科研之友
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摘要
The endogenous deposition of protein fibrillar aggregates in the tissues is the cause of several neurodisorders. In the present study the native beta-lactoglobulin (beta-lg) has been driven towards amyloid fibrillar aggregates when it was exposed to heat at 75 degrees C for 1 h at pH 7.5. The citrate stabilized gold nanoparticle (AuNPs) of 20 nm diameter is shown to inhibit the thermal aggregation of beta-lg. The stability of the beta-lg against heat stress was assessed by studying its aggregation at 75 degrees C, either in presence or in absence of AuNPs. AuNPs stabilizes the monomeric and dimeric forms of the beta-lg inhibiting the nucleation and elongation for the formation of higher aggregates. Incubation of beta-lg with AuNPs at 75 degrees C results in the formation of smaller ragged aggregates. Results show that AuNPs possess the capability of inhibiting the formation of amyloid fibrillar aggregates of beta-lg in a concentration-dependent manner and may thus facilitate the refolding into native like structure. AuNPs thus serve as nano-chaperon to inhibit the protein aggregation. Thus chaperon like activity of AuNP may be exploited in the design of rational therapeutics for the neurodegenerative diseases.
- 出版日期2014-8
