The aim of this study was to assess the modifications of fish myosin induced by interactions with four aldehydes: hexanal, 2-hexenal, 2,4-hexadienal, and 2,6-nonadienal. These compounds are generated during lipid oxidation and are known to have an impact on the functional properties of proteins. The interactions between protein and aldehydes were highlighted by measuring the content of aldehydes in the gaseous phase by the SPME-GC technique. Results show that the partition of aldehydes between the proteinaceous system and the gas phase decreases with time, except for hexanal. This decrease is proportional to the number of carbons and double bonds. The reaction between myosin and unsaturated aldehydes induces a decrease in the free sulfhydryl and amino groups of the protein and the formation of dityrosine. The solubility of myosin is significantly affected by the presence of unsaturated aldehydes. All the modifications increase with increasing numbers of carbons and double bonds in the aldehydes.