In 2017 the Raskatov lab introduced the oligomer-to-fibril conversion paradigm, “Chiral Inactivation”, as a strategy to block neurotoxic actions of Aβ using mirror image peptides. The ensuing mechanistic research led the lab to the “rippled” beta sheet: a structural class predicted by Linus Pauling and Robert Corey of CalTech in 1953 and largely forgotten since. From 2022 onwards, (69 years later!), the Raskatov lab put the rippled sheet on a firm experimental foundation. We were meanwhile able to obtain ~25 crystal structures, with over half of the canonical amino acid alphabet confirmed ripple-genic, i.e., capable of forming a rippled sheet. In addition to what one may now consider standard, canonical rippled sheets, our most recent developments include next generation designs, such as, rippled sheet macrocycles. Such macrocycles may hold promise for supramolecular targeting approaches that use rippled sheet interfaces to bind intrinsically disordered peptides.