AI Article Synopsis
- Monitoring amyloid-prone proteins, like insulin, helps us understand how amyloid fibrils form.
- When insulin is dissolved in a low pH buffer, its surface tension is measured at 61-64 mN/m, which increases to 71.2-73.5 mN/m upon the formation of amyloid fibrils.
- The study confirms that using surface tension measurements, alongside ThT fluorescence and AFM for kinetics and morphology, is an effective method for detecting insulin amyloid aggregation.
Article Abstract
Monitoring the aggregation of amyloid-prone proteins is critical for understanding the mechanism of amyloid fibril formation. Insulin, when dissolved in low pH buffer, has a surface tension of 61-64 mN m, as measured by the pendant drop technique. Formation of insulin amyloid fibrils resulted in the increase of the surface tension values up to 71.2-73.5 mN m. The kinetics of fibril formation and fibril morphology were validated by ThT fluorescence and AFM, respectively. The results demonstrate that monitoring the surface tension by the pendant drop technique is a valuable tool for the detection of insulin amyloid aggregation.
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| http://dx.doi.org/10.1039/d1ay01126j | DOI Listing |
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