ArticleThe journal of physical chemistry. B2015
Polymorphism in self-assembly of peptide-based β-hairpin contributes to network morphology and hydrogel mechanical rigidity.
Article in The journal of physical chemistry. B, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- β-Hairpin-Based Peptide Hydrogels: The Case of MAX1.Gels (Basel, Switzerland) · 2026Review
- Functional Peptide-Based Biomaterials for Pharmaceutical Application: Sequences, Mechanisms, and Optimization Strategies.Journal of functional biomaterials · 2026Review
- Peptide Self-Assembled Nanocarriers for Cancer Drug Delivery.The journal of physical chemistry. B · 2023Review
- Different states and the associated fates of biomolecular condensates.Essays in biochemistry · 2022Review
- Direct observation of peptide hydrogel self-assembly.Chemical science · 2022Article
- Polymorphism in peptide self-assembly visualized.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- De novo design of a pH-triggered self-assembled β-hairpin nanopeptide with the dual biological functions for antibacterial and entrapment.Journal of nanobiotechnology · 2021Article
- Atomistic fibrillar architectures of polar prion-inspired heptapeptides.Chemical science · 2020Article
- Designer Self-Assembling Peptide Hydrogels to Engineer 3D Cell Microenvironments for Cell Constructs Formation and Precise Oncology Remodeling in Ovarian Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020Review
- From Microscale to Macroscale: Nine Orders of Magnitude for a Comprehensive Modeling of Hydrogels for Controlled Drug Delivery.Gels (Basel, Switzerland) · 2019Review
- Molecular simulations of self-assembling bio-inspired supramolecular systems and their connection to experiments.Chemical Society reviews · 2018Review
- Structural and Spectroscopic Properties of Assemblies of Self-Replicating Peptide Macrocycles.ACS nano · 2017Article
- A Protocol for the Design of Protein and Peptide Nanostructure Self-Assemblies Exploiting Synthetic Amino Acids.Methods in molecular biology (Clifton, N.J.) · 2017Article
- A minimal conformational switching-dependent model for amyloid self-assembly.Scientific reports · 2016Article
- Supramolecular Hydrogelators and Hydrogels: From Soft Matter to Molecular Biomaterials.Chemical reviews · 2015Review
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Authors and funding
3 authors.
Funding
Abstract
Hydrogels are proving to be an excellent class of materials for biomedical applications. The molecular self-assembly of designed MAX1 β-hairpin peptides into fibrillar networks has emerged as a novel route to form responsive hydrogels. Herein, computational modeling techniques are used to investigate the relative arrangements of individual hairpins within the fibrils that constitute the gel. The modeling provides insight into the morphology of the fibril network, which defines the gel's mechanical properties. Our study suggests polymorphic arrangements of the hairpins within the fibrils; however, the relative populations and the relative conformational energies of the polymorphic arrangements show a preference toward an arrangement of hairpins where their turn regions are not capable of forming intermolecular interaction. Repulsive intramolecular electrostatic interactions appear to dictate the formation of fibrils with shorter, rather than longer, persistent lengths. These repulsive intramolecular interactions also disfavor the formation of fibril entanglements. Taken together, the modeling predicts that MAX1 forms a network containing a large number of branch points, a network morphology supported by the formation of short fibril segments. We posit that, under static conditions, the preferred branched structures of the MAX1 peptide assembly result in a cross-linked hydrogel organization. At the same time, the shear stress leads to short fibrillar structures, thus fluidic hydrogel states.
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Registered trials
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