Bioconjugation techniques are methods that covalently connect a biomolecule to another molecular component while retaining the structural features required for its biological activity ^[1]. Protein and peptide conjugation can target endogenous amino acid side chains or terminal groups, with reaction selectivity governed by functional group reactivity and accessibility ^[1][2]. Cysteine thiols and lysine amino groups provide common attachment sites, although other residues can also participate in selective transformations ^[2]. Reactive groups may instead be introduced before conjugation to distinguish the intended site from competing functionalities ^[1]. Carbonyl groups react with aminooxy or hydrazine derivatives to form oximes or hydrazones, respectively; substrate structure and catalysis affect reaction rates and product stability ^[3]. Azide-based ligations provide another route to joining components through installed chemical handles ^[4]. The resulting conjugate may contain one defined attachment site or a distribution of modified sites. Reaction medium, stoichiometry, and chemical compatibility shape both the efficiency of coupling and the molecular composition of the product ^[1][2][3].