Master and Slave Relationship Between Two Types of Self-Propagating Insulin Amyloid Fibrils
PBN-AR
Instytucja
Instytut Wysokich Ciśnień Polskiej Akademii Nauk
Źródłowe zdarzenia ewaluacyjne
Informacje podstawowe
Główny język publikacji
EN
Czasopismo
Journal of Physical Chemistry B
ISSN
1520-6106
EISSN
1520-5207
Wydawca
American Chemical Society
Rok publikacji
2014
Numer zeszytu
47
Strony od-do
13582-13589
Numer tomu
118
Identyfikator DOI
Liczba arkuszy
0,8
Streszczenia
Język
angielski
Treść
Cross-seeding of fibrils of bovine insulin (BI) and LysB31-ArgB32 human insulin analog (KR) induces self-propagating amyloid variants with infrared features inherited from mother seeds. Here we report that when native insulin (BI or KR) is simultaneously seeded with mixture of equal amounts of both templates (i.e., of separately grown fibrils of BI and KR), the phenotype of resulting daughter fibrils is as in the case of the purely homologous seeding: heterologous cotemplates accelerate the fibrillation but do not determine infrared traits of the daughter amyloid. This implies that fibrillation-promoting and structure-imprinting properties of heterologous seeds become uncoupled in the presence of homologous seeds. We argue that explanation of such behavior requires that insulin molecules partly transformed through interactions with heterologous fibrils are subsequently recruited by homologous seeds. The selection bias toward homologous daughter amyloid is exceptional: more than 200-fold excess of heterologous seed is required to imprint its structural phenotype upon mixed seeding. Our study captures a snapshot of elusive docking interactions in statu nascendi of elongation of amyloid fibril and suggests that different types of seeds may collaborate in sequential processing of soluble protein into fibrils.
Inne
System-identifier
PX-56b474538106eb71826ed418
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