02022nas a2200277   4500008004100000022001400041245013000055210006900185260007300254300001400327490000800341520102500349653001701374653001601391653002001407653001301427653001701440100001801457700002701475700002101502700002001523700002301543700002801566700002201594856012801616       2015                        eng d  a0014-579300aNew insights into in vitro amyloidogenic properties of human serum albumin suggest considerations for therapeutic precautions0 aNew insights into in vitro amyloidogenic properties of human ser  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcDEC  a4033-40380 v5893 a<p>Amyloid aggregates display striking features of detergent stability and self-seeding. Human serum albumin (HSA), a preferred drug-carrier molecule, can also aggregate in vitro. So far, key amyloid properties of stability against ionic detergents and self-seeding, are unclear for HSA aggregates. Precautions against amyloid contamination would be required if HSA aggregates were self-seeding. Here, we show that HSA aggregates display detergent sarkosyl stability and have self-seeding 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 via free cysteine-34, without any potentially immunogenic cross-linkers that are usually pre-requisite for homodimerization. Alike the monomer, HSA dimers also aggregated as amyloid, necessitating precautions while using for therapeutics. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</p>10aDrug carrier10aHSA amyloid10aPlasma expander10aSarkosyl10aSelf-seeding1 aSharma, Neetu1 aSivalingam, Vishwanath1 aMaurya, Sonalika1 aPrasad, Archana1 aKhandelwal, Puneet1 aYadav, Subhash, Chandra1 aPatel, Basant, K.  uhttps://library.ncl.res.in/content/new-insights-vitro-amyloidogenic-properties-human-serum-albumin-suggest-considerations-0