The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
Self-assembly of Surfactant-like Peptides with Variable Glycine Tails to Form Nanotubes and Nanovesicles
Abstract
The self-assembly of surfactant-like peptides containing 4−10 glycines as the component of the hydrophobic tails and aspartic acids as the hydrophilic heads is described. The peptide monomers form nanotubes and nanovesicles in water at neutral pH. These nanostructures become more polydisperse as the length of the glycine tails increases. These unique structures may serve not only as scaffolds for constructing diverse nanodevices but also as enclosures to encapsulate rudimentary enzymes for studying prebiotic molecular evolution.
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
Miller, S. L., & Urey, H. C. (1959) · Science · doi:10.1126/science.130.3370.245 · Cited by 1,405
Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane.
Zhang, S., Holmes, T., Lockshin, C., & Rich, A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.8.3334 · Cited by 1,304
Self-citationExtensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds
Holmes, T. C., de Lacalle, S., Su, X., Liu, G., Rich, A., & Zhang, S. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.12.6728 · Cited by 1,124
Self-citationInteractions between acidic proteins and crystals: stereochemical requirements in biomineralization.
Addadi, L., & Weiner, S. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4110 · Cited by 1,089
Aggeli, A., Nyrkova, I. A., Bell, M., Harding, R., Carrick, L., McLeish, T. C. B., Semenov, A. N., & Boden, N. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.191250198 · Cited by 1,048
Artificial transmembrane ion channels from self-assembling peptide nanotubes
Ghadiri, M. R., Granja, J. R., & Buehler, L. K. (1994) · Nature · doi:10.1038/369301a0 · Cited by 971
Antibacterial agents based on the cyclic d,l-α-peptide architecture
Fernandez-Lopez, S., Kim, H.-S., Choi, E. C., Delgado, M., Granja, J. R., Khasanov, A., Kraehenbuehl, K., Long, G., Weinberger, D. A., Wilcoxen, K. M., et al. (2001) · Nature · doi:10.1038/35086601 · Cited by 938
Responsive gels formed by the spontaneous self-assembly of peptides into polymeric β-sheet tapes
Aggeli, A., Bell, M., Boden, N., Keen, J. N., Knowles, P. F., McLeish, T. C. B., Pitkeathly, M., & Radford, S. E. (1997) · Nature · doi:10.1038/386259a0 · Cited by 858
Lipid Tubules: A Paradigm for Molecularly Engineered Structures
Schnur, J. M. (1993) · Science · doi:10.1126/science.262.5140.1669 · Cited by 723
Self-complementary oligopeptide matrices support mammalian cell attachment
Zhang, S., Holmes, T. C., DiPersio, C. M., Hynes, R. O., Su, X., & Rich, A. (1995) · Biomaterials · doi:10.1016/0142-9612(95)96874-y · Cited by 680
Self-citation
Cited by
Fabrication of novel biomaterials through molecular self-assembly
Zhang, S. (2003) · Nature Biotechnology · doi:10.1038/nbt874 · Cited by 3,347
Self-citationHydrogels in regenerative medicine
Slaughter, B. V., Khurshid, S. S., Fisher, O. Z., Khademhosseini, A., & Peppas, N. A. (2009) · Advanced Materials · doi:10.1002/adma.200802106 · Cited by 2,703
Molecular self-assembly and applications of designer peptide amphiphiles
Zhao, X., Pan, F., Xu, H., Yaseen, M., Shan, H., Hauser, C. A. E., Zhang, S., & Lu, J. R. (2010) · Chemical Society Reviews · doi:10.1039/b915923c · Cited by 668
Self-citationDesign of nanostructured biological materials through self-assembly of peptides and proteins
Zhang, S., Marini, D. M., Hwang, W., & Santoso, S. (2002) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(02)00391-5 · Cited by 572
Self-citationEmerging biological materials through molecular self-assembly
Zhang, S. (2002) · Biotechnology Advances · doi:10.1016/s0734-9750(02)00026-5 · Cited by 558
Self-citationSelf-assembling peptides and proteins for nanotechnological applications
Rajagopal, K., & Schneider, J. P. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2004.06.006 · Cited by 476
Self‐assembly in nature: using the principles of nature to create complex nanobiomaterials
Mendes, A. C., Baran, E. T., Reis, R. L., & Azevedo, H. S. (2013) · WIREs Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.1238 · Cited by 440
Prebiotic Peptides: Molecular Hubs in the Origin of Life
Frenkel-Pinter, M., Samanta, M., Ashkenasy, G., & Leman, L. J. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00664 · Cited by 354
Hamley, I. W. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201310006 · Cited by 323
Self-assembly of peptides to nanostructures
Mandal, D., Nasrolahi Shirazi, A., & Parang, K. (2014) · Org. Biomol. Chem. · doi:10.1039/c4ob00447g · Cited by 318
Self-assembling peptide nanotubes
Scanlon, S., & Aggeli, A. (2008) · Nano Today · doi:10.1016/s1748-0132(08)70041-0 · Cited by 293
Self-Assembling Peptide EAK16 and RADA16 Nanofiber Scaffold Hydrogel
Gelain, F., Luo, Z., & Zhang, S. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00690 · Cited by 267
Self-citationTesauro, D., Accardo, A., Diaferia, C., Milano, V., Guillon, J., Ronga, L., & Rossi, F. (2019) · Molecules · doi:10.3390/molecules24020351 · Cited by 225
Peptidic Biomaterials: From Self-Assembling to Regenerative Medicine
Pugliese, R., & Gelain, F. (2017) · Trends in Biotechnology · doi:10.1016/j.tibtech.2016.09.004 · Cited by 133
Lipid-like Self-Assembling Peptides
Zhang, S. (2012) · Accounts of Chemical Research · doi:10.1021/ar300034v · Cited by 132
Self-citationPeptide-Based Functional Biomaterials for Soft-Tissue Repair
Hosoyama, K., Lazurko, C., Muñoz, M., McTiernan, C. D., & Alarcon, E. I. (2019) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2019.00205 · Cited by 118
The origin and evolution of the ribosome
Smith, T. F., Lee, J. C., Gutell, R. R., & Hartman, H. (2008) · Biology Direct · doi:10.1186/1745-6150-3-16 · Cited by 85
Self-citationMungi, C., & Rajamani, S. (2015) · Life · doi:10.3390/life5010065 · Cited by 49
(2008) · doi:10.1017/cbo9780511536557.022 · Cited by 4
Metadata
- Authors
- Santoso, S., Hwang, W., Hartman, H., & Zhang, S.
- Venue
- Nano Letters
- Publisher
- American Chemical Society (ACS)
- Published
- 2002-05-30
- Volume
- 2
- Issue
- 7
- Pages
- 687-691
- ISSN
- 1530-6984 (ISSN-L)
- 1530-6992
- OpenAlex
- W2147251458
- Cited by
- 326
- References
- 25
- FWCI
- 5.53
- Type
- journal article
- Language
- en
- Open access
- closed
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
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.