KLVFF peptide functionalized nanoparticles capture Aβ_(42) by co-assembly for decreasing cytotoxicity

The accumulation of extracellular senile plagues of amyloid β-proteins(Aβ) in the patient brain is one of most important facture in Alzheimer’s disease(AD), which is resulted from abnormal self-assembly of Aβpeptide. Nanoparticles show greatly potential for therapeutic studies due to the sophisticated surface which can mimic the functionality of protein. Herein, we design the bis(pyrene)-Lys-Leu-Val-Phe-PheGly-poly ethylene glycol(BP-KLVFFGPEG) based nanoparticles, which capture Aβthrough recognition and co-assembly of KLVFF. The resulting co-assemblies show different morphologies, such as large aggregates, nanoparticles and nanofibers corresponding to the different length chain of PEG, leading to different capture efficiencies. The co-assembly strategy shows a decrease of cytotoxicity, potentially for AD treatment.

The accumulation of extracellular senile plagues of amyloid β-proteins(Aβ) in the patient brain is one of most important facture in Alzheimer's disease(AD), which is resulted from abnormal self-assembly of Aβpeptide. Nanoparticles show greatly potential for therapeutic studies due to the sophisticated surface which can mimic the functionality of protein. Herein, we design the bis(pyrene)-Lys-Leu-Val-Phe-PheGly-poly ethylene glycol(BP-KLVFFGPEG) based nanoparticles, which capture Aβ_(42) through recognition and co-assembly of KLVFF. The resulting co-assemblies show different morphologies, such as large aggregates, nanoparticles and nanofibers corresponding to the different length chain of PEG, leading to different capture efficiencies. The co-assembly strategy shows a decrease of cytotoxicity, potentially for AD treatment.