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In this study, a robust and straightforward method to covalently attach multi-functional hydrogel thin layers onto substrates was provided. In our strategy, double bonds were firstly introduced onto substrates to provide anchoring points for hydrogel layers, and then hydrogel thin layers were prepared via surface cross-linking copolymerization of the immobilized double bonds with functional monomers. Sulfobetaine methacrylate (SBMA), sodium allysulfonate (SAS), and methyl acryloyloxygen ethyl trimethyl ammonium chloride (METAC) were selected as functional monomers to form hydrogel layers onto polyether sulfone (PES) membrane surfaces, respectively. The thickness of the formed hydrogel layers could be controlled, and the layers showed excellent long-term stability. The PSBMA hydrogel layer exhibited superior antifouling property demonstrated by undetectable protein adsorption and excellent bacteria resistant property; after attaching PSAS hydrogel layer, the membrane showed incoagulable surface property when contacting with blood confirmed by the activated partial thromboplastin time (APTT) value exceeding 600s; while, the PMETAC hydrogel thin layer could effectively kill attached bacteria. The proposed method provides a new platform to directly modify material surfaces with desired properties, and thus has great potential to be widely used in designing materials for blood purification, drug delivery, wound dressing, and intelligent biosensors., (Copyright © 2016 Elsevier Inc. All rights reserved.)

In an in-vitro assay, rabbit serum, but not human serum, killed Listeria monocytogenes, a foodborne pathogen. The aim of our study was to purify and partially characterize this killing factor. Listericidin was purified from rabbit serum by a single-step ion-exchange chromatography with DEAE-Sephadex A-50 and its antimicrobial activity was assessed by a microdilution method. Listericidin is a protein with a molecular weight of 9 kDa and an isoelectric point of 8.1. It kills L. monocytogenes at 4°C, 25°C, and 37°C, and its activity is resistant to heat (boiling) and acidic conditions (pH <2). Listericidin's activity is inhibited by sodium chloride and various growth media, is sensitive to proteolytic enzymes and is enhanced by calcium chloride, and is neutralized by monoclonal antibodies to human complement C3a. However, the listericidin reacts weakly with these antibodies in an ELISA. The first 33 N-terminal residues of listericidin (SVQLTEKRMDKVGQYTNKELRKXXEDGMRDNPM) have homology to various complement C3a components. Listericidin also kills other Listeria spp., Vibrio spp., Salmonella spp., Escherichia spp., Cronobacter spp., and Bacillus spp. The listericidin peptide purified in a single-step chromatography is pH and heat stable, and has a broad antimicrobial spectrum against major foodborne pathogens in addition to L. monocytogenes.