@article{open1726,
          volume = {139},
          number = {2},
           month = {January},
          author = {Santi M Mandal and William F Porto and Debasis De and Ajit Phule and Suresh Korpole and Ananta K Ghosh and Sanat K Roy and Octavio L Franco},
            note = {Copyright of this article belongs to RSC.},
           title = {Screening of serine protease inhibitors with antimicrobial activity using iron oxide nanoparticles functionalized with dextran conjugated trypsin and in silico analyses of bacterial serine protease inhibition.},
       publisher = {Royal Society of Chemistry},
            year = {2014},
         journal = {Analyst},
           pages = {464--72},
        keywords = {Antimicrobial},
             url = {http://crdd.osdd.net/open/1726/},
        abstract = {Plants produce a variety of proteins and peptides which are involved in their defense against pathogens. Serine protease inhibitors are a well-established class of inhibitors correlated with plant defense. Increased levels of protease inhibitors delay cell damage and expand the cell's life-span. Recently, the rapid emergence of antibiotic-resistant microbial pathogens has prompted immense interest in purifying novel antimicrobial proteins or peptides from plant sources. Usually, the purification of protease inhibitors is accomplished by salt-extraction, ultrafiltration and affinity chromatography. Here, we developed a novel approach based on iron oxide nanoparticles conjugated to dextran functionalized with trypsin beads that accelerate the quick screening and purification of antimicrobial peptides with serine protease inhibitor activity. The method described here also works for screening other inhibitors using particular protein kinases, and it is therefore a novel tool for use as the leading method in the development of novel antimicrobial agents with protease inhibitory activity. Finally, and no less important, molecular modelling and dynamics studies of a homologous inhibitor studied here with Escherichia coli trypsin and chymotrypsin are provided in order to shed some light on inhibitor-enzyme interactions.}
}