Small regulatory RNA segments, such as microRNA (miRNA) or silencing RNA (siRNA) binding to proteins could effect the association mechanisms of protein aggregation. Extended protein aggregation, known as fibrillization, has links to degenerative diseases like Alzheimers or prion disease. The formation of fibrils is thought to be a non-specific property of proteins, and can be demonstrated with well-known model globular proteins like serum albumin, lysozyme, beta-lactoglobulin and the like. Much research has been devoted to this field, but with the recent discovery of micro/silencing RNA, small regulatory RNA generally less than 70 base pairs, the question arises on the effect of these nucleic acids on the aggregation process behind fibril formation. Therefore, this study attempted for the first time to probe two effects in the fibrillization process: first, the binding affinity of the selected microRNA MIR106A to the model proteins lysozyme and bovine serum albumin in fibril forming conditions, and second, the long-term effect of the protein-nucleic acid complex on the fibril formation process. Fluorescence spectroscopy, to include time-resolved anisotropy decay of fluorescein or dansyl-labeled complexes, and sizing techniques like atomic force microscopy to track aggregation patterns were incorporated.