Advanced microscopy techniques have decoded how hydrophobin RolA, a fungal surface protein, transforms from individual molecules into protective fiber structures called rodlets through a surface-catalyzed assembly process. The research employed high-speed atomic force microscopy to capture real-time molecular dynamics previously invisible to scientists. This mechanistic insight into amyloid fiber formation represents a significant advance in understanding how organisms engineer protective biological materials at the molecular level. The findings bridge structural biology and materials science, potentially informing development of bio-inspired protective coatings and self-assembling materials. While amyloids are often associated with neurodegenerative diseases, this work highlights their beneficial roles in nature as functional biomaterials. The surface-catalyzed mechanism suggests that environmental interfaces play crucial roles in directing protein assembly, which could influence how we approach designing therapeutic interventions for pathological amyloid formation. For biotechnology applications, understanding this natural assembly process may enable engineering of novel materials with tailored protective properties, from antimicrobial surfaces to water-resistant coatings.