Nanoscale Microscopy and Spectroscopy

Food-derived protein amyloid fibrils (PAF) has been employed as advanced materials in biomedical, environmental and biomaterial applications in the recent years. Both intrinsic and extrinsic conditions affect self-assembly of PAF, thereby modulating the multi-scale structures, morphology, and techno-functional properties. Compared with animal proteins, plant proteins are ideal alternatives with large environmental abundance, availability, and sustainability. However, current knowledge on the fibrillation of plant proteins, temporal-spatial polymorphisms which are usually correlated with cytotoxicity and mechanical properties, remain elusive. The diverse composition, low purity and heterogenous subunits of plant proteins also make the study complex. Within the research framework of the Nanoscale Microscopy and Spectroscopy group, we aim to use cutting-edged Atomic Force Microscopy (AFM)-based techniques, including AFM with chemical identification power of IR Spectroscopy (AFM-IR), Peak Force Quantitative Nanomechanical Mapping (PF-QNM), bulk spectroscopic methods and polymer statistics, to (1) compare the differences of fibrilization process and multi-scale structures between typical animal and plant proteins, and (2) gain insights into the structural, chemical, and nanomechanical complexities of plant proteins during aggregation. These findings will give significant implications for the fields of material science and food science.