6K4W

smart chimeric peptide SCP-A6

Summary for 6K4W

• Entry DOI: 10.2210/pdb6k4w/pdb
• Descriptor: SCP-A6 (1 entity in total)
• Functional Keywords: chimeric peptide, lipopolysaccharide, lbp14, antibacterial activity, anti-inflammatory activity, n6, antibiotic
• Biological source: Arenicola marina
• Total number of polymer chains: 1
• Total formula weight: 5178.02

Authors

Wang, J.H.,Liu, X.H. (deposition date: 2019-05-27, release date: 2019-06-12, Last modification date: 2024-05-15)

Primary citation

Wang, Z.,Liu, X.,Mao, R.,Hao, Y.,Yang, N.,Wang, X.,Li, Z.,Wang, X.,Wang, J.
Development of chimeric peptides to facilitate the neutralisation of lipopolysaccharides during bactericidal targeting of multidrug-resistant Escherichia coli.
Commun Biol, 3:41-41, 2020

PubMed Abstract: Pathogenic Escherichia coli can cause fatal diarrheal diseases in both animals and humans. However, no antibiotics or antimicrobial peptides (AMPs) can adequately kill resistant bacteria and clear bacterial endotoxin, lipopolysaccharide (LPS) which leads to inflammation and sepsis. Here, the LPS-targeted smart chimeric peptides (SCPs)-A6 and G6 are generated by connecting LPS-targeting peptide-LBP14 and killing domain-N6 via different linkers. Rigid and flexible linkers retain the independent biological activities from each component. SCPs-A6 and G6 exert low toxicity and no bacterial resistance, and they more rapidly kill multiple-drug-resistant E. coli and more effectively neutralize LPS toxicity than N6 alone. The SCPs can enhance mouse survival more effectively than N6 or polymyxin B and alleviate lung injuries by blocking mitogen-activated protein kinase and nuclear factor kappa-B p65 activation. These findings uniquely show that SCPs-A6 and G6 may be promising dual-function candidates as improved antibacterial and anti-endotoxin agents to treat bacterial infection and sepsis.

PubMed: 31974490
DOI: 10.1038/s42003-020-0761-3

Experimental method

SOLUTION NMR