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Bacteria produce a range of proteolytic enzymes, for which a number humanequivalent or structurally similar examples exist and the primary focus of thisstudy was to analyse the published literature to find proteolytic enzymes,specifically endoproteses and to examine the similarity in the substrates thatthey act on so as to predict a suitable structural motif which can be used asthe basis for preparation of useful prodrug carriers against diseases caused byspecific bacteria like Salmonella. Also, the similarities between the bacterialproteases and the action of human matrix metalloproteinases (MMPs), togetherwith the MMP-like activity of bacterial endoproteases to activate human MMPs,were also analysed. This information was used to try to identify substrates onwhich the MMPs and bacterial proteases act, to aid the design of oligopeptideprodrug carriers to treat cancer and its metastatic spread. MMPs are greatlyinvolved in cancer growth and progression, a few MMPs and certain proteasesshare a similar type of activity in degrading the extra cellular matrix (ECM)and substrates including gelatin. Our primary targets of study were to identifythe proteases and MMPs that facilitate the migration of bacteria and growth oftumour cells respectively. The study was thus a two-way approach to study thesubstrate specificity of both bacterial proteases and MMPs, thereby to help incharacterisation of their substrates. Various bioinformatics tools were used inthe characterisation of the proteases and substrates as well as in theidentification of possible binding sites and conserved regions in a range ofcandidate proteins. Central to this project was the salmonella derived PgtEsurface protease that has been shown recently to act upon the pro-forms ofhuman MMP-9.

The Structural Biology and Critical Evaluation of Bacterial Proteases as Targets in New Drug Design