Reversion of protein or peptide aggregation is important in various domain of research at the interface of chemistry, nanoscience, and medicine. a novel class of dipeptides, termed as ?-breaker dipeptides (bbdp), has been identified. the bbdp can be incorporated into the self-recognizing sequences to generate a novel class of conformational switch, which forms ?-sheet at an initial stage and then converts in a controlled manner to random coil at specific condition. such conformational switches may be used to study aggregation/disaggregation process and may find many biomedical applications relevant to aggregation related disorders. incorporation of bbdps in a well designed amyloidogenic peptides generates a special class of ?-sheet breaker peptides those undergo a chemical change at physiological condition generating a breaker element in situ. these ?-breaker peptides are shown to first incorporate into the amyloid and then disrupt it. this may be important for drug design against various amyloidoses. the reversion of peptide aggregation using chemical tricks may find application in material chemistry as well.