ArticleProceedings of the National Academy of Sciences of the United States of America2010
Stabilizing capping motif for beta-hairpins and sheets.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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Who cites it
38 citing papers in PubMed.
- Article
- Structure-Based Experimental Datasets for Benchmarking Protein Simulation Force Fields [Article v1.0].Living journal of computational molecular science · 2025Article
- Article
- Capping motifs in antimicrobial peptides and their relevance for improved biological activities.Frontiers in chemistry · 2024Review
- Tunable CH/π Interactions within a Tryptophan Zipper Motif to Stabilize the Fold of Long β-Hairpin Peptides.ACS chemical biology · 2023Article
- Terminal repeats impact collagen triple-helix stability through hydrogen bonding.Chemical science · 2022Article
- An N-capping asparagine-lysine-proline (NKP) motif contributes to a hybrid flexible/stable multifunctional peptide scaffold.Chemical science · 2022Article
- A Conformationally Stable Acyclic β-Hairpin Scaffold Tolerating the Incorporation of Poorly β-Sheet-Prone Amino Acids.Chembiochem : a European journal of chemical biology · 2022Article
- Current Approaches in Supersecondary Structures Investigation.International journal of molecular sciences · 2021Review
- Folding in Place: Design of β-Strap Motifs to Stabilize the Folding of Hairpins with Long Loops.The Journal of organic chemistry · 2021Article
- Tau local structure shields an amyloid-forming motif and controls aggregation propensity.Nature communications · 2019Article
- Mutational analysis implicates the amyloid fibril as the toxic entity in Huntington's disease.Neurobiology of disease · 2018Article
- Model Selection Using BICePs: A Bayesian Approach for Force Field Validation and Parameterization.The journal of physical chemistry. B · 2018Article
- Biological consequences of improving the structural stability of hairpins that have antimicrobial activity.Journal of peptide science : an official publication of the European Peptide Society · 2017Article
- Optimization of a β-sheet-cap for long loop closure.Biopolymers · 2017Article
- Backbone Engineering within a Latent β-Hairpin Structure to Design Inhibitors of Polyglutamine Amyloid Formation.Journal of molecular biology · 2017Article
- Hairpin structure stability plays a role in the activity of two antimicrobial peptides.FEBS letters · 2016Article
- Peptide Inhibitors of the amyloidogenesis of IAPP: verification of the hairpin-binding geometry hypothesis.FEBS letters · 2016Article
- Aryl-aryl interactions in designed peptide folds: Spectroscopic characteristics and optimal placement for structure stabilization.Biopolymers · 2016Article
- X-ray Crystallographic Structure of Oligomers Formed by a Toxic β-Hairpin Derived from α-Synuclein: Trimers and Higher-Order Oligomers.Journal of the American Chemical Society · 2016Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Although much has been learned about the design of models of beta-sheets during the last decade, modest fold stabilities in water and terminal fraying remain a feature of most beta-hairpin peptides. In the case of hairpin capping, nature did not provide guidance for solving the problem. Some observations from prior turn capping designs, with further optimization, have provided a generally applicable, "unnatural" beta cap motif (alkanoyl-Trp at the N terminus and Trp-Thr-Gly at the C terminus) that provides a net contribution of 6 + kJ/mol to beta-hairpin stability, surpassing all other interactions that stabilize beta-hairpins including the covalent disulfide bond. The motif, made up entirely of natural residues, is specific to the termini of antiparallel beta-strands and reduces fraying at the ends of hairpins and other beta-sheet models. Utilizing this motif, 10- to 22-residue peptide scaffolds of defined stereochemistry that are greater than 98% folded in water have been prepared. The beta-cap can also be used to staple together short antiparallel beta-strands connected by a long flexible loop.
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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.