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Amyloids are stable, β-sheet-rich protein/peptides aggregates with 2–15 nm diameter and few micrometers long. It is originally associated with many human diseases such as Alzheimer's, Parkinson's and prion diseases. Amyloids are resistant to enzyme degradation, temperature changes and wide ranges of pH. Although, amyloids are hard and their stiffness is comparable to steel, a constant recycling of monomer occur inside the amyloid fibrils. It grows in a nucleation dependent polymerization manner by recruiting native soluble protein and by converting them to amyloid. These extraordinary physical properties make amyloids attractive for nanotechnological applications. Some amyloid fibrils have also evolved to perform native biological functions (functional amyloid) of the host organism. Functional amyloids are present in mammals such as amyloids of pMel17 and pituitary hormones, where they help in skin pigmentation and hormone storage, respectively. Here, the progress of utilizing amyloid fibrils for nanobiotechnological applications with particular emphasis on the recent studies that amyloid could be utilized for the formulation of peptide/protein drugs depot and how secretory cells uses amyloid for hormone storage will be reviewed.