Recruitment of human light chain proteins by synthetic fibrils is dependent on disease state and may be used to predict amyloidogenic propensity

Emily B. MartinDepartment of Medicine and Correspondence[email protected]

Angela WilliamsDepartment of Medicine and

Craig WooliverDepartment of Medicine and

R. Eric HeidelDepartment of Surgery, University of Tennessee Medical Center, Knoxville, TN, USA,

Sarah AdamsDepartment of Surgery, University of Tennessee Medical Center, Knoxville, TN, USA,

John DunlapMicroscopy and Imaging Center, University of Tennessee, Knoxville, TN, USA,

Marina Ramirez-AlvaradoDepartments of Biochemistry and Molecular Biology, and Immunology, Mayo Clinic, Rochester, NY, USA, and

Luis Blancas-MejiaDepartments of Biochemistry and Molecular Biology, and Immunology, Mayo Clinic, Rochester, NY, USA, and

Stephen J. KennelDepartment of Medicine and ;Department of Radiology, University of Tennessee Medical Center, Knoxville, TN, USA

Jonathan S. WallDepartment of Medicine and ;Department of Radiology, University of Tennessee Medical Center, Knoxville, TN, USA

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"Recruitment of human light chain proteins by synthetic fibrils is dependent on disease state and may be used to predict amyloidogenic propensity." Amyloid, 24(sup1), pp. 24–25

Declaration of interest

EBM and JSW are named on a patent application that describes the use of a recruitment assay to discriminate LC proteins with amyloidogenic potential.

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Recruitment of human light chain proteins by synthetic fibrils is dependent on disease state and may be used to predict amyloidogenic propensity

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Recruitment of human light chain proteins by synthetic fibrils is dependent on disease state and may be used to predict amyloidogenic propensity

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