ArticleChembiochem : a European journal of chemical biology2019
Heterogeneous-Backbone Foldamer Mimics of a Computationally Designed, Disulfide-Rich Miniprotein.
Article in Chembiochem : a European journal of chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Advancing protein engineering via organic chemistry.Communications chemistry · 2026Review
- Directing the oxidative folding of disulfide-rich peptides for enhanced engineering and applications.Chemical science · 2025Review
- Interplay between CChembiochem : a European journal of chemical biology · 2025Article
- Backbone Modification in a Protein Hydrophobic Core.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Article
- Protein Backbone Alteration in Non-Hairpin β-Turns: Impacts on Tertiary Folded Structure and Folded Stability.Chembiochem : a European journal of chemical biology · 2023Article
- Chemical Shifts of Artificial Monomers Used to Construct Heterogeneous-Backbone Protein Mimetics in Random Coil and Folded States.Peptide science (Hoboken, N.J.) · 2023Article
- Heterogeneous-Backbone Proteomimetic Analogues of Lasiocepsin, a Disulfide-Rich Antimicrobial Peptide with a Compact Tertiary Fold.ACS chemical biology · 2022Article
- Analysis of folded structure and folding thermodynamics in heterogeneous-backbone proteomimetics.Methods in enzymology · 2021Review
- Proteomimetic Zinc Finger Domains with Modified Metal-binding β-Turns.Peptide science (Hoboken, N.J.) · 2020Article
- A twist in the road less traveled: The AMBER ff15ipq-m force field for protein mimetics.The Journal of chemical physics · 2020Article
- Proteomimetics as protein-inspired scaffolds with defined tertiary folding patterns.Nature chemistry · 2020Review
- Exploring the Functional Consequences of Protein Backbone Alteration in Ubiquitin through Native Chemical Ligation.Chembiochem : a European journal of chemical biology · 2019Article
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Authors and funding
3 authors.
Funding
Abstract
Disulfide-rich peptides have found widespread use in the development of bioactive agents; however, low proteolytic stability and the difficulty of exerting synthetic control over chain topology present barriers to their application in some systems. Herein, we report a method that enables the creation of artificial backbone ("foldamer") mimics of compact, disulfide-rich tertiary folds. Systematic replacement of a subset of natural α-residues with various artificial building blocks in the context of a computationally designed prototype sequence leads to "heterogeneous-backbone" variants that undergo clean oxidative folding, adopt tertiary structures indistinguishable from that of the prototype, and enjoy proteolytic protection beyond that inherent to the topologically constrained scaffold. Collectively, these results demonstrate systematic backbone substitution to be a viable method to engineer the properties of disulfide-rich sequences and expands the repertoire of protein mimicry by foldamers to an exciting new structural class.
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