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However, almost no deposition of A\u03b2 in the peripheral tissues could be found. Human serum albumin (HSA), the most abundant protein in the blood, has been reported to inhibit amyloid formation through binding A\u03b2, which is believed to play an important role in the peripheral clearance of A\u03b2. We identified the A\u03b2 binding site on HSA and developed HSA mutants with high binding capacities for A\u03b2 using a phage display method. HSA fragment 187\u2013385 (Domain II) was found to exhibit the highest binding capacity for A\u03b2 compared with the other two HSA fragments. To elucidate the sequence that forms the binding site for A\u03b2 on Domain II, a random screening of Domain II display phage biopanning was constructed. A number of mutants with higher A\u03b2 binding capacities than the wild type were identified. These mutants exhibited stronger scavenging abilities than the wild type, as revealed via in vitro equilibrium dialysis of A\u03b2 experiments. These findings provide useful basic data for developing a safer alternative therapy than A\u03b2 vaccines and for application in plasma exchange as well as extracorporeal dialysis.<\/jats:p>","DOI":"10.1002\/iub.2203","type":"journal-article","created":{"date-parts":[[2019,12,3]],"date-time":"2019-12-03T14:05:25Z","timestamp":1575381925000},"page":"641-651","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Albumin domain mutants with enhanced A\u03b2 binding capacity identified by phage display analysis for application in various peripheral A\u03b2 elimination approaches of Alzheimer's disease treatment"],"prefix":"10.1002","volume":"72","author":[{"given":"Yu","family":"Ishima","sequence":"first","affiliation":[{"name":"Department of Pharmacokinetics and Biopharmaceutics Institute of Biomedical Sciences, Tokushima University  Tokushima Japan"},{"name":"School of Pharmacy Monash University Malaysia, Jalan Lagoon 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