3 research outputs found
Evidence of Rapid Coaggregation of Globular Proteins during Amyloid Formation
The
question of how an aggregating protein can influence aggregation
of other proteins located in its vicinity is particularly significant
because many proteins coexist in cells. We demonstrate <i>in
vitro</i> coaggregation and cross-seeding of lysozyme, bovine
serum albumin, insulin, and cytochrome <i>c</i> during their
amyloid formation. The coaggregation process seems to be more dependent
on the temperature-induced intermediate species of these proteins
and less dependent on their sequence identities. Because amyloid-linked
inclusions and plaques are recognized as multicomponent entities originating
from aggregation of the associated protein, these findings may add
new insights into the mechanistic understanding of amyloid-related
pathologies