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U.S.A."],"published-print":{"date-parts":[[2020,6,2]]},"abstract":"<jats:title>Significance<\/jats:title>\n                  <jats:p>Deposition of some aggregated and misfolded polypeptides (amyloids) is the hallmark of many degenerative diseases. Amyloid assembly is slow, unfavorable, and still poorly understood. Here, we show that liquid\u2013liquid demixing (like oil forming droplets in water) of type II diabetes IAPP amyloid precursors is not dependent on the human amyloidogenic sequence and leads to the formation of a water-filled gel within phase-separated droplets. Both processes then trigger pathological aggregation at the droplet surface, which is modulated by insulin. This localized aggregation propagates to interconnect droplets, leading to a macroscopic meshwork formation with increased local viscosity, eventually percolating the whole system. 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