biostudies-literatureUnknown103(11)Ivanova MIIdentifying sequence determinants of fibril-forming proteins is crucial for understanding the processes causing >20 proteins to form pathological amyloid depositions. Our approach to identifying which sequences form amyloid-like fibrils is to screen the amyloid-forming proteins human insulin and beta(2)-microglobulin for segments that form fibrils. Our screen is of 60 sequentially overlapping peptides, 59 being six residues in length and 1 being five residues, covering every noncysteine-containing segment in these two proteins. Each peptide was characterized as amyloid-like or nonfibril-forming. Amyloid-like peptides formed fibrils visible in electron micrographs or needle-like microcrystals showing a cross-beta diffraction pattern. Eight of the 60 peptides (three from insulin and five froProceedings of the National Academy of Sciences of the United States of America4079-82https://www.ebi.ac.uk/biostudies/studies/S-EPMC1449649biostudies-literatureA systematic screen of beta(2)-microglobulin and insulin for amyloid-like segments.PMC1449649Eisenberg DThompson MJIvanova MIfalseA systematic screen of beta(2)-microglobulin and insulin for amyloid-like segments.Identifying sequence determinants of fibril-forming proteins is crucial for understanding the processes causing >20 proteins to form pathological amyloid depositions. Our approach to identifying which sequences form amyloid-like fibrils is to screen the amyloid-forming proteins human insulin and beta(2)-microglobulin for segments that form fibrils. Our screen is of 60 sequentially overlapping peptides, 59 being six residues in length and 1 being five residues, covering every noncysteine-containing segment in these two proteins. Each peptide was characterized as amyloid-like or nonfibril-forming. Amyloid-like peptides formed fibrils visible in electron micrographs or needle-like microcrystals showing a cross-beta diffraction pattern. Eight of the 60 peptides (three from insulin and five fro2006-01-01T00:00:00Z2006 Mar2026-05-02T17:25:06.614Z2019-03-27T01:26:19ZS-EPMC14496491653748810.1073/pnas.0511298103