ArticleCommunications biology2023
Enhanced hexamerization of insulin via assembly pathway rerouting revealed by single particle studies.
Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 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
- Monomeric Insulin Analog and Stabilizing Excipient Enabled Ultrafast Insulin Formulation.Advanced materials (Deerfield Beach, Fla.) · 2026Article
- Diverse intracellular trafficking of insulin analogs by machine learning-based colocalization and diffusion analysis.iScience · 2026Article
- Chromatin boundary permeability is controlled by CTCF conformational ensembles.bioRxiv : the preprint server for biology · 2026Article
- Modulation of insulin aggregation by betaine and proline directly observed via real-time super-resolution microscopy.Protein science : a publication of the Protein Society · 2025Article
- Deep learning-assisted analysis of single-particle tracking for automated correlation between diffusion and function.Nature methods · 2025Article
- SEMORE: SEgmentation and MORphological fingErprinting by machine learning automates super-resolution data analysis.Nature communications · 2024Article
- Enhanced hexamerization of insulin via assembly pathway rerouting revealed by single particle studies.Communications biology · 2023Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Insulin formulations with diverse oligomerization states are the hallmark of interventions for the treatment of diabetes. Here using single-molecule recordings we firstly reveal that insulin oligomerization can operate via monomeric additions and secondly quantify the existence, abundance and kinetic characterization of diverse insulin assembly and disassembly pathways involving addition of monomeric, dimeric or tetrameric insulin species. We propose and experimentally validate a model where the insulin self-assembly pathway is rerouted, favoring monomeric or oligomeric assembly, by solution concentration, additives and formulations. Combining our practically complete kinetic characterization with rate simulations, we calculate the abundance of each oligomeric species from nM to mM offering mechanistic insights and the relative abundance of all oligomeric forms at concentrations relevant both for secreted and administrated insulin. These reveal a high abundance of all oligomers and a significant fraction of hexamer resulting in practically halved bioavailable monomer concentration. In addition to providing fundamental new insights, the results and toolbox presented here can be universally applied, contributing to the development of optimal insulin formulations and the deciphering of oligomerization mechanisms for additional proteins.
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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.