{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,30]],"date-time":"2026-01-30T07:54:30Z","timestamp":1769759670371,"version":"3.49.0"},"reference-count":44,"publisher":"Public Library of Science (PLoS)","issue":"7","license":[{"start":{"date-parts":[[2024,7,11]],"date-time":"2024-07-11T00:00:00Z","timestamp":1720656000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"abstract":"<jats:p>For the study of amyloid beta (A\u03b2) associated toxicity which is supposed to be the main pathological agent in Alzheimer\u2019s disease (AD), it is important to secure A\u03b2 peptide with appropriate biological activity. However, commercial and synthetic A\u03b2 often have some pitfalls like less cell toxicity, prompt aggregation and excess price, using recombinant technology, these issues can be resolved though the method also suffered from some problems such as low yield, aggregation and prolong time to purify. Thus, we previously developed an easy, economic and convenient method for A\u03b242 purification using highly expressed GroES-Ubiquitin-A\u03b242 fusion protein. The method was efficient, but further development was performed to improve the procedure and increase the yield. Focus was on the isolation of the fusion protein (GroES-Ubiquitin) from A\u03b242 peptide. After a series of systematic testing with several chemicals, we found that methanol could precipitate efficiently the fusion protein, while the A\u03b2 peptide was recovered in the supernatant. By this method, A\u03b2 peptide was easily purified without tedious chromatographic steps which are main obstacles to purify the peptide in the previous method. This method yielded ~20 mg highly pure A\u03b242 peptide from 1-liter bacterial culture. Different biophysical characterizations and bioactivity assays indicate that the peptide purified using this method was competitive with others which have been previously reported whereas considering the simplicity, final yield and time of purification, this method is the optimal solution.<\/jats:p>","DOI":"10.1371\/journal.pone.0307213","type":"journal-article","created":{"date-parts":[[2024,7,11]],"date-time":"2024-07-11T17:50:28Z","timestamp":1720720228000},"page":"e0307213","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":5,"title":["An expeditious and facile method of amyloid beta (1\u201342) purification"],"prefix":"10.1371","volume":"19","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1680-3006","authenticated-orcid":true,"given":"Md. 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