Effect of chaperones on prion protein PrP23-98 aggregation in vitro

Recent studies have indicated that prp23-98,an n-terminal portion of prp,polymerizes into amyloid-like and proteinase k (pk)-resistant aggregates in the presence of nadph with copper ions [19],and then that crt suppressed aggregation of prp23-98 and also promoted solubilization of the aggregates [18]. as it is interesting to find out whether other chaperones can inhibit aggregation of prp23-98 in vitro similar to crt,this study was conducted to determine whether bip,grp94,pdi grp58 and heat shock cognate protein70 (hsc70) can inhibit aggregation of prp23-98 in vitro. the present results indicated that grp94 suppressed aggregation of prp23-98,but that grp94 could not mediate solubilization occurred in the aggregates in contrast to crt. other chaperons induced aggregation of prp23-98 in the absence of nadph. © 2016 bentham science publishers.