Amyloids are a broad class of proteins and peptides that can misfold and assemble into long unbranched fibrils with a cross-β conformation. The aggregation of proteins is associated with the onset of a variety of human neurodegenerative diseases, such as Alzheimer’s disease, Parkinson’s disease, and Huntington disease. Our understanding of amyloids aggregation has been greatly fostered using fluorescent molecular probes, such as Thioflavin T, which shows an increase in fluorescence emission upon binding to fibrillar aggregates. However, the major drawback of standard bioimaging exploiting Thioflavin T dye is lacking in sensitivity to oligomeric forms of amyloids aggregates. The lasing spectroscopy of the liquid solutions containing stained proteins sandwiched in Fabry–Pérot microcavity overcomes this limitation, assuring traceability of prefibrillar form and agglomeration process. Unfortunately, the utilisation of Fabry–Pérot microcavities is associated with a lack of repeatability, difficulty in operation, and is only effective for cerebrospinal fluid, which is transparent in visible light region. Thus, I proposed the sensing platform in a form of solid-state porous nanomaterial functioning as both nanoscale confinement hosts and potential photonic amplifiers. The filtering properties of nanoporous anodic alumina is viable for immobilisation of specific proteins due to structural engineering of nanopores and available surface functionalisation. During the lecture, I would like to show the photo-physics of Thioflavin T dye, the structural engineering of nanoporous anodic alumina, the integration of stained nanoporous anodic alumina with lasing spectroscopy,