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Version 1
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Current State Of Monoclonal Antibody Therapy for Transthyretin Amyloidosis
Version 1
: Received: 8 August 2024 / Approved: 10 August 2024 / Online: 12 August 2024 (02:57:10 CEST)
How to cite: Chakrabartty, A. Current State Of Monoclonal Antibody Therapy for Transthyretin Amyloidosis. Preprints 2024, 2024080738. https://doi.org/10.20944/preprints202408.0738.v1 Chakrabartty, A. Current State Of Monoclonal Antibody Therapy for Transthyretin Amyloidosis. Preprints 2024, 2024080738. https://doi.org/10.20944/preprints202408.0738.v1
Abstract
The disease of transthyretin (TTR) amyloidosis (ATTR) has been known since the 1960s, and during these past 60 or so years, there has been a sustained peri-od of steady discoveries that have led to the current model of ATTR pathogene-sis. More recent research has achieved major advances in both diagnostics and therapeutics for ATTR, which are having a significant impact on ATTR patients today. Aiding these recent achievements has been the remarkable ability of cryo-electron microscopy (EM) to determine high-resolution structures of amy-loid fibrils obtained from individual patients. Here, we will examine cryo-EM structures of transthyretin amyloid fibrils to explore the structural basis of re-cent monoclonal antibody therapies for ATTR, including ALXN-2220 and Co-ramitug; as well as to point out potential applications of this approach to other systemic amyloid diseases.
Keywords
transthyretin; amyloidosis; antibody therapy; protein structure; cryo-electron microscopy
Subject
Medicine and Pharmacology, Cardiac and Cardiovascular Systems
Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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