ArticleMacromolecular bioscience2017
Effect of Terminal Modification on the Molecular Assembly and Mechanical Properties of Protein-Based Block Copolymers.
Article in Macromolecular bioscience, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- Charting the envelope of mechanical properties of synthetic silk fibers through predictive modeling of the drawing process.Science advances · 2025Article
- Progress in Multiscale Modeling of Silk Materials.Biomacromolecules · 2024Review
- Materials-by-Design: Computation, Synthesis, and Characterization from Atoms to Structures.Physica scripta · 2018Article
- Multiscale modeling of keratin, collagen, elastin and related human diseases: Perspectives from atomistic to coarse-grained molecular dynamics simulations.Extreme Mechanics Letters · 2018Article
- High-Strength, Durable All-Silk Fibroin Hydrogels with Versatile Processability toward Multifunctional Applications.Advanced functional materials · 2018Article
- Predicting Silk Fiber Mechanical Properties through Multiscale Simulation and Protein Design.ACS biomaterials science & engineering · 2017Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
Accurate prediction and validation of the assembly of bioinspired peptide sequences into fibers with defined mechanical characteristics would aid significantly in designing and creating materials with desired properties. This process may also be utilized to provide insight into how the molecular architecture of many natural protein fibers is assembled. In this work, computational modeling and experimentation are used in tandem to determine how peptide terminal modification affects a fiber-forming core domain. Modeling shows that increased terminal molecular weight and hydrophilicity improve peptide chain alignment under shearing conditions and promote consolidation of semicrystalline domains. Mechanical analysis shows acute improvements to strength and elasticity, but significantly reduced extensibility and overall toughness. These results highlight an important entropic function that terminal domains of fiber-forming peptides exhibit as chain alignment promoters, which ultimately has notable consequences on the mechanical behavior of the final fiber products.
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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.