Slowdown of 1-40 beta-peptide aggregation by addition of two synthetic biocompatible polymers

Fibril deposit formation of ainyloid P-protreiri (AP) iii the braiii is a liallmark oi Alzlieiiiicr disease (AD). Fibril: forination is triggered by 1nolecu1a.rc o~lformationacl hangeii and protein-protein interactions iiivolvirig partially unfo1de:i regioris of different AP peptide moleciiles. lncreasing cvi(.erice suggests that toxicity is linlced to diffusible AP oligoiners, which liave bccri foiind in soluble brain extracts of AI) patients, ratl-ier thail to the insoluble fibres. New thcrapcl tical approach, based 011 searchiiig molecules capable of regulating the peptide aggregation, is currently developiilg.