Amyloidoses are a group of complex diseases marked by the abnormal deposition of amyloid proteins in extracellular spaces, leading to progressive organ dysfunction. This review delves into the pathogenesis, classification, diagnosis, and treatment of amyloidoses, emphasizing the critical role of protein misfolding and aggregation in disease progression. The transformation of soluble proteins into insoluble fibrils through fibrillogenesis, involving abnormal folding into β-pleated sheets, induces the development of amyloidosis. These processes are influenced by genetic mutations, aging, and the proteolytic conversion of normal proteins, challenging the body's protein quality control mechanisms. The classification of amyloidosis is determined by the specific amyloid protein implicated, with more than 36 amyloidogenic proteins recognized, leading to deposits that are either localized or systemic. The diagnosis involves a combination of clinical evaluation, lab tests, biopsies, and sophisticated imaging methods to precisely determine the nature and scope of amyloid accumulation. Treatment strategies focus on reducing amyloid protein production, promoting amyloid removal, and supporting organ function, incorporating chemotherapy, targeted therapies, stem cell transplantation, and innovative approaches like gene editing. The review highlights the ongoing challenges in amyloidosis management, including late diagnosis and the need for improved therapeutic strategies. It underscores the importance of early detection and intervention in enhancing patient outcomes, advocating for increased research into diagnostic and treatment innovations.