Abstract

Light-harvesting proteins can be used as versatile building blocks for the realization of functional biomaterials. A pathway to the hierarchical arrangement of protein molecules into functional biomaterials is provided by mesoscale (>50 nm) self-assembly. This nanotechnological approach opens new avenue in applications of light-harvesting proteins in materials science and bioelectronics (e.g., biosensors, energy-conversion devices).Phycocyanin (PC), a phycobiliprotein found in the majority of cyanobacteria and red algae’s photosynthetic light-harvesting phycobilisome complex, has the potential to be used in a wide range of nanobiotechnological applications, such as biological photovoltaic devices and as a natural photosensitizer for dye-sensitized solar cells. However, such applications frequently need for certain operating conditions, with thermal stability as one of the most crucial. Here we compare three advanced methods: Cryo-EM, X-ray nanodifraction and XFEL, previously used for probing local temperature-induced self-assembly in thermally annealed PC LB multilayered nanofilms.

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