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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.