lanzhou Univ, Chinese Acad Med Sci, Sch Basic Med Sci, Key Lab Preclin Study New Drugs Gansu Prov,Inst Ph, Lanzhou 730000, Peoples R China; 2.Lanzhou Univ, Chinese Acad Med Sci, Res Unit Peptide Sci, 2019RU066, Lanzhou 730000, Peoples R China; 3.Chinese Acad Med Sci & Peking Union Med Coll, Inst Mat Med, State Key Lab Bioact Subst & Funct Nat Med, Beijing 100050, Peoples R China |
| First Author Affilication | School of Basic Medical Sciences; Lanzhou University |
| First Signature Affilication | School of Basic Medical Sciences |
| Recommended Citation GB/T 7714 | Li, Beibei,Ouyang, Xu,Liu, Yao,et al. Novel β-Hairpin Antimicrobial Peptide Containing the β-Turn Sequence of -NG- and the Tryptophan Zippers Facilitate Self-Assembly into Nanofibers, Exhibiting Excellent Antimicrobial Performance[J]. JOURNAL OF MEDICINAL CHEMISTRY,2024. |
| APA | Li, Beibei.,Ouyang, Xu.,Liu, Yao.,Ba, Zufang.,Yang, Yinyin.,...&Ni, Jingman.(2024).Novel β-Hairpin Antimicrobial Peptide Containing the β-Turn Sequence of -NG- and the Tryptophan Zippers Facilitate Self-Assembly into Nanofibers, Exhibiting Excellent Antimicrobial Performance.JOURNAL OF MEDICINAL CHEMISTRY. |
| MLA | Li, Beibei,et al."Novel β-Hairpin Antimicrobial Peptide Containing the β-Turn Sequence of -NG- and the Tryptophan Zippers Facilitate Self-Assembly into Nanofibers, Exhibiting Excellent Antimicrobial Performance".JOURNAL OF MEDICINAL CHEMISTRY (2024). |
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