Fragment Correlation Mass Spectrometry Enables Direct Characterization of Disulfide Bond Cleavage Pathways of Therapeutic Peptides-Reference-Cited by-同舟云学术

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Fragment Correlation Mass Spectrometry Enables Direct Characterization of Disulfide Bond Cleavage Pathways of Therapeutic Peptides

Published:2024-09-09 Issue: Volume: Page:
ISSN:0003-2700
Container-title:Analytical Chemistry
language:en
Short-container-title:Anal. Chem.

Author:

Li Yangjie¹^ORCID,Cavet Guy²,Zare Richard N.¹^ORCID,Driver Taran³^ORCID

Affiliation:

1. Department of Chemistry, Stanford University, Stanford, California 94305, United States

2. Flatiron Bio, LLC, Palo Alto, California 94301, United States

3. Stanford PULSE Institute, SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States

Funder

Air Force Office of Scientific Research

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.analchem.4c03202

Reference20 articles.

1. Cysteine oxidation and disulfide formation in the ribosomal exit tunnel

2. Orphan PTMs: Rare, yet functionally important modifications of cysteine

3. Dithiol amino acids can structurally shape and enhance the ligand-binding properties of polypeptides

4. Macrocyclic Peptides as Drug Candidates: Recent Progress and Remaining Challenges

5. Silica particles convert thiol-containing molecules to disulfides

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