Peptide Cyclization by the Use of Acylammonium Species.

Continuous Flow Cyclization Natural Products Peptides Specialty Peptides

Journal

Angewandte Chemie (International ed. in English)
ISSN: 1521-3773
Titre abrégé: Angew Chem Int Ed Engl
Pays: Germany
ID NLM: 0370543

Informations de publication

Date de publication:
03 07 2023
Historique:
received: 13 01 2023
medline: 29 6 2023
pubmed: 10 5 2023
entrez: 10 5 2023
Statut: ppublish

Résumé

Although cyclic peptides have become increasingly important as drugs, the most conventional peptide cyclization method using moderately active coupling agents suffers from a lot of waste and high cost as well as long reaction times and burdensome purification. Herein, we report an unconventional approach to peptide cyclization that uses acylammonium species generated from inexpensive and less wasteful Me

Identifiants

pubmed: 37161693
doi: 10.1002/anie.202300647
doi:

Substances chimiques

Peptides 0
Peptides, Cyclic 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

e202300647

Informations de copyright

© 2023 Wiley-VCH GmbH.

Références

For recent selected reviews that describe importance of cyclic peptide based drugs, see:
A. A. Vinogradov, Y. Yin, H. Suga, J. Am. Chem. Soc. 2019, 141, 4167-4181;
X. Jing, K. Jin, Med. Res. Rev. 2020, 40, 753-810;
H. Zhang, S. Chen, RSC Chem. Biol. 2022, 3, 18-31.
C. Jayanta, R. Florian, K. Horst, Angew. Chem. Int. Ed. 2013, 52, 254-269.
For selected reviews on chemical peptide cyclization, see:
C. J. White, A. K. Yudin, Nat. Chem. 2011, 3, 509-524;
A. El-Faham, F. Albericio, Chem. Rev. 2011, 111, 6557-6602;
F. Albericio, A. El-Faham, Org. Process Res. Dev. 2018, 22, 760-772;
V. Sarojini, A. J. Cameron, K. G. Varnava, W. A. Denny, G. Sanjayan, Chem. Rev. 2019, 119, 10318-10359.
F. Albericio, J. M. Bofill, A. El-Faham, S. A. Kates, J. Org. Chem. 1998, 63, 9678-9683.
J. Magano, Org. Process Res. Dev. 2022, 26, 1562-1689.
A. Isidro-Llobet, M. N. Kenworthy, S. Mukherjee, M. E. Kopach, K. Wegner, F. Gallou, A. G. Smith, F. Roschangar, J. Org. Chem. 2019, 84, 4615-4628.
 
R. A. Boissonnas, Helv. Chim. Acta 1951, 34, 874-879;
J. R. Vaughan, J. Am. Chem. Soc. 1951, 73, 3547;
T. Wieland, H. Bernhard, Justus Liebigs Ann. Chem. 1951, 572, 190-194.
 
T. Wieland, J. Faesel, H. Faulstich, Justus Liebigs Ann. Chem. 1968, 713, 201-208;
T. Wieland, J. Faesel, W. Konz, Justus Liebigs Ann. Chem. 1969, 722, 197-209;
H. Faulstich, E. Nebelin, T. Wieland, Justus Liebigs Ann. Chem. 1973, 1973, 50-58;
L. Tomasic, G. P. Lorenzi, Helv. Chim. Acta 1987, 70, 1012-1016;
G. C. Zanotti, B. E. Campbell, K. R. K. Easwaran, E. R. Blout, Int. J. Pept. Protein Res. 1988, 32, 527-535;
G. Zanotti, F. Rossi, M. Saviano, T. Tancredi, G. Saviano, A. Maione, M. Filizola, B. Di Blasio, C. Pedone, J. Am. Chem. Soc. 1995, 117, 8651-8658;
A. D‘Ursi, S. Albrizio, C. Fattorusso, A. Lavecchia, G. Zanotti, P. A. Temussi, J. Med. Chem. 1999, 42, 1705-1713.
R. A. Boissonnas, I. Schumann, Helv. Chim. Acta 1952, 35, 2229-2235.
 
S. Fuse, Y. Mifune, T. Takahashi, Angew. Chem. Int. Ed. 2014, 53, 851-855;
S. Fuse, Y. Mifune, H. Nakamura, H. Tanaka, Nat. Commun. 2016, 7, 13491;
Y. Mifune, H. Nakamura, S. Fuse, Org. Biomol. Chem. 2016, 14, 11244-11249;
S. Fuse, K. Masuda, Y. Otake, H. Nakamura, Chem. Eur. J. 2019, 25, 15091-15097;
Y. Otake, Y. Shibata, Y. Hayashi, S. Kawauchi, H. Nakamura, S. Fuse, Angew. Chem. Int. Ed. 2020, 59, 12925-12930.
S. Fuse, K. Komuro, Y. Otake, H. Masui, H. Nakamura, Chem. Eur. J. 2021, 27, 7525-7532.
 
J.-i. Yoshida, Flash Chemistry-Fast Organic Synthesis in Micro Systems, Wiley-VCH, Weinheim, 2008;
J.-i. Yoshida, A. Nagaki, T. Yamada, Chem. Eur. J. 2008, 14, 7450-7459.
D. J. Brunelle, E. P. Boden, Makromol. Chem. Macromol. Symp. 1992, 54-5, 397-412.
H. Mayr and co-workers reported higher nucleophilicity parameters for secondary amines (Me2NH in MeCN: 17.96, MeHNCH2CN in H2O: 13.50) compared with that of corresponding primary amines (MeNH2 in MeCN: 15.19, H2NCH2CN in H2O: 12.29).
T. A. Nigst, A. Antipova, H. Mayr, J. Org. Chem. 2012, 77, 8142-8155;
F. Brotzel, Y. C. Chu, H. Mayr, J. Org. Chem. 2007, 72, 3679-3688.
Y.-R. Zhao, X.-K. Wang, J. Zhou, C.-X. Cheng, X.-L. Huang, H.-M. Wu, Chin. J. Chem. 1995, 13, 552-557.
J. Han, M. Huang, Z. Wang, Y. Zheng, G. Zeng, W. He, N. Tan, J. Pept. Sci. 2015, 21, 550-553.
A. D. Curzons, D. J. C. Constable, D. N. Mortimer, V. L. Cunningham, Green Chem. 2001, 3, 1-6.
S. Zhang, Z. Amso, L. M. De Leon Rodriguez, H. Kaur, M. A. Brimble, J. Nat. Prod. 2016, 79, 1769-1774.
J. M. Humphrey, A. R. Chamberlin, Chem. Rev. 1997, 97, 2243-2266.
R. Chen, Z. Cheng, J. Huang, D. Liu, C. Wu, P. Guo, W. Lin, RSC Adv. 2017, 7, 49235-49243.
L. Posada, G. Serra, Tetrahedron Lett. 2019, 60, 151281.
B. Liebermann, W. Ihn, E. Baumann, D. Tresselt, Phytochemistry 1988, 27, 357-359.
R. Sato, K. Oyama, H. Konno, Tetrahedron 2018, 74, 6173-6181.

Auteurs

Otoka Shamoto (O)

Department of Basic Medicinal Sciences, Graduate School of Pharmaceutical Sciences, Nagoya University, Furo-cho, 464-8601, Nagoya, Chikusa-ku, Japan.

Keiji Komuro (K)

School of Life Science and Technology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, 226-8503, Yokohama, Midori-ku, Japan.

Naoto Sugisawa (N)

Department of Basic Medicinal Sciences, Graduate School of Pharmaceutical Sciences, Nagoya University, Furo-cho, 464-8601, Nagoya, Chikusa-ku, Japan.

Ting-Ho Chen (TH)

Department of Basic Medicinal Sciences, Graduate School of Pharmaceutical Sciences, Nagoya University, Furo-cho, 464-8601, Nagoya, Chikusa-ku, Japan.

Hiroyuki Nakamura (H)

Laboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, 4259 Nagatsuta-cho, 226-8503, Yokohama, Midori-ku, Japan.

Shinichiro Fuse (S)

Department of Basic Medicinal Sciences, Graduate School of Pharmaceutical Sciences, Nagoya University, Furo-cho, 464-8601, Nagoya, Chikusa-ku, Japan.

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