The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.
β‐Peptides: Synthesis by Arndt‐Eistert homologation with concomitant peptide coupling. Structure determination by NMR and CD spectroscopy and by X‐ray crystallography. Helical secondary structure of a β‐hexapeptide in solution and its stability towards pepsin
Abstract
The β‐hexapeptide (H‐β‐HVal‐β‐HAla‐β‐HLeu)2‐OH (2) was prepared from the component L‐β‐amino acids by conventional peptide synthesis, including fragment coupling. A cyclo‐β‐tri‐ and a cyclo‐β‐hexapeptide were also prepared. The β‐amino acids were obtained from α‐amino acids by Arndt‐Eistert homologation. All reactions leading to the β‐peptides occur smoothly and in high yields. The β‐peptides were characterized by their CD and NMR spectra (COSY, ROESY, TOCSY, and NOE‐restricted modelling), and by an X‐ray crystal‐structure analysis. β‐Sheet‐type structures (in the solid state) and a compact, left‐handed or (M) 31 helix of 5‐Å pitch (in solution) were discovered. Comparison with the analogous secondary structures of α‐peptides shows fundamental differences, the most surprising one at this point being the greater stability of β‐peptide helices. There are structural relationships of β‐peptides with oligomers of β‐hydroxyalkanoic acids, and dissimilarities between the two classes of compounds are a demonstration of the power of H‐bonding. The β‐hexapeptide 2 is stable to cleavage by pepsin at pH 2 in H 2 O for at least 60 h at 37°, while the corresponding α‐peptide H‐(Val‐Ala‐Leu)2‐OH is cleaved instantaneously under these conditions. The implication of the described results are discussed.
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
Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320
NMR with Proteins and Nucleic Acids
Wüthrich, K. (1986) · Europhysics News · doi:10.1051/epn/19861701011 · Cited by 7,989
Hydrogen Bonding in Biological Structures
Jeffrey, G. A., & Saenger, W. (1991) · Springer eBooks · doi:10.1007/978-3-642-85135-3 · Cited by 2,566
Chen, Y.-H., Yang, J. T., & Martinez, H. M. (1972) · Biochemistry · doi:10.1021/bi00772a015 · Cited by 1,957
Self-assembling organic nanotubes based on a cyclic peptide architecture
Ghadiri, M. R., Granja, J. R., Milligan, R. A., McRee, D. E., & Khazanovich, N. (1993) · Nature · doi:10.1038/366324a0 · Cited by 1,746
Turns in Peptides and Proteins
Rose, G. D., Glerasch, L. M., & Smith, J. A. (1985) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60063-7 · Cited by 1,666
Bothner-By, A. A., Stephens, R. L., Lee, J., Warren, C. D., & Jeanloz, R. W. (1984) · Journal of the American Chemical Society · doi:10.1021/ja00315a069 · Cited by 1,654
A Thermodynamic Scale for the Helix-Forming Tendencies of the Commonly Occurring Amino Acids
O'Neil, K. T., & DeGrado, W. F. (1990) · Science · doi:10.1126/science.2237415 · Cited by 1,188
Structural characteristics of .alpha.-helical peptide molecules containing Aib residues
Karle, I. L., & Balaram, P. (1990) · Biochemistry · doi:10.1021/bi00481a001 · Cited by 989
Cited by
Yashima, E., Ousaka, N., Taura, D., Shimomura, K., Ikai, T., & Maeda, K. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00354 · Cited by 2,004
Reversible peptide folding in solution by molecular dynamics simulation 1 1Edited by R. Huber
Daura, X., Jaun, B., Seebach, D., van Gunsteren, W. F., & Mark, A. E. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1885 · Cited by 373
Self-citationVasudev, P. G., Chatterjee, S., Shamala, N., & Balaram, P. (2011) · Chemical Reviews · doi:10.1021/cr100100x · Cited by 329
Ong, Z. Y., Wiradharma, N., & Yang, Y. Y. (2014) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2014.10.013 · Cited by 313
Peptides As Therapeutics with Enhanced Bioactivity
Goodwin, D., Simerska, P., & Toth, I. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712803251548 · Cited by 176
Metadata
- Authors
- Seebach, D., Overhand, M., Kühnle, F. N. M., Martinoni, B., Oberer, L., Hommel, U., & Widmer, H.
- Venue
- Helvetica Chimica Acta
- Publisher
- Wiley
- Published
- 1996-06-26
- Volume
- 79
- Issue
- 4
- Pages
- 913-941
- ISSN
- 0018-019X (ISSN-L)
- 1522-2675
- OpenAlex
- W2024935501
- Cited by
- 734
- References
- 54
- FWCI
- 10.27
- 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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: β‐Peptides: Synthesis by Arndt‐Eistert homologation with concomitant peptide coupling. Structure determination by NMR and CD spectroscopy and by X‐ray crystallography. Helical secondary structure of a β‐hexapeptide in solution and its stability towards pepsin. https://app.cochat.ai/papers/10.1002/hlca.19960790402
- The paper
- Seebach, D., Overhand, M., Kühnle, F. N. M., Martinoni, B., Oberer, L., Hommel, U., & Widmer, H. (1996). β‐Peptides: Synthesis by Arndt‐Eistert homologation with concomitant peptide coupling. Structure determination by NMR and CD spectroscopy and by X‐ray crystallography. Helical secondary structure of a β‐hexapeptide in solution and its stability towards pepsin. Helvetica Chimica Acta. https://doi.org/10.1002/hlca.19960790402
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.
