Amyloid Composition and Structure-Based Development of Therapeutic and Diagnostic Agents

A special issue of Pharmaceuticals (ISSN 1424-8247). This special issue belongs to the section "Medicinal Chemistry".

Deadline for manuscript submissions: 25 July 2024 | Viewed by 319

Special Issue Editors

E-Mail Website
Guest Editor
Department of Medicine, University of Tennessee Graduate School of Medicine, Knoxville, TN 37920, USA
Interests: amyloidosis; diagnostics; early detection strategies

E-Mail Website
Guest Editor
Department of Medicine, University of Tennessee Graduate School of Medicine, Knoxville, TN 37920, USA
Interests: amyloidosis; immunotherapy; imaging

Special Issue Information

Dear Colleagues,

The treatment and diagnosis of systemic amyloidosis is a constantly developing and important field. Despite remarkable advances in these areas over the last few years, there remain significant unmet clinical needs and improvements in clinical care that can be made, especially in the rarer forms of hereditary amyloidosis.

This Special Issue, entitled “Amyloid Composition and Structure-Based Development of Therapeutic and Diagnostic Agents”, seeks to provide a comprehensive collection of informative articles that describe the interrelationship between an understanding of the structure of amyloid and the development of clinically relevant therapeutics and diagnostics.

We cordially invite you to contribute an article to this volume as either original research, a mini review, or a clinical case study.

Topics of interest include structural studies of amyloid precursor proteins and amyloid fibrils and how this knowledge has or may inform the development of clinically relevant reagents, characterization of the composition of tissue amyloid and how this impacts the development of novel clinical agents, and descriptions of current and novel clinical reagents that rely on structural and compositional characteristics of amyloid for efficacy.

The aim of this Special Issue is to highlight diagnostic and therapeutic reagents that were developed, or may be developed, based on the composition of amyloid and the growing appreciation of the structure of amyloidogenic proteins and amyloid fibrils.

Dr. Emily B. Martin
Prof. Dr. Jonathan S. Wall
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Pharmaceuticals is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Published Papers

This special issue is now open for submission, see below for planned papers.

Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.



Avi Chakrabartty 1,2*

1    Professor Emeritus, Department of Medical Biophysics, University of Toronto, Toronto, Ontario, M5G 2M9, CANADA;

2    Principal, Proteotoxicity Solutions, Toronto, Ontario, L4K 2E1, CANADA

*    Correspondence:

The disease of transthyretin (TTR) amyloidosis (ATTR) has been known since the 1960s, and during these past 60 or so years, we have seen a sustained period of steady discoveries that have established the current model of ATTR pathogenesis. Notably, 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 amyloid fibrils obtained from individual patients. Here, we will examine cryo-EM structures of transthyretin amyloid fibrils to explore the structural basis of recent monoclonal antibody clinical trial results for ATTR, as well as to point out potential applications of this approach to other systemic amyloid diseases.

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