<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Sharma, Neetu</style></author><author><style face="normal" font="default" size="100%">Sivalingam, Vishwanath</style></author><author><style face="normal" font="default" size="100%">Maurya, Sonalika</style></author><author><style face="normal" font="default" size="100%">Prasad, Archana</style></author><author><style face="normal" font="default" size="100%">Khandelwal, Puneet</style></author><author><style face="normal" font="default" size="100%">Yadav, Subhash Chandra</style></author><author><style face="normal" font="default" size="100%">Patel, Basant K.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">New insights into in vitro amyloidogenic properties of human serum albumin suggest considerations for therapeutic precautions</style></title><secondary-title><style face="normal" font="default" size="100%">Febs Letters</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Drug carrier</style></keyword><keyword><style  face="normal" font="default" size="100%">HSA amyloid</style></keyword><keyword><style  face="normal" font="default" size="100%">Plasma expander</style></keyword><keyword><style  face="normal" font="default" size="100%">Sarkosyl</style></keyword><keyword><style  face="normal" font="default" size="100%">Self-seeding</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2015</style></year><pub-dates><date><style  face="normal" font="default" size="100%">DEC</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">24, B</style></number><publisher><style face="normal" font="default" size="100%">ELSEVIER SCIENCE BV</style></publisher><pub-location><style face="normal" font="default" size="100%">PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS</style></pub-location><volume><style face="normal" font="default" size="100%">589</style></volume><pages><style face="normal" font="default" size="100%">4033-4038</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">24</style></issue><custom3><style face="normal" font="default" size="100%">&lt;p&gt;Foreign&lt;/p&gt;</style></custom3><custom4><style face="normal" font="default" size="100%">3.519</style></custom4></record></records></xml>