It is of high importance to measure and map the surface charge distribution of amyloids, since electrostatic interaction between amyloidogenic proteins and biomolecules plays a vital role in amyloidogenesis. In this work, we have measured and mapped the surface charge distributions of amyloids (i.e., β-lactoglobulin fibril) using Kelvin probe force microscopy. It is shown that the surface charge distribution is highly dependent on the conformation of amyloids (e.g., the helical pitch of amyloid fibrils) as well as the pH of a solvent.
Bibliographical noteFunding Information:
This work was supported by the National Research Foundation (NRF) of Korea under Grant Nos. NRF-2010-0009428 and NRF-2012-008616.
ASJC Scopus subject areas
- Physics and Astronomy (miscellaneous)