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As the therapeutic landscape for peptides continues to evolve, improving the chemical and metabolic stability of disulfide-containing peptides has emerged as a critical priority in peptide drug development ( 2 The function and limitations of native disulfides in bioactive peptides A defining feature of many bioactive peptides is the formation of disulfide bond, a covalent linkage formed between the thiol groups of two cysteine residues (Cys) (Figure 1a) ( FIGURE 1 Disulfide bonds play a central role in stabilizing the three-dimensional structures by constraining conformational flexibility, thereby preserving bioactive peptide conformations essential for molecular recognition, receptor binding, and enzymatic regulation ( Despite their structural and functional advantages, disulfide-containing peptides face notable limitations that restrict their broader therapeutic applications ( in vivo circulation, can generate heterogeneous mixtures of isomers with variable or undesired biological activity

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