While amyloid fibrils are usually associated with pathological aggregates of proteins and peptides in amyloid diseases, accumulating discoveries start to uncover functional roles of amyloids beyond pathology, known as functional amyloids. For example, amyloid fibrils formed by PMEL17 are a major functional component of the melanosomal compartment as they optimize melanin polymerization, condensation and storage. Beta-endorphin, an endogenous opioid peptide, forms amyloid fibrils in the low pH environment of secretory vesicles for efficient storage. Bacteria secret peptides (e.g., Curli CsgA in E. Coli, FapC in pseudomonas, and PSM in staphylococcus) to form amyloid fibrils important for biofilm formation. Vicilin amyloid accumulation increases during seed maturation and wanes at germination. In addition, amyloid fibrils have been discovered as building blocks for bionanotechnology and used to develop hybrid composite nanomaterials for novel applications. Recently, our lab starts to investigate structures and assembly dynamics of functional amyloids and explore their applications and implications.<\/p>\n
10. H. Xu, X. Zhang, Z. Lv, F. Huang, Y. Zou, C. Wang, F. Ding*, and Y. Sun*, \u201cComputational exploration of the self-aggregation mechanisms of phenol-soluble modulins \u03b21 and \u03b22 in Staphylococcus aureus biofilms\u201d, Colloids Surf B Biointerfaces, 248: 114498 (2025) doi: 10.1016\/j.colsurfb.2025.114498<\/p>\n
9. Y. Wang, X. Liang, N. Andrikopoulos, H. Tang, F. He, X. Yin, Y. Li, F. Ding, G. Peng, M. Mortimer, P.C. Ke, \u201cRemediation of Metal Oxide Nanotoxicity with a Functional Amyloid\u201d, Advanced Science, 11(23):2310314 (2024) doi:10.1002\/advs.202310314<\/p>\n
8. Y. Liu, Y. Wang, C. Tong, G. Wei, F. Ding*, Y. Sun*, \u201cMolecular Insights into the Self-assembly of Block Copolymer Suckerin Polypeptides into Nanoconfined \u03b2-sheets\u201d, Small, in press, doi: 10.1002\/smll.202202642 (2022)<\/p>\n
7. Y. Liu, Y. Zhang, Y. Sun and F. Ding, \u201cA Buried Glutamate in the Cross-\u03b2 Core Renders \u03b2-endorphin Fibrils Reversible\u201d, Nanoscale, in press (2021) doi:10.1039\/D1NR05679D<\/a><\/p>\n 6. I Javed,Z Zhang, J Adamcik, N Andrikopoulos, Y Li, DE Otzen, S Lin, R Mezzenga, TP Davis, F Ding* and P Ke*, \u201cAccelerated Amyloid Beta Pathogenesis by Bacterial Amyloid FapC\u201d, Advanced Science, 7, 2001299 (2020) doi: doi.org\/10.1002\/advs.202001299<\/a> 5. Y. Xing, Y. Sun, B. Wang, & F. Ding, \u201cMorphological Determinants of Carbon Nanomaterial-Induced Amyloid Peptide Self-Assembly\u201d, Frontiers in Chemistry, 8: 160 (2020) DOI: 10.3389\/fchem.2020.00160 PMCID:PMC7076083<\/p>\n 4. I Javed,Z Zhang, J Adamcik, N Andrikopoulos, Y Li, DE Otzen, S Lin, R Mezzenga, TP Davis, F Ding* and P Ke*, \u201cAccelerated Amyloid Beta Pathogenesis by Bacterial Amyloid FapC\u201d, Adv Sci, 7, 2001299 (2020) doi: doi.org\/10.1002\/advs.202001299 3. Y. Sun, F. Ding, \u201cThermo- and pH-Responsive Fibrillization of Squid Suckerin A1H1 Peptide\u201d, Nanoscale, 12, 6307 \u2013 6317 (2020) DOI: 10.1039\/C9NR09271D<\/p>\n 2. Z Huma,I Javed, Z Zhang, H Bilal, Y Sun, SZ Hussain, TP Davis, DE Otzen, CB Landersdorfer, F Ding, I Hussain and PC Ke, \u201cNano Silver Mitigates Biofilm Formation via FapC Amyloidosis Inhibition\u201d, Small, 1906674-1906683 (2019) DOI: 10.1002\/smll.201906674<\/p>\n 1. I. Javed, Y. Sun, J. Adamcik, B. Wang, A. Kakinen, E. Pilkington, F. Ding, R. Mezzenga, T. Davis, Thomas; P. Ke, \u201cCo-fibrillization of pathogenic and functional amyloid proteins with gold nanoparticles against amyloidogenesis\u201d, Biomacromolecules, 18, 4316\u20134322 (2017) DOI: 10.1021\/acs.biomac.7b01359<\/p>\n","protected":false},"excerpt":{"rendered":" While amyloid fibrils are usually associated with pathological aggregates of proteins and peptides in amyloid diseases, accumulating discoveries start to uncover functional roles of amyloids beyond pathology, known as functional amyloids. For example, amyloid fibrils formed by PMEL17 are a major functional component of the melanosomal compartment as they optimize melanin polymerization, condensation and storage. … <\/p>\n
\n\u2013 Featured as the Cover<\/a>.<\/p>\n
\n\u2013 Featured as the Cover.<\/p>\n