Skip to main content
Have a personal or library account? Click to login
The Landscape of Amyloid-Targeting Therapeutics in Alzheimer's Disease Part 1: Anti-Amyloid Approaches Cover

The Landscape of Amyloid-Targeting Therapeutics in Alzheimer's Disease Part 1: Anti-Amyloid Approaches

Open Access
|Jun 2026

Figures & Tables

Figure 1.

Unified IgG1 antibody structure and therapeutic targets across the amyloid-β aggregation cascade. Panel A shows the general structure of an IgG1 antibody. The variable regions (antigen-binding domains) determine the unique specificity of these therapeutics for different amyloid-β species, as detailed in the accompanying table. In contrast, the Fc region mediates effector functions, such as microglia-mediated phagocytosis, which is essential for the clearance of established plaques (e.g., by donanemab). Panel B illustrates the progression from soluble monomers to deposited plaques, with specific binding sites for approved and investigational agents.* Binds both fibrils and established plaques (residues 3-7).** pGlu+ specific antibodies.

Figure 2.

Structural formula of valiltramiprosate (ALZ-801). An oral small-molecule prodrug of tramiprosate designed to inhibit the formation of neurotoxic amyloid-beta oligomers. The structure was generated in ChemDraw based on the SMILES string from the PubChem database.
DOI: https://doi.org/10.2478/bgbl-2026-0005 | Journal eISSN: 2956-6851 | Journal ISSN: 0373-174X
Language: English
Page range: 53 - 70
Accepted on: May 4, 2026
Published on: Jun 11, 2026
In partnership with: Paradigm Publishing Services
Publication frequency: 2 issues per year

© 2026 Oliwier Szewczyk, Małgorzata Wojsław, Michał Pstrągowski, published by The Medical Library named after S. Konopka in Warsaw
This work is licensed under the Creative Commons Attribution-NonCommercial 4.0 License.