A new trick for an old dog! Aberrant cathepsin B activity is associated with tumor progression, however, despite extensive research, there are no cathepsinB inhibitors in clinical use. Here, nitroxoline, an established antimicrobial agent, is identified as a potent, reversible inhibitor of cathepsin B, and is thus a potential drug candidate for the treatment of cancer and other diseases in which cathepsin B activity plays a role.
COBISS.SI-ID: 3024241
It is well established that contact order and folding rates are correlated for small proteins. The folding rates of stefins A and B differ by nearly two orders of magnitude despite sharing an identical native fold and hence contact order. We break down the determinants of this behavior and demonstrate that the modulation of contact order effects can be accounted for by the combined contributions of a framework-like mechanism, characterized by intrinsic helix stabilities, together with nonnative helical backbone conformation and nonnative hydrophobic interactions within the folding transition state. These contributions result in the formation of nonnative interactions in the transition state as evidenced by the opposing effects on folding rate and stability of these proteins.
COBISS.SI-ID: 24679719
A single-chain V5B2 antibody fragment (scFv) that specifically recognizes the pathogenic form of the prion protein was humanized by variable domain resurfacing approach guided by computer modelling. For the recombinant humanized scFv , unaltered binding affinity to the original antigen was demonstrated by ELISA and maintained binding specificity was proved by Western blotting and immunohistochemistry. Since monoclonal antibodies against prion protein can antagonize prion propagation, the humanized scFv might become a potential therapeutic reagent.
COBISS.SI-ID: 34754053