Effect of the Air-Water Interface on the Conformation of Amyloid Beta

16 September 2020, Version 1
This content is a preprint and has not undergone peer review at the time of posting.


Using MD simulation the conformation of the fibril forming protein amyloid beta at the air-water interface. It is found that adsorption at the air-water interface induces the formation of aggregation prone alpha-helical conformations, consistent with experimental studies of amyloid beta. Adsorption on the air-water interface also reduces the number of distinct conformations that the protein exhibits. This provides insight into the role of protein conformational change into the enhancement of protein fibrillation at interfaces.


Molecular dynamics simulation
amyloid fibril
Air-water interface


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