Glycation accelerates fibrillization of the amyloidogenic W7FW14F apomyoglobin.

ABSTRACT: Neurodegenerative diseases are associated with misfolding and deposition of specific proteins, either intra or extracellularly in the nervous system. Advanced glycation end products (AGEs) originate from different molecular species that become glycated after exposure to sugars. Several proteins implicated in neurodegenerative diseases have been found to be glycated in vivo and the extent of glycation is related to the pathologies of the patients. Although it is now accepted that there is a direct correlation between AGEs formation and the development of neurodegenerative diseases, several questions still remain unanswered: whether glycation is the triggering event or just an additional factor acting on the aggregation pathway. To this concern, in the present study we have investigated the

SUBMITTER: Iannuzzi C 

PROVIDER: S-EPMC3851467 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature