Abstract
Amyloid fibrils are excellent bioderived nanotemplates for controlling molecular and optical properties of small molecules such as organic dyes. Here we demonstrate that two representative fibril-forming proteins, lysozyme and insulin, from the amyloids family can determine the optical signature of rhodamine 6G. Their structural variety leads to a unique molecular arrangement of dye aggregates on the biotemplate surface. This significantly influences the light amplification threshold as well as the stimulated emission profiles, which show remarkable broadband wavelength tunability. We show in addition that amyloid fibrils can be potentially used in constructing broadband emission biolasers.
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