{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,17]],"date-time":"2025-10-17T00:25:53Z","timestamp":1760660753513,"version":"build-2065373602"},"reference-count":28,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2005,2,10]],"date-time":"2005-02-10T00:00:00Z","timestamp":1107993600000},"content-version":"vor","delay-in-days":9,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J. Mass Spectrom."],"published-print":{"date-parts":[[2005,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The aggregation of full\u2010length (residues 1\u201340) amyloid \u03b2\u2010peptide (A\u03b2) and fragments corresponding to residues 1\u201323 and 24\u201340 was studied by electrospray mass spectrometry, using gramicidin as a non\u2010aggregating reference. Following a lag period, A\u03b2(1\u201340) at 140 \u00b5<jats:sc>M<\/jats:sc> concentration aggregates with apparent first\u2010order kinetics. Under acidic conditions A\u03b2(1\u201340) undergoes spontaneous cleavage between Asp23\u2013Val24 and to a lesser extent also at two other Asp\u2013X motifs. Incubation in acidic H<jats:sub>2<\/jats:sub><jats:sup>18<\/jats:sup>O showed incorporation of <jats:sup>18<\/jats:sup>O in fragment A\u03b2(1\u201323), confirming that the Asp23\u2013Val24 peptide bond had been hydrolyzed. Incubation of synthetic A\u03b2(1\u201323) and A\u03b2(24\u201340) peptides with A\u03b2(1\u201340) showed that A\u03b2(24\u201340) remained in solution for several months, that A\u03b2(1\u201323) partly disappeared from solution, whereas A\u03b2(1\u201340) completely disappeared. Further, treatment of sedimentable aggregates formed after co\u2010incubation of the three peptides with hexafluoro\u20102\u2010propanol or formic acid recovered the intensity of A\u03b2(1\u201340). These data support previous studies showing that the region of A\u03b2 encompassing residues 16\u201324 is necessary for aggregation into amyloid fibrils. Copyright \u00a9 2005 John Wiley &amp; Sons, Ltd.<\/jats:p>","DOI":"10.1002\/jms.732","type":"journal-article","created":{"date-parts":[[2005,2,10]],"date-time":"2005-02-10T12:17:39Z","timestamp":1108037859000},"page":"142-145","source":"Crossref","is-referenced-by-count":10,"title":["Hydrolysis of the amyloid \u03b2\u2010peptide (A\u03b2) 1\u201340 between Asp23\u2013Val24 produces non\u2010aggregating fragments. 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