The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Self-Assembly of Multidomain Peptides: Balancing Molecular Frustration Controls Conformation and Nanostructure
Abstract
A series of nine, frustrated, multidomain peptides is described in which forces favoring self-assembly into a nanofiber versus those favoring disassembly could be easily modified. The peptides are organized into an ABA block motif in which the central B block is composed of alternating hydrophilic and hydrophobic amino acids (glutamine and leucine, respectively). This alternation allows the amino acid side chains to segregate on opposite sides of the peptide backbone when it is in a fully extended beta-sheet conformation. In water, packing between two such peptides stabilizes the extended conformation by satisfying the desire of the leucine side chains to exclude themselves from the aqueous environment. Once in this conformation intermolecular backbone hydrogen bonding can readily take place between additional peptides eventually growing into high aspect ratio fibers. B block assembly may continue infinitely or until monomeric peptides are depleted from solution which results in an insoluble precipitate. Block A consists of a variable number of positively charged lysine residues whose electrostatic repulsion at pH 7 works against the desire of the B block to assemble. Here we show that balancing the forces of block A against B allows the formation of controlled length, individually dispersed, and fully soluble nanofibers with a width of 6 +/- 1 nm and length of 120 +/- 30 nm. Analysis by infrared, circular dichroism, and vitreous ice cryo-transmission electron microscopy reveals that the relative sizes of blocks A and B dictate the peptide secondary structure which in turn controls the resulting nanostructure. The system described epitomizes the use of molecular frustration in the design of finite self-assembled structures. These materials, and ones based on their architecture, may find applications where nanostructured control over fiber architecture and chemical functionality is required.
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
Self-Assembly and Mineralization of Peptide-Amphiphile Nanofibers
Hartgerink, J. D., Beniash, E., & Stupp, S. I. (2001) · Science · doi:10.1126/science.1063187 · Cited by 3,601
Self-citationCrystal Engineering and Organometallic Architecture
Braga, D., Grepioni, F., & Desiraju, G. R. (1998) · Chemical Reviews · doi:10.1021/cr960091b · Cited by 1,178
Molecular self-assembly of surfactant-like peptides to form nanotubes and nanovesicles
Vauthey, S., Santoso, S., Gong, H., Watson, N., & Zhang, S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.072089599 · Cited by 835
Dynamic reassembly of peptide RADA16 nanofiber scaffold
Yokoi, H., Kinoshita, T., & Zhang, S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407843102 · Cited by 679
Paramonov, S. E., Jun, H.-W., & Hartgerink, J. D. (2006) · Journal of the American Chemical Society · doi:10.1021/ja060573x · Cited by 675
Self-citationFactors Controlling Long- and Short-Term Sequestration of Atmospheric CO 2 in a Mid-latitude Forest
Barford, C. C., Wofsy, S. C., Goulden, M. L., Munger, J. W., Pyle, E. H., Urbanski, S. P., Hutyra, L., Saleska, S. R., Fitzjarrald, D., & Moore, K. (2001) · Science · doi:10.1126/science.1062962 · Cited by 655
Ordered Mesoporous Polymers of Tunable Pore Size from Colloidal Silica Templates
Johnson, S. A., Ollivier, P. J., & Mallouk, T. E. (1999) · Science · doi:10.1126/science.283.5404.963 · Cited by 603
Pochan, D. J., Schneider, J. P., Kretsinger, J., Ozbas, B., Rajagopal, K., & Haines, L. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0353154 · Cited by 463
Salt-Triggered Peptide Folding and Consequent Self-Assembly into Hydrogels with Tunable Modulus
Ozbas, B., Kretsinger, J., Rajagopal, K., Schneider, J. P., & Pochan, D. J. (2004) · Macromolecules · doi:10.1021/ma0491762 · Cited by 429
Cope's Rule, Hypercarnivory, and Extinction in North American Canids
Van Valkenburgh, B., Wang, X., & Damuth, J. (2004) · Science · doi:10.1126/science.1102417 · Cited by 338
Positively Charged Surfactant-like Peptides Self-assemble into Nanostructures
von Maltzahn, G., Vauthey, S., Santoso, S., & Zhang, S. (2003) · Langmuir · doi:10.1021/la026526+ · Cited by 234
Compensation of Horizontal Temperature and Salinity Gradients in the Ocean Mixed Layer
Rudnick, D. L., & Ferrari, R. (1999) · Science · doi:10.1126/science.283.5401.526 · Cited by 228
Exploring amyloid formation by a de novo design
Kammerer, R. A., Kostrewa, D., Zurdo, J., Detken, A., García-Echeverría, C., Green, J. D., Müller, S. A., Meier, B. H., Winkler, F. K., Dobson, C. M., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0306786101 · Cited by 164
Conversion of Supramolecular Clusters to Macromolecular Objects
Zubarev, E. R., Pralle, M. U., Li, L., & Stupp, S. I. (1999) · Science · doi:10.1126/science.283.5401.523 · Cited by 161
Pagel, K., Wagner, S. C., Samedov, K., von Berlepsch, H., Böttcher, C., & Koksch, B. (2006) · Journal of the American Chemical Society · doi:10.1021/ja057450h · Cited by 111
Water-Soluble β-Sheet Models Which Self-Assemble into Fibrillar Structures
Janek, K., Behlke, J., Zipper, J., Fabian, H., Georgalis, Y., Beyermann, M., Bienert, M., & Krause, E. (1999) · Biochemistry · doi:10.1021/bi990510+ · Cited by 97
Short Homodimeric and Heterodimeric Coiled Coils
Dong, H., & Hartgerink, J. D. (2006) · Biomacromolecules · doi:10.1021/bm050833n · Cited by 59
Self-citation
Cited by
Shear-thinning hydrogels for biomedical applications
Guvendiren, M., Lu, H. D., & Burdick, J. A. (2012) · Soft Matter · doi:10.1039/c1sm06513k · Cited by 911
Galler, K. M., Aulisa, L., Regan, K. R., D’Souza, R. N., & Hartgerink, J. D. (2010) · Journal of the American Chemical Society · doi:10.1021/ja910481t · Cited by 339
Self-citationDentin Conditioning Codetermines Cell Fate in Regenerative Endodontics
Galler, K. M., D’Souza, R. N., Federlin, M., Cavender, A. C., Hartgerink, J. D., Hecker, S., & Schmalz, G. (2011) · Journal of Endodontics · doi:10.1016/j.joen.2011.08.027 · Cited by 323
Self-citationA Customized Self-Assembling Peptide Hydrogel for Dental Pulp Tissue Engineering
Galler, K. M., Hartgerink, J. D., Cavender, A. C., Schmalz, G., & D'Souza, R. N. (2012) · Tissue Engineering Part A · doi:10.1089/ten.tea.2011.0222 · Cited by 276
Self-citationMulti-component extracellular matrices based on peptide self-assembly
Collier, J. H., Rudra, J. S., Gasiorowski, J. Z., & Jung, J. P. (2010) · Chemical Society Reviews · doi:10.1039/b914337h · Cited by 229
Metadata
- Authors
- Dong, H., Paramonov, S. E., Aulisa, L., Bakota, E. L., & Hartgerink, J. D.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2007-09-26
- Volume
- 129
- Issue
- 41
- Pages
- 12468-12472
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2066181296
- Cited by
- 344
- References
- 17
- FWCI
- 7.55
- 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.
