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EN
Fibril formation of proteins and peptides is associated with a large group of major human diseases, including Alzheimer’s disease, prion disorders, amy otrophic lateral sclerosis, type 2 diabetes, etc. Therefore, understanding the key factors th at govern this process is of paramount importance. The fibrillogenesis of polypeptide chains depends on their intrinsic properties as well as on the external conditions. In this mini-review w e discuss the relationship between fibril formation kinetics and the sequence, aromaticity, hydr ophobicity, charge and population of the so called fibril-prone conformation in a monomer state. The high er the population, the faster is the fibril elongation and this dependence may b e described by a single exponential function. This observation opens up a new way to unders tand the fibrillogenesis of bio-molecules at the monomer level. We will also discuss the influence of t he environment with focus on the recently observed dual effect of crowders on the aggregation rat es of polypeptide chains.
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