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Micellization of Lipopeptides Containing Toll-like Receptor Agonist and Integrin Binding Sequences.

ACS Appl Mater Interfaces

December 2024

School of Chemistry, Food Biosciences and Pharmacy, University of Reading, Whiteknights, Reading RG6 6AD, U.K.

Short bioactive peptide sequences are of great interest in biomaterials development. We investigate the self-assembly of a lipopeptide containing both the highly cationic CSK toll-like receptor agonist hexapeptide sequence and RGDS integrin-binding motif, i.e.

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Development of lipopeptide-based HIV-1/2 fusion inhibitors targeting the gp41 pocket site with a new design strategy.

Antiviral Res

December 2024

NHC Key Laboratory of Systems Biology of Pathogens, National Institute of Pathogen Biology, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, 100730, China; Center for AIDS Research, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, 100730, China. Electronic address:

Emerging studies demonstrate that lipid conjugation is a vital strategy for designing peptide-based viral fusion inhibitors, and the so-called lipopeptides exhibit greatly improved antiviral activity. In the design of lipopeptides, a flexible linker between the peptide sequence and lipid molecule is generally required, mostly with a short polyethylene glycol or glycine-serine sequence. Very recently, we discovered that the helix-facilitating amino acid sequence "EAAAK" as a rigid linker is a more efficient method in the design of SARS-CoV-2 fusion inhibitory lipopeptides.

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Article Synopsis
  • * Two specific bacteriophages (vB_kpnM_05 and vB_kpnP_08) were isolated from Thai wastewater and demonstrated effectiveness against a high percentage of drug-resistant K. pneumoniae strains, showing rapid replication and stability under different conditions.
  • * A phage cocktail combining these two phages alongside the antibiotic amikacin exhibited enhanced antibacterial activity, preventing bacterial regrowth and highlighting a promising therapeutic approach to combat XDR K. pneumoniae infections.
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Combined antimicrobial activity of short peptide and phage-derived endolysin against antibiotic-resistant Salmonella Typhimurium.

Food Microbiol

January 2025

Department of Biomedical Science, Kangwon National University, Chuncheon, Gangwon, 24341, Republic of Korea; Future Food Laboratory, Innovation Center of Yangtze River Delta, Zhejiang University, Jiaxing, Zhejiang, 314100, China. Electronic address:

This study was designed to evaluate the combination effects of antimicrobial peptides (FK13 and FK16) and phage-encoded endolysin (LysPB32) on the inhibition of growth of polymyxin B-resistant Salmonella Typhimurium ATCC 19585 (ST). The inhibitory effects of FK13, FK16, and LysPB32 against ST were evaluated by using antimicrobial susceptibility, membrane permeability, biofilm reduction, cross-resistance, and mutant frequency assay. The minimum inhibitory concentrations (MICs) of FK13 and FK16 treated with LysPB32 (FK13+LysPB32 and FK16+LysPB32) against ST were decreased from more than 512 to 128 μg/ml and from 64 to 32 μg/ml, respectively.

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Background: Wastewaters are considered as important players in the spread of antimicrobial resistance, thus affecting the health of humans and animals. Here, we focused on wastewaters as a possible source of carbapenemase-producing Enterobacterales for the environment.

Methods: A total of 180 presumptive coliforms from hospital and municipal wastewaters, and a river in the Czech Republic were obtained by selective cultivation on meropenem-supplemented media and tested for presence of carbapenemase-encoding genes by PCR.

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