ArticleBiophysical journal2019
The Hydration Shell of Monomeric and Dimeric Insulin Studied by Terahertz Time-Domain Spectroscopy.
Article in Biophysical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 17 citations in OpenAlex.
- Dual Mechanistic Role of Polyphenols in Modulating the Insulin-Related Metabolic Pathways: Insights from Computer-Aided Analysis.Cell biochemistry and biophysics · 2026Article
- Vibrational contribution to the sub-terahertz dielectric response of kinesin and its hydration shell.Scientific reports · 2026Article
- A new horizon for neuroscience: terahertz biotechnology in brain research.Neural regeneration research · 2025Article
- Saponins Effect on Human Insulin Amyloid Aggregation.Biomolecules · 2024Article
- Water determines the intramolecular dynamics of proteins. En example of bovine serum albumin.Frontiers in chemistry · 2024Article
- Terahertz spectroscopy as a method for investigation of hydration shells of biomolecules.Biophysical reviews · 2023Review
- Bioconjugation of a Near-Infrared DNA-Stabilized Silver Nanocluster to Peptides and Human Insulin by Copper-Free Click Chemistry.Journal of the American Chemical Society · 2023Article
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Authors and funding
6 authors at 4 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Protein aggregation is believed to be a significant biological mechanism related to neurodegenerative disease, which makes the early-stage detection of aggregates a major concern. We demonstrated the use of terahertz (THz) time-domain spectroscopy to study protein-water interaction of monomeric and dimeric bovine insulin in aqueous samples. Regulated by changing pH and verified by size-exclusion chromatography and dynamic light scattering, we then measured their concentration-dependent changes in THz absorption between 0.5 and 3.0 THz and quantitatively deduced the extended hydration shell thickness by cubic distribution model and random distribution model. Under a random distribution assumption, the extended hydration thickness is 15.4 ± 0.4 Å for monomeric insulin and 17.5 ± 0.5 Å for dimeric insulin, with the hydration number of 6700 and 11,000, respectively. The hydration number of dimeric insulin is not twice but 1.64 times that of monomeric insulin, further supported by the ratio of solvent-accessible surface area. This "1.64-times" relation probably originates from the structural and conformational changes accompanied with dimerization. Combined with the investigations on insulin samples with different single amino acid mutations, residue B24 is believed to play an important role in the dimerization process. It is demonstrated that THz time-domain spectroscopy is a useful tool and has the sensitivity to provide the hydration information of different protein aggregates at an early stage.
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