The protection of primary amines available in proteins holds great potential to introduce a plethora of diverse functionalities along the protein backbone (e.g., via its carboxylic acid or alcohol moieties) while circumventing the crosslinking issue using conventional approaches. This paper reports on a straightforward and efficient proof-of-concept including the chemoselective N-tert-butyloxycarbonylation of the primary amines in the protein gelatin (gel-NH-BOC), followed by introducing crosslinkable methacrylamide moieties. The reaction is performed successfully under relatively mild conditions (50 degrees C). Following selective protein functionalization, the deprotection is realized by adding a catalytic amount of an aqueous hydrogen chloride solution. The present communication illustrates the occurrence of a straightforward and selective deprotection procedure, which is typically required to circumvent the occurrence of acidic hydrolysis of the protein backbone. The results hold promise for a large range of biomedical applications in which the presence of primary amines is essential for preserving the biological activity.