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So far, key amyloid properties of stability against ionic detergents and self\u2010seeding, are unclear for HSA aggregates. Precautions against amyloid contamination would be required if HSA aggregates were self\u2010seeding. Here, we show that HSA aggregates display detergent sarkosyl stability and have self\u2010seeding potential. HSA dimer is preferable for clinical applications due to its longer retention in circulation and lesser oedema owing to its larger molecular size. Here, HSA was homodimerized <jats:italic>via<\/jats:italic> free cysteine\u201034, without any potentially immunogenic cross\u2010linkers that are usually pre\u2010requisite for homodimerization. Alike the monomer, HSA dimers also aggregated as amyloid, necessitating precautions while using for therapeutics.<\/jats:p>","DOI":"10.1016\/j.febslet.2015.11.004","type":"journal-article","created":{"date-parts":[[2015,11,8]],"date-time":"2015-11-08T01:02:20Z","timestamp":1446944540000},"page":"4033-4038","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":24,"title":["New insights into in vitro amyloidogenic properties of human serum albumin suggest considerations for therapeutic 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