the effect of hoffmeister salts on the chaperoning action of β-casein in preventing aggregation of reduced β-lactalbumin

protein aggregation and precipitation is associated with many debilitating diseases including alzheimer's, parkinson's, and light-chain amyloidosis. β-casein, a member of the casein family, has been demonstrated to exhibit chaperone-like activity to protect protein form aggregation. hofmeister salts (lyotropice series) are a class of ions which have an effect on the solubility and also the stability of proteins. in this study, using a range of hofmeister salts (na2so4, nacl and kscn) altered the rate of aggregation and precipitation of α-lactalbumin. the rate of aggregation of α-lactalbumin increased in the presence of all the added salts. however, na2so4 had the greatest effect on the rate of aggregation of α-lactalbumin. β-casein effectively prevented the aggregation of α-lactalbumin but not as well as in the presence of the salt. interestingly, in the presence of na2so4, β-casein was the poorer chaperone toward aggregation of α-lactalbumin compare to in the presence of nacl and kscn. our result showed that all salts had structural effects on the β-casein which affects its chaperone ability. in summary, structural change and kinetic factors maybe be determinant the poorer chaperone ability of β-casein in the presence of salts.