Alzheimer’s disease (AD) is a neurodegenerative disorder generally carrying a poor prognosis with no established treatments for halting or reversing symptoms. While many of AD’s biophysical mechanisms have yet to be elucidated, recent evidence suggests a correlation of AD symptomology to the presence of amyloid beta (AB) plaques. Normally a membrane protein, pathologically AB is formed from cleavage of the Amyloid Precursor Protein (APP) into isoforms of varying sizes, the most common being 40 and 42 amino acid sequences (AB40 and AB42, respectively). Both isoforms collect in the extracellular matrix surrounding nerve cells, where they exert toxicity on nerve cells, and are therefore detrimental to neurological function.<br/>Therapeutic efforts into slowing or reversing the progression of this neurodegenerative disease have been focused on either clearing the insoluble protein aggregates or inhibiting the aggregation of amyloid peptides. However, there has been no discovery of an inhibitor or drug that can effectively cure AD. A novel protein targeting machinery from chloroplast, cpSRP43 (chloroplast signal recognition particle), is an effective molecular chaperone that can both prevent and reverse protein aggregation effectively. CpSRP43 is a highly specific ATP-independent membrane protein chaperone that can inhibit protein aggregation through binding interactions to mediate its anti-aggregation activity. Thioflavin T (ThT) fluorescence dye is widely used to detect Aβ peptide aggregation. When ThT dye binds to protein aggregates, the dye displays enhanced fluorescence intensity allowing to monitor the rate of aggregation in real time. Through the use of ThT dye, we are able to obtain time-dependent fluorescence data to determine the activity of the chaperone in preventing protein aggregation. Our results suggest that cpSRP43 will suppress Aβ40 peptides from aggregation, and open new avenues to strategically develop an effective treatment for AD.

Applying membrane protein chaperone as therapeutics to prevent Alzheimer’s disease

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.