ReviewACS pharmacology & translational science2022
Amyloid Fibrillation of Insulin: Amelioration Strategies and Implications for Translation.
Review in ACS pharmacology & translational science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 37 citations in OpenAlex.
- Mass Spectrometric Characterization of Native Insulin Hexamers and Non-Native Heptamers: Formation and Stability Across Insulin Analogs.Journal of mass spectrometry : JMS · 2026Article
- Damping amyloid-associated conformational fluctuations in a protein by an engineered diselenide bridge.Protein science : a publication of the Protein Society · 2026Article
- FAIM Inhibits Insulin Amyloidogenesis through a Noncanonical Aggregation Pathway.bioRxiv : the preprint server for biology · 2026Article
- To contact or not: an investigation into the polymeric surface interactions with human insulin and their therapeutic implications.RSC advances · 2026Article
- Gangliosides GM3 And GD3 Modulate Insulin Aggregation Pathways and Reduce Cytotoxicity Through Structural Remodeling.bioRxiv : the preprint server for biology · 2026Article
- Encapsulated Control: Shaping Insulin Fibrillation through Polymer Confinement.Biomacromolecules · 2026Article
- Nanoparticle-Based Oral Insulin Delivery: Challenges, Advances, and Future Directions.Pharmaceutics · 2025Review
- AmyloGram reveals amyloidogenic potential in stroke thrombus proteomes.The Biochemical journal · 2025Article
- A microscopic investigation on insulin uptake in human hepatocellular carcinoma-derived HepG2 cells.RSC advances · 2025Article
- Article
- Saponins Effect on Human Insulin Amyloid Aggregation.Biomolecules · 2024Article
- Site-Specific Glyco-Tagging of Native Proteins for the Development of Biologicals.Journal of the American Chemical Society · 2024Article
- Proteomic Evidence for Amyloidogenic Cross-Seeding in Fibrinaloid Microclots.International journal of molecular sciences · 2024Article
- Amyloidoma: A Case Report of Remote Insulin-Derived Amyloidosis in the Setting of Insulin-Dependent Diabetes.Cureus · 2024Article
- Fibrinaloid Microclots and Atrial Fibrillation.Biomedicines · 2024Review
- Semisynthesis of A6-A11 lactam insulin.Journal of peptide science : an official publication of the European Peptide Society · 2024Article
- An Investigation into the Acidity-Induced Insulin Agglomeration: Implications for Drug Delivery and Translation.ACS omega · 2023Article
- Peptide Inhibitors of Insulin Fibrillation: Current and Future Challenges.International journal of molecular sciences · 2023Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Insulin is a therapeutically relevant molecule with use in treating diabetes patients. Unfortunately, it undergoes a range of untoward and often unpredictable physical transformations due to alterations in its biochemical environment, including pH, ionic strength, temperature, agitation, and exposure to hydrophobic surfaces. The transformations are prevalent in its physiologically active monomeric form, while the zinc cation-coordinated hexamer, although physiologically inactive, is stable and less susceptible to fibrillation. The resultant molecular reconfiguration, including unfolding, misfolding, and hydrophobic interactions, often results in agglomeration, amyloid fibrillogenesis, and precipitation. As a result, a part of the dose is lost, causing a compromised therapeutic efficacy. Besides, the amyloid fibrils form insoluble deposits, trigger immunologic reactions, and harbor cytotoxic potential. The physical transformations also hold back a successful translation of non-parenteral insulin formulations, in addition to challenges related to encapsulation, chemical modification, purification, storage, and dosing. This review revisits the mechanisms and challenges that drive such physical transformations in insulin, with an emphasis on the observed amyloid fibrillation, and presents a critique of the current amelioration strategies before prioritizing some future research objectives.
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.