Circular RNA Protein Aβ175 Characterized In Silico in Alzheimer’s Study

Researchers at the University of Kalyani in India have carried out a computational characterization of Aβ175, a protein produced from a circular RNA molecule linked to the amyloid beta region of the APP gene, in a study exploring its possible role in Alzheimer’s disease. The work, published as an original research article in Frontiers in Bioinformatics, is entirely in silico, meaning the structural predictions and analyses were performed with computational tools rather than laboratory experiments on biological samples.

Circular RNAs, or circRNAs, are single-stranded molecules with covalently closed termini that were once dismissed as mere transcriptional artefacts. They have since been implicated as significant players in tumorigenesis, neurodegeneration and other diseases. Although generally classified as non-coding, certain circular RNAs have demonstrated the ability to encode proteins, a finding that has reshaped understanding of their biological roles.

The circRNA at the center of this study, circAβ-a, contains the amyloid beta (Aβ)-coding region of the APP gene and acts as an alternative source of Aβ peptides. According to the authors, its discovery suggests that Aβ peptides can be generated through a non-canonical translation mechanism independent of APP processing, the conventional route by which these peptides are produced. Aβ peptides are considered key contributors to Alzheimer’s disease pathogenesis.

CircAβ-a is reported to be efficiently translated into Aβ175, a larger protein that is subsequently processed into Aβ peptides. Because inhibiting circAβ-a translation or modifying its expression might help reduce Aβ accumulation in the brain, the researchers argue that understanding the structural characteristics, functional properties and interaction patterns of Aβ175 is crucial for developing effective inhibitors targeting these peptides.

To that end, the study focused on predicting the structural features of the Aβ175 protein. The authors frame the work as an exploration of the protein’s potential as an alternative biomarker for Alzheimer’s disease, an idea they note would need to be verified through wet-lab experiments before any such application could be established.

The article lists keywords including Alzheimer’s disease, Aβ175, circRNA, MD simulation, neurodegeneration and pathway analysis, indicating that molecular dynamics simulation and pathway analysis formed part of the computational toolkit used to characterize the protein. Molecular dynamics simulations allow researchers to model how a predicted protein structure behaves over time, while pathway analysis can situate a molecule within known biological networks.

It is important to note the scope and limitations of the research. As a purely computational study, it reports predictions rather than experimentally measured structures or clinical findings. The authors themselves state that the biomarker potential of Aβ175 can be verified only through future wet-lab experiments, and no therapeutic efficacy has been demonstrated. The claims expressed in the article are solely those of the authors and do not necessarily represent those of their affiliated organizations, the publisher, the editors or the reviewers, as the journal’s disclaimer makes clear.

The research article was received on 26 August 2026 and accepted on 28 September 2026, and is published open access under the Creative Commons Attribution License. The work was carried out at the University of Kalyani’s Bioinformatics Infrastructure Facility Centre in Kalyani, India, by a team including Srsreekanya Roy, Sima Biswas, Dipanjan Guha, Aniruddha Biswas, Rakhi Dasgupta and corresponding author Angshuman Bagchi.

For the Alzheimer’s research field, the study adds to a growing body of work on circular RNAs as more than genetic leftovers. If future experimental studies confirm the predicted structural features of Aβ175 and its processing into Aβ peptides, the protein could offer a new target for strategies aimed at reducing amyloid accumulation. For now, the findings remain computational predictions awaiting laboratory validation.

Subject of Research: In silico structural characterization of the circular RNA-derived protein Aβ175 and its proposed role in Alzheimer's disease

Article Title: In silico characterization of the protein Aβ175 from circular RNA CircAβ-a and its involvement in the pathogenesis of Alzheimer’s disease (AD)

Article References: Roy, S., Biswas, S., Guha, D., Biswas, A., Dasgupta, R., & Bagchi, A. (2026). In silico characterization of the protein Aβ175 from circular RNA CircAβ-a and its involvement in the pathogenesis of Alzheimer’s disease (AD). Frontiers in Bioinformatics, 6, Article 1979627. https://doi.org/10.3389/fbinf.2026.1979627

Image Credits: AI Generated

DOI: 10.3389/fbinf.2026.1979627

Keywords: Alzheimer's disease, circular RNA, circAβ-a, Aβ175, amyloid beta, APP gene, in silico, molecular dynamics simulation, neurodegeneration, biomarker, computational biology, Frontiers in Bioinformatics