CORRELATION BETWEEN STABILITY AND PROPENSITY TO FORM AMYLOID-LIKE FIBRILS

摘要

In several cases of single point mutations inverse correlation between stability and propensity to form amyloid-like fibrils has been demonstrated (1). Previously, chimeric mutants of human stefins A and B have been studied. Results on their stability and folding rates (Kenig et al., submitted) have shown that there is no correlation between stability and the propensity to fibrillise. The apparent contradiction may be understood if we compare proteins of the same structural class : all stefin B-like and all stefin A-like. Deciding for the propensity to form amyloid-fibrils seems structural factors : the beta-sheet structure of both homologues, with stefin's B p-sheet being more hydrophobic and strand-prone already in the denatured state (Zerovnik et al., to be submitted).