Details
| Original language | English |
|---|---|
| Pages (from-to) | 5259-5269 |
| Number of pages | 11 |
| Journal | Bioorganic and Medicinal Chemistry |
| Volume | 26 |
| Issue number | 19 |
| Early online date | 26 Mar 2018 |
| Publication status | Published - 15 Oct 2018 |
Abstract
The argyrins are a family of non-ribosomal peptides that exhibits different biological activities through only small structural changes. Ideally, a biologically active molecule can be tracked and observed in a variety of biological and clinical settings in a non-invasive manner. As a step towards this goal, we report here a chemical synthesis of unnatural deep blue amino acid β-(1-azulenyl)-L alanine with different fluorescence and photophysical properties, which allows a spectral separation from the native tryptophan signal. This might be especially useful for cell localization studies and visualizing the targeted proteins. In particular, the synthesis of β-(1-azulenyl)-L alanine was achieved through a Negishi coupling which proved to be a powerful tool for the synthesis of unnatural tryptophan analogs. Upon β-(1-azulenyl)-L alanine incorporation into argyrin C, deep blue octapeptide variant was spectrally and structurally characterized.
Keywords
- Argyrin, Azulene, Cyclic peptide, Fluorescent label, Modified amino acids
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Medicine
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Pharmacology, Toxicology and Pharmaceutics(all)
- Pharmaceutical Science
- Pharmacology, Toxicology and Pharmaceutics(all)
- Drug Discovery
- Biochemistry, Genetics and Molecular Biology(all)
- Clinical Biochemistry
- Chemistry(all)
- Organic Chemistry
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In: Bioorganic and Medicinal Chemistry, Vol. 26, No. 19, 15.10.2018, p. 5259-5269.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Painting argyrins blue
T2 - Negishi cross-coupling for synthesis of deep-blue tryptophan analogue β-(1-azulenyl)-L alanine and its incorporation into argyrin C
AU - Stempel, Erik
AU - Kaml, Robert Franz Xaver
AU - Budisa, Nediljko
AU - Kalesse, Markus
N1 - Funding Information: We thank Dr. J. Fohrer, M. Rettstadt, and D. Körtje for detailed 2D-NMR analysis and R. Reichel for mass spectra. Dr. Tobias Baumann is acknowledged for instrumental supervision during measurements of spectral properties. In terms of preparation of this manuscript we thank Annika Kalks and Timo Hans-Martin Hoffmann. RFXK acknowledges DFG Grant BU1404/9-1 for a PhD position.
PY - 2018/10/15
Y1 - 2018/10/15
N2 - The argyrins are a family of non-ribosomal peptides that exhibits different biological activities through only small structural changes. Ideally, a biologically active molecule can be tracked and observed in a variety of biological and clinical settings in a non-invasive manner. As a step towards this goal, we report here a chemical synthesis of unnatural deep blue amino acid β-(1-azulenyl)-L alanine with different fluorescence and photophysical properties, which allows a spectral separation from the native tryptophan signal. This might be especially useful for cell localization studies and visualizing the targeted proteins. In particular, the synthesis of β-(1-azulenyl)-L alanine was achieved through a Negishi coupling which proved to be a powerful tool for the synthesis of unnatural tryptophan analogs. Upon β-(1-azulenyl)-L alanine incorporation into argyrin C, deep blue octapeptide variant was spectrally and structurally characterized.
AB - The argyrins are a family of non-ribosomal peptides that exhibits different biological activities through only small structural changes. Ideally, a biologically active molecule can be tracked and observed in a variety of biological and clinical settings in a non-invasive manner. As a step towards this goal, we report here a chemical synthesis of unnatural deep blue amino acid β-(1-azulenyl)-L alanine with different fluorescence and photophysical properties, which allows a spectral separation from the native tryptophan signal. This might be especially useful for cell localization studies and visualizing the targeted proteins. In particular, the synthesis of β-(1-azulenyl)-L alanine was achieved through a Negishi coupling which proved to be a powerful tool for the synthesis of unnatural tryptophan analogs. Upon β-(1-azulenyl)-L alanine incorporation into argyrin C, deep blue octapeptide variant was spectrally and structurally characterized.
KW - Argyrin
KW - Azulene
KW - Cyclic peptide
KW - Fluorescent label
KW - Modified amino acids
UR - http://www.scopus.com/inward/record.url?scp=85046637685&partnerID=8YFLogxK
U2 - 10.1016/j.bmc.2018.03.037
DO - 10.1016/j.bmc.2018.03.037
M3 - Article
C2 - 29729984
AN - SCOPUS:85046637685
VL - 26
SP - 5259
EP - 5269
JO - Bioorganic and Medicinal Chemistry
JF - Bioorganic and Medicinal Chemistry
SN - 0968-0896
IS - 19
ER -