Rapid Mapping of Disulfide Bonds in Complex Cyclic Peptides Via a Sequence-tailored Enzymatic Digestion and LC-HRMS Workflow

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July 17,2026

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Disulfide bonds play a pivotal role in stabilizing the conformation and ensuring the therapeutic efficacy of complex cyclic peptides. Conventional characterization strategies—including partial reduction/alkylation, chemical derivatization, exhaustive synthesis, and surface plasmon resonance (SPR) verification—are highly tedious, low-throughput, and resource-intensive. To overcome these bottlenecks, this study established a comprehensive workflow integrating a sequence-dependent enzymatic digestion strategy with liquid chromatography-high resolution mass spectrometry (LC-HRMS) and innovative software to rapidly map disulfide bonds.

Rapid Mapping of Disulfide Bonds in Complex Cyclic Peptides Via a Sequence-tailored Enzymatic Digestion and LC-HRMS Workflow.jpg

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