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-1, 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-1. 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.
Original language | English (US) |
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Pages (from-to) | 4174-4178 |
Number of pages | 5 |
Journal | Analytical Methods |
Volume | 13 |
Issue number | 36 |
DOIs | |
State | Published - Sep 28 2021 |
Externally published | Yes |
ASJC Scopus subject areas
- Analytical Chemistry
- Chemical Engineering(all)
- Engineering(all)