| Short, mirror-symmetric antimicrobial peptides centered on ?RRR? have broad-spectrum antibacterial activity with low drug resistance and toxicity | |
Zhang, Fangyan1,2,3,4; Yang, Ping1,2,3,4; Mao, Wenbo1,2,3,4; Zhong, Chao1,2,3,4; Zhang, Jingying1,2,3,4; Chang, Linlin1,2,3,4; Wu, Xiaoyan1,2,3,4; Liu, H(刘晖)1,2,3,4 ; Zhang, Y(张云)1,2,3,4; Gou, Sanhu1,2,3,4; Ni, JM(倪京满)1,2,3,4 | |
| 2022-12-01 | |
| Source Publication | ACTA BIOMATERIALIA
 |
| ISSN | 1742-7061 |
| Volume | 154Pages:145-167 |
| Abstract | The increasingly severe bacterial resistance worldwide pushes people to discover and design potential antibacterial drugs unavoidably. In this work, a series of short, mirror-symmetric peptides were designed and successfully synthesized, centered on RRR and labeled with hydrophobic amino acids at both ends. Based on the structure-activity relationship analysis, LWWR (LWWRRRWWL-NH 2 ) was screened as a desirable mirror-symmetric peptide for further study. As expected, LWWR displayed broad-spectrum antibacterial activity against the standard bacteria and antibiotic-resistant strains. Undoubtedly, the high stability of LWWR in a complex physiological environment was an essential guarantee to maximizing its antibacterial activity. Indeed, LWWR also exhibited a rapid bactericidal speed and a low tendency to develop bacterial resistance, based on the multiple actions of non-receptor-mediated membrane actions and intra-cellular mechanisms. Surprisingly, although LWWR showed similar in vivo antibacterial activity compared with Polymyxin B and Melittin, the in vivo safety of LWWR was far higher than that of them, so LWWR had better therapeutic potential. In summary, the desirable mirror-symmetric peptide LWWR was promised as a potential antibacterial agent to confront the antibiotics resistance crisis. |
| Keyword | Antimicrobial peptides Mirror -symmetric structure Bacterial resistance Multiple mechanisms In vitro and in vivo |
| Publisher | ELSEVIER SCI LTD |
| DOI | 10.1016/j.actbio.2022.10.003 |
| Indexed By | SCIE |
| Language | 英语 |
| WOS Research Area | Engineering ; Materials Science |
| WOS Subject | Engineering, Biomedical ; Materials Science, Biomaterials |
| WOS ID | WOS:000898811900001 |
| Original Document Type | Article |
| Citation statistics | |
| Document Type | 期刊论文 |
| Identifier | https://ir.lzu.edu.cn/handle/262010/492660 |
| Collection | 药学院 |
| Affiliation | 1.Chinese Acad Med Sci, Peking Union Med Coll, Inst Mat Med, 2019RU066,1 Xian Nong Tan St, Beijing 100050, Peoples R China; 2.Chinese Acad Med Sci, Peking Union Med Coll, Res Unit Peptide Sci, 2019RU066,1 Xian Nong Tan St, Beijing 100050, Peoples R China; 3.Lanzhou Univ, Sch Pharm, Inst Pharmaceut, Lanzhou 730000, Peoples R China; 4.Lanzhou Univ, Sch Basic Med Sci, Key Lab Preclin Study New Drugs Gansu Prov, Lanzhou 730000, Peoples R China |
| First Author Affilication | School of Pharmacy; School of Basic Medical Sciences |
| Recommended Citation GB/T 7714 | Zhang, Fangyan,Yang, Ping,Mao, Wenbo,et al. Short, mirror-symmetric antimicrobial peptides centered on ?RRR? have broad-spectrum antibacterial activity with low drug resistance and toxicity[J]. ACTA BIOMATERIALIA,2022,154:145-167. |
| APA | Zhang, Fangyan.,Yang, Ping.,Mao, Wenbo.,Zhong, Chao.,Zhang, Jingying.,...&Ni, Jingman.(2022).Short, mirror-symmetric antimicrobial peptides centered on ?RRR? have broad-spectrum antibacterial activity with low drug resistance and toxicity.ACTA BIOMATERIALIA,154,145-167. |
| MLA | Zhang, Fangyan,et al."Short, mirror-symmetric antimicrobial peptides centered on ?RRR? have broad-spectrum antibacterial activity with low drug resistance and toxicity".ACTA BIOMATERIALIA 154(2022):145-167. |
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