The DOI matches its Crossref record; 222 of the 222 references it cites were found in a registry or an index.
Biomimetic peptide self-assembly for functional materials
Open accessAbstract
Natural biomolecular systems have evolved to form a rich variety of supramolecular materials and machinery fundamental to cellular function. The assembly of these structures commonly involves interactions between specific molecular building blocks, a strategy that can also be replicated in an artificial setting to prepare functional materials. The self-assembly of synthetic biomimetic peptides thus allows the exploration of chemical and sequence space beyond that used routinely by biology. In this Review, we discuss recent conceptual and experimental advances in self-assembling artificial peptidic materials. In particular, we explore how naturally occurring structures and phenomena have inspired the development of functional biomimetic materials that we can harness for potential interactions with biological systems. As our fundamental understanding of peptide self-assembly evolves, increasingly sophisticated materials and applications emerge and lead to the development of a new set of building blocks and assembly principles relevant to materials science, molecular biology, nanotechnology and precision medicine. The self-assembly of biomimetic peptides can mimic complex natural systems involving whole proteins. This Review describes how synthetic peptides afford tunable scaffolds for biomineralization, drug delivery and tissue growth.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Antimicrobial peptides of multicellular organisms
Zasloff, M. (2002) · Nature · doi:10.1038/415389a · Cited by 8,457
Whitesides, G. M., & Grzybowski, B. (2002) · Science · doi:10.1126/science.1070821 · Cited by 7,439
Biomolecular condensates: organizers of cellular biochemistry
Banani, S. F., Lee, H. O., Hyman, A. A., & Rosen, M. K. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.7 · Cited by 6,100
Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
Brogden, K. A. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1098 · Cited by 5,829
A Hexanucleotide Repeat Expansion in C9ORF72 Is the Cause of Chromosome 9p21-Linked ALS-FTD
Renton, A. E., Majounie, E., Waite, A., Simón-Sánchez, J., Rollinson, S., Gibbs, J. R., Schymick, J. C., Laaksovirta, H., van Swieten, J. C., Myllykangas, L., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.09.010 · Cited by 4,409
Liquid phase condensation in cell physiology and disease
Shin, Y., & Brangwynne, C. P. (2017) · Science · doi:10.1126/science.aaf4382 · Cited by 4,152
Functional Supramolecular Polymers
Aida, T., Meijer, E. W., & Stupp, S. I. (2012) · Science · doi:10.1126/science.1205962 · Cited by 3,696
Fabrication of novel biomaterials through molecular self-assembly
Zhang, S. (2003) · Nature Biotechnology · doi:10.1038/nbt874 · Cited by 3,347
Liquid-Liquid Phase Separation in Biology
Hyman, A. A., Weber, C. A., & Jülicher, F. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100913-013325 · Cited by 3,155
Lehn, J. (1990) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199013041 · Cited by 3,027
Cited by
Accelerating the prediction and discovery of peptide hydrogels with human-in-the-loop
Xu, T., Wang, J., Zhao, S., Chen, D., Zhang, H., Fang, Y., Kong, N., Zhou, Z., Li, W., & Wang, H. (2023) · Nature Communications · doi:10.1038/s41467-023-39648-2 · Cited by 132
Clinical translation of nanomedicines for brain diseases: Current challenges and future directions
Wang, G., Wang, N., Xia, X., Ismail, M., & Shi, B. (2026) · Journal of Controlled Release · doi:10.1016/j.jconrel.2025.114426 · Cited by 33
Regulation of Peptide Liquid–Liquid Phase Separation by Aromatic Amino Acid Composition
Netzer, A., Baruch Leshem, A., Veretnik, S., Edelstein, I., & Lampel, A. (2024) · Small · doi:10.1002/smll.202401665 · Cited by 28
Design of the Hydrophobic Core of Self‐Assembling Peptide Fibrils for Enhanced Neural Regeneration
Tsai, Y., Cavallo, P., Lu, Q., Yu, J., Ender, C. P., Link, J., Amann‐Winkel, K., Endres, K., Synatschke, C. V., & John, T. (2025) · Small Science · doi:10.1002/smsc.202500224 · Cited by 3
Metadata
- Authors
- Levin, A., Hakala, T. A., Schnaider, L., Bernardes, G. J. L., Gazit, E., & Knowles, T. P. J.
- Venue
- Nature Reviews Chemistry
- Published
- 2020-09-15
- Volume
- 4
- Issue
- 11
- Pages
- 615-634
- ISSN
- 2397-3358 (ISSN-L)
- OpenAlex
- W4230321861
- Cited by
- 853
- References
- 222
- FWCI
- 5.01
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Biomimetic peptide self-assembly for functional materials. https://app.cochat.ai/papers/10.1038/s41570-020-0215-y
- The paper
- Levin, A., Hakala, T. A., Schnaider, L., Bernardes, G. J. L., Gazit, E., & Knowles, T. P. J. (2020). Biomimetic peptide self-assembly for functional materials. Nature Reviews Chemistry. https://doi.org/10.1038/s41570-020-0215-y
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
