ArticleACS nano2013
Molecular structure of RADA16-I designer self-assembling peptide nanofibers.
Article in ACS nano, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed.
- Artificial intelligence-assisted design of self-assembling peptide hydrogels for neural regeneration: Principles and opportunities.Bioactive materials · 2027Review
- Supramolecular nanofiber stabilization of microdroplets enables ultra-sensitive virus infection analysis.Nature communications · 2026Article
- Nanomedicines and stroke: Advantages in chronic inflammation treatment and neural regeneration.Neural regeneration research · 2026Article
- Construction of a Three-Dimensional Culture Model of HSV-1 Based on the Nano-Self-Assembling Peptide RADA16-I and Preliminary Exploration of the Relationship Between HSV-1 and Autophagy.Microorganisms · 2026Article
- Nasal RADA16 hydrogel application decreases epistaxis severity scores in adults with hereditary hemorrhagic telangiectasia.Blood vessels, thrombosis & hemostasis · 2025Article
- A Photoresponsive Hybrid of Viruses and Supramolecular Peptide Fibers for Multidimensional Control of Patterning and Infection.Angewandte Chemie (International ed. in English) · 2025Article
- Host-Gated Enzymatic Release (H-GER) Enables Colorimetric Transduction for Enzyme Measurement.ACS applied materials & interfaces · 2025Article
- Efficacy of RADA16-Based Self-Assembling Peptides on Wound Healing: A Meta-Analysis of Preclinical Animal Studies.Pharmaceuticals (Basel, Switzerland) · 2025Article
- Nano-scaffold containing functional motif of stromal cell-derived factor 1 enhances neural stem cell behavior and synaptogenesis in traumatic brain injury.Scientific reports · 2025Article
- Peptide-Based Biomaterials for Combatting Infections and Improving Drug Delivery.Pharmaceutics · 2024Review
- Design of parallel 𝛽-sheet nanofibrils using Monte Carlo search, coarse-grained simulations, and experimental testing.Protein science : a publication of the Protein Society · 2024Article
- Parallel β-Sheet Structure and Structural Heterogeneity Detected within Q11 Self-Assembling Peptide Nanofibers.The journal of physical chemistry. B · 2024Article
- Molecular basis for curvature formation in SepF polymerization.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Self-Assembling Peptides with Insulin-Like Growth Factor Mimicry.ACS applied materials & interfaces · 2024Article
- Leveraging Biomaterial Platforms to Study Aging-Related Neural and Muscular Degeneration.Biomolecules · 2024Review
- Release systems based on self-assembling RADA16-I hydrogels with a signal sequence which improves wound healing processes.Scientific reports · 2023Article
- Computational approaches for the design of modulators targeting protein-protein interactions.Expert opinion on drug discovery · 2023Review
- Preparation and Characterization of Biomimetic Functional Scaffold with Gradient Structure for Osteochondral Defect Repair.Bioengineering (Basel, Switzerland) · 2023Review
- An Overview of Supramolecular Platforms Boosting Drug Delivery.Bioinorganic chemistry and applications · 2023Review
- Sequence patterns and signatures: Computational and experimental discovery of amyloid-forming peptides.PNAS nexus · 2022Article
4 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors.
Funding
Abstract
The designer self-assembling peptide RADA16-I forms nanofiber matrices which have shown great promise for regenerative medicine and three-dimensional cell culture. The RADA16-I amino acid sequence has a β-strand-promoting alternating hydrophobic/charged motif, but arrangement of β-strands into the nanofiber structure has not been previously determined. Here we present a structural model of RADA16-I nanofibers, based on solid-state NMR measurements on samples with different schemes for (13)C isotopic labeling. NMR peak positions and line widths indicate an ordered structure composed of β-strands. The NMR data show that the nanofibers are composed of two stacked β-sheets stabilized by a hydrophobic core formed by alanine side chains, consistent with previous proposals. However, the previously proposed antiparallel β-sheet structure is ruled out by measured (13)C-(13)C dipolar couplings. Instead, neighboring β-strands within β-sheets are parallel, with a registry shift that allows cross-strand staggering of oppositely charged arginine and aspartate side chains. The resulting structural model is compared to nanofiber dimensions observed via images taken by transmission electron microscopy and atomic force microscopy. Multiple NMR peaks for each alanine side chain were observed and could be attributed to multiple configurations of side chain packing within a single scheme for intermolecular packing.
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