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Cryo-EM of cardiac AL-224L amyloid reveals shared features in l6 light chain fibril folds

ABSTRACT: Structural characterization of an amyloid fibril from a patient afected by cardiac light chain amyloidosis.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Heart

DISEASE(S): Immunoglobulin Light Chain Amyloidosis

SUBMITTER: Francesca Lavatelli

LAB HEAD: Francesca Lavatelli

PROVIDER: PXD064296 | Pride | 2026-01-23

REPOSITORIES: Pride

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			Action	DRS
	250207X_SAM14049_09-109_Water_Fraction3_Spot15.raw	Raw
	250207X_SAM14050__09-109_Water_Fraction3_Spot16.raw	Raw
	250207X_SAM14050__09-109_Water_Fraction3_Spot16_fin.msf	Msf
	250207X_SAM14072_09-109_Water_Fraction_3_total_protein_digest.raw	Raw
	checksum.txt	Txt

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Publications

Cryo-EM of Cardiac AL-224L Amyloid Reveals Shared Structural Motifs and Mutation-induced Differences in λ6 Light Chain Fibrils.

Hicks Chad W CW Prokaeva Tatiana T Spencer Brian B Jayaraman Shobini S Huda Noorul N Wong Sherry S Chen Hui H Sanchorawala Vaishali V Lavatelli Francesca F Gursky Olga O

Journal of molecular biology 20251211 3

In light chain amyloidosis (AL), aberrant monoclonal antibody light chains (LCs) deposit in vital organs causing organ damage. Each AL patient features a unique LC; previous cryogenic electron microscopy (cryo-EM) studies revealed different amyloid structures in different AL patients. How LC mutations influence amyloid structures remains unclear. We report a cryo-EM structure of cardiac AL-224L amyloid (2.92 Å resolution) from λ6-LC family, which is overrepresented in AL amyloidosis. Comparison ...[more]

PMID: 41389958

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