Cryo-EM reveals that cardiac IGLV6-derived AL fibrils can be polymorphic DOI Open Access
Parker Bassett, Binh A. Nguyen, Virender Singh

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: Dec. 5, 2024

ABSTRACT AL amyloidosis is a systemic disease caused by the aggregation of free antibody light chains (LC) secreted aberrant plasma cell clones into bloodstream. These LC aggregates form amyloid fibrils that deposit in multiple organs, leading to organ failure and, ultimately, death. Investigating structural basis critical avenue for understanding biopathology amyloidosis. Structural insights fibril formation may reveal mechanisms driving deposition and inspire novel therapeutic strategies. Previous studies using cryo-electron microscopy have uncovered diverse structures extracted from patients, highlighting variability architecture. Here, we present cryo-EM structure cardiac patient with This reveals unique fold coexistence morphologies, including single- double-protofilament forms. Notably, some these exhibit an uncommon rotational symmetry, raising intriguing questions about governing evolution over time.

Language: Английский

Does the structure of transthyretin amyloid fibrils vary depending on the organ of accumulation? DOI
Mineyuki Mizuguchi

Structure, Journal Year: 2024, Volume and Issue: 32(12), P. 2181 - 2182

Published: Dec. 1, 2024

Language: Английский

Citations

0
Cryo-EM reveals that cardiac IGLV6-derived AL fibrils can be polymorphic DOI Open Access
Parker Bassett, Binh A. Nguyen, Virender Singh

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: Dec. 5, 2024

ABSTRACT AL amyloidosis is a systemic disease caused by the aggregation of free antibody light chains (LC) secreted aberrant plasma cell clones into bloodstream. These LC aggregates form amyloid fibrils that deposit in multiple organs, leading to organ failure and, ultimately, death. Investigating structural basis critical avenue for understanding biopathology amyloidosis. Structural insights fibril formation may reveal mechanisms driving deposition and inspire novel therapeutic strategies. Previous studies using cryo-electron microscopy have uncovered diverse structures extracted from patients, highlighting variability architecture. Here, we present cryo-EM structure cardiac patient with This reveals unique fold coexistence morphologies, including single- double-protofilament forms. Notably, some these exhibit an uncommon rotational symmetry, raising intriguing questions about governing evolution over time.

Language: Английский

Citations

0