Protein aggregation is a biological phenomenon caused by the accumulation of misfolded proteins which correlates with diseases like Alzheimer's disease (AD). Amyloid beta (Aβ) peptides are derived from the cleavage of larger membrane protein molecule and accumulates to form plaques extracellularly around nerve endings. According to the amyloid hypothesis, accumulation of misfolded Aβ in the brain is primarily responsible for AD. Therefore, the disassembly of Aβ aggregates may provide opportunities for alleviating or treating AD. We show that the novel protein targeting machinery from chloroplast signal recognition particle (cpSRP43) is an effective ATP-independent membrane protein chaperone that can prevent and reverse Aβ aggregation. Thioflavin T dye determines the kinetics of Aβ aggregation and shows that the chaperone prevents Aβ aggregation in a concentration-dependent manner. Electron microscopy reveals the fibril structure is disrupted in the presence of chaperone. Fluorescence anisotropy and light scattering show that the disaggregation effect of cpSRP43 on Aβ aggregation correlates with urea denaturation. Importantly, cpSRP43 utilizes the binding energy to active remodeling the preformed Aβ aggregates without assistance by a co-chaperone and ATP, emphasizing its unique function among protein chaperones. Our results demonstrate that the presence of cpSRP43 will inhibit or disrupt Aβ peptide aggregation, potentially opening new avenues to develop an effective treatment for AD.