Mechanisms of protein-guided mineralization in enamel, leading to organized fibrillar apatite nanocrystals, remain elusive. In vitro studies reveal recombinant human amelogenin (rH174), a matrix protein templating this process, self-assembles into a variety of structures. This study endeavors to clarify the self-assembly of rH174 in physiologically relevant conditions. Self-assembly in simulated enamel fluid was monitored up to 2 months. At alkali (7.3-8.7) and acidic (5.5-6.1) pH ranges, a distinct progression in formation was observed from nanospheres (17-23 nm) to intermediate-length nanorods, concluding with the formation of long 17-18 nm wide nanoribbons decorated with nanospheres. Assembly in acidic condition progressed quicker to nanoribbons with fewer persistent nanospheres. X-ray diffraction exhibited reflections characteristic of antiparallel β-sheets (4.7 and 9.65 Å), supporting the model of amyloid-like nanoribbon formation. This is the first observation of rH174 nanoribbons at alkaline pH as well as concurrent nanosphere formation, indicating both supramolecular structures are stable together under physiological conditions.