Introduction: Autoimmune diseases result from an immune response directed against self-antigens; however, the precise underlying mechanisms remain incompletely understood. Molecular mimicry represents one proposed mechanism whereby infectious agents possess antigens that resemble host proteins, leading to immune cross-reactivity.Objectives: The primary objective of our study was to employ bioinformatics techniques in order to investigate the existence of molecular mimicry between SARS-CoV-2 and the human proteome.Methods: In pursuit of our objective, we generated sequences comprising eight consecutive amino acids from structural proteins of SARS-CoV-2, including spike, nucleocapsid, membrane, and envelope proteins. Subsequently, we assessed the extent of mimicry between these sequences and the human proteome, while also evaluating their antigenicity, allergenicity, toxicity, TAP affinity, as well as their potential to induce IFNγ and IL-10.Results: Furthermore, we calculated the affinity of the amino acid sequence DEDDSEPV, which demonstrated molecular mimicry, towards HLA receptors and determined it to possess favorable binding energy. Through our in silico analysis, we identified that the DEDDSEPV amino acid sequence may provoke autoimmunity due to its similarity to the myosin-16 protein.Conclusion: The outcomes of our investigation provide substantiation for the potential of SARS-CoV-2 to trigger autoimmunity through molecular mimicry. These findings bear significant implications for comprehending the pathophysiology of autoimmune diseases and have the potential to contribute to the development of novel therapeutic strategies.