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The twists and turns of β‐peptides
Abstract
Abstract: Recently, it has been discovered that peptides composed of β‐amino acids are capable of adopting novel secondary structures demonstrating that peptides composed of α‐amino acids are not unique in their ability to fold into well‐defined structures. Cyclic as well as acyclic peptides composed of β‐amino acid residues adopt turn, helical, and sheet‐like conformations. Here, we discuss the synthesis and conformational preferences of individual, substituted β‐amino acids as well as the structures that peptides composed of these residues, β‐peptides, may adopt.
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Cited by
Vasudev, P. G., Chatterjee, S., Shamala, N., & Balaram, P. (2011) · Chemical Reviews · doi:10.1021/cr100100x · Cited by 329
Masui, H., & Fuse, S. (2022) · Organic Process Research & Development · doi:10.1021/acs.oprd.2c00074 · Cited by 38
Metadata
- Authors
- DeGrado, W. F., Schneider, J. P., & Hamuro, Y.
- Venue
- The Journal of Peptide Research
- Publisher
- Wiley
- Published
- 1999-09
- Volume
- 54
- Issue
- 3
- Pages
- 206-217
- ISSN
- 1397-002X (ISSN-L)
- OpenAlex
- W1900730650
- Cited by
- 174
- References
- 0
- FWCI
- 4.02
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: The twists and turns of β‐peptides. https://app.cochat.ai/papers/10.1034/j.1399-3011.1999.00131.x
- The paper
- DeGrado, W. F., Schneider, J. P., & Hamuro, Y. (1999). The twists and turns of β‐peptides. The Journal of Peptide Research. https://doi.org/10.1034/j.1399-3011.1999.00131.x
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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.
