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Literature DB >> 33575525

Bent Into Shape: Folded Peptides to Mimic Protein Structure and Modulate Protein Function.

Haley I Merritt¹, Nicholas Sawyer¹, Paramjit S Arora¹.

Abstract

Protein secondary and tertiary structure mimics have served as model systems to probe biophysical parameters that guide protein folding and as attractive reagents to modulate protein interactions. Here we review contemporary methods to reproduce loop, helix, sheet and coiled-coil conformations in short peptides.

Entities: CellLine Chemical Disease Gene Species

Year: 2020 PMID： 33575525 PMCID： PMC7875438 DOI： 10.1002/pep2.24145

Source DB: PubMed Journal: Pept Sci (Hoboken) ISSN： 2475-8817

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Cited

6 in total

1. Improved RAD51 binders through motif shuffling based on the modularity of BRC repeats.

Authors: Laurens H Lindenburg; Teodors Pantelejevs; Fabrice Gielen; Pedro Zuazua-Villar; Maren Butz; Eric Rees; Clemens F Kaminski; Jessica A Downs; Marko Hyvönen; Florian Hollfelder
Journal: Proc Natl Acad Sci U S A Date: 2021-11-16 Impact factor: 12.779

6. Uncoupling the Folding-Function Paradigm of Lytic Peptides to Deliver Impermeable Inhibitors of Intracellular Protein-Protein Interactions.

Authors: Stephen E Miller; Kohei Tsuji; Rachel P M Abrams; Terrence R Burke; Joel P Schneider
Journal: J Am Chem Soc Date: 2020-11-11 Impact factor: 15.419

6 in total

Bent Into Shape: Folded Peptides to Mimic Protein Structure and Modulate Protein Function.

1. Improved RAD51 binders through motif shuffling based on the modularity of BRC repeats.

2. Identification of Secondary Binding Sites on Protein Surfaces for Rational Elaboration of Synthetic Protein Mimics.

3. Identification of β-strand mediated protein-protein interaction inhibitors using ligand-directed fragment ligation.

4. Covalent and Noncovalent Targeting of the Tcf4/β-Catenin Strand Interface with β-Hairpin Mimics.

5. Second-generation non-hematopoietic erythropoietin-derived peptide for neuroprotection.

6. Uncoupling the Folding-Function Paradigm of Lytic Peptides to Deliver Impermeable Inhibitors of Intracellular Protein-Protein Interactions.