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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

N., Nez-lvarez, C., Joglar, B

Firstly, it is based on the NHANES database, which employs a multistage complex probability sampling design and weighted adjustments, enhancing the representativeness and reliability of the study resultsa crucial factor for improving the generalizability of our findings within the American context

Cysteine is found naturally in whole foods, including chicken, fish, garlic, yogurt, and eggs