ArticleChemical science2017
Artificial disulfide-rich peptide scaffolds with precisely defined disulfide patterns and a minimized number of isomers.
Article in Chemical science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- Rational Design and Delivery of Engineered Peptides: Toward a Unified Framework for Structure, Screening, and Application.Biology · 2026Review
- Construction and Functional Evaluation of Cyclic Peptide-Based CAR T Cells in Tumor Models.Bio-protocol · 2026Article
- Resolving conformational polymorphism in disulfide-rich peptide drugs.Frontiers in chemistry · 2026Article
- Directing the oxidative folding of disulfide-rich peptides for enhanced engineering and applications.Chemical science · 2025Review
- A Cysteine-Directed Proximity-Driven Crosslinking Method for Native Peptide Bicyclization.Angewandte Chemie (International ed. in English) · 2023Article
- Structure-guided design of CPPC-paired disulfide-rich peptide libraries for ligand and drug discovery.Chemical science · 2022Article
- De novo design and directed folding of disulfide-bridged peptide heterodimers.Nature communications · 2022Article
- Structural Transition-Induced Raman Enhancement in Bioinspired Diphenylalanine Peptide Nanotubes.ACS applied materials & interfaces · 2022Article
- Approaches for peptide and protein cyclisation.Organic & biomolecular chemistry · 2021Review
- A Chemical Biology Approach to Probing the Folding Pathways of the Inhibitory Cystine Knot (ICK) Peptide ProTx-II.Frontiers in chemistry · 2020Article
- Structure and Oxidative Folding of AAI, the Major Alfa-Amylase Inhibitor From Amaranth Seeds.Frontiers in chemistry · 2020Review
- Heterogeneous-Backbone Foldamer Mimics of a Computationally Designed, Disulfide-Rich Miniprotein.Chembiochem : a European journal of chemical biology · 2019Article
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Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Disulfide-rich peptides are emerging as potential templates for drug design applications. However, the synthesis and reengineering of disulfide-rich peptides are challenging, owing to the complexity of the oxidative folding process involving a number of diverse isomeric structures. Novel disulfide-rich peptide scaffolds that are not besieged by their disulfide isomers are still greatly desired. In this work, we report the design and synthesis of a novel class of artificial disulfide-rich peptide scaffolds with precisely defined disulfide patterns and a minimized number of isomers. In theory, natural peptides with three disulfide bonds have 15 possible isomers. By rationally engineering the thiol-framework of a peptide containing six cysteines with penicillamines and a dithiol amino acid, we demonstrated, for the first time, that the total number of isomers formed after oxidative folding can be decreased to a minimum of two (
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.