{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T21:40:22Z","timestamp":1791668422124,"version":"4.3.4"},"reference-count":366,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2018,1,30]],"date-time":"2018-01-30T00:00:00Z","timestamp":1517270400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004329","name":"ARRS","doi-asserted-by":"publisher","award":["P3-0171"],"award-info":[{"award-number":["P3-0171"]}],"id":[{"id":"10.13039\/501100004329","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Intracellular synthesis, folding, trafficking and degradation of proteins are controlled and integrated by proteostasis. The frequency of protein misfolding disorders in the human population, e.g., in Alzheimer\u2019s disease (AD), is increasing due to the aging population. AD treatment options are limited to symptomatic interventions that at best slow-down disease progression. The key biochemical change in AD is the excessive accumulation of per-se non-toxic and soluble amyloid peptides (A\u03b2(1-37\/44), in the intracellular and extracellular space, that alters proteostasis and triggers A\u03b2 modification (e.g., by reactive oxygen species (ROS)) into toxic intermediate, misfolded soluble A\u03b2 peptides, A\u03b2 dimers and A\u03b2 oligomers. The toxic intermediate A\u03b2 products aggregate into progressively less toxic and less soluble protofibrils, fibrils and senile plaques. This review focuses on peptides that inhibit toxic A\u03b2 oligomerization, A\u03b2 aggregation into fibrils, or stabilize A\u03b2 peptides in non-toxic oligomers, and discusses their potential for AD treatment.<\/jats:p>","DOI":"10.3390\/molecules23020283","type":"journal-article","created":{"date-parts":[[2018,1,30]],"date-time":"2018-01-30T08:03:34Z","timestamp":1517299414000},"page":"283","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":65,"title":["Peptides as Potential Therapeutics for Alzheimer\u2019s Disease"],"prefix":"10.3390","volume":"23","author":[{"given":"Samo","family":"Ribari\u010d","sequence":"first","affiliation":[{"name":"Institute of Pathophysiology, Faculty of Medicine, Zalo\u0161ka 4, SI-1000 Ljubljana, Slovenia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2018,1,30]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1056\/NEJMra0909142","article-title":"Alzheimer\u2019s disease","volume":"362","author":"Querfurth","year":"2010","journal-title":"N. 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