Peptide-Chain Elongation Using Unprotected Amino Acids in a Micro-Flow Reactor.


Journal

Chemistry (Weinheim an der Bergstrasse, Germany)
ISSN: 1521-3765
Titre abrégé: Chemistry
Pays: Germany
ID NLM: 9513783

Informations de publication

Date de publication:
27 Nov 2019
Historique:
received: 02 08 2019
revised: 28 08 2019
pubmed: 31 8 2019
medline: 14 1 2020
entrez: 31 8 2019
Statut: ppublish

Résumé

Conventional peptide synthesis requires a deprotection step after each amidation step, which decreases synthetic efficiency. Therefore, peptide synthesis using unprotected amino acids is considered an ideal approach. Here, we report peptide chain elongation using unprotected amino acids via a mixed carbonic anhydride. Micro-flow technology enabled rapid mixing of an organic layer containing a protected amino acid or dipeptide and an aqueous layer containing an unprotected amino acid or dipeptide to accelerate the desired amidation, and this approach successfully suppressed undesired racemization/epimerization (≤0.4 %). Various di-, tri-, and tetra-peptides were obtained in good to high yields. This is the first report on peptide chain elongation that proceeds without severe racemization from unprotected amino acids using inexpensive, nonexplosive, less wasteful, and less toxic reagents.

Identifiants

pubmed: 31468609
doi: 10.1002/chem.201903531
doi:

Substances chimiques

Amino Acids 0
Peptides 0
Carbon Dioxide 142M471B3J

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

15091-15097

Subventions

Organisme : Japan Science and Technology Agency
ID : JPMJMI18G7
Organisme : Japan Society for the Promotion of Science
ID : ID No. 19J14624

Informations de copyright

© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

Références

 
D. J. C. Constable, P. J. Dunn, J. D. Hayler, G. R. Humphrey, J. J. L. Leazer, R. J. Linderman, K. Lorenz, J. Manley, B. A. Pearlman, A. Wells, A. Zaks, T. Y. Zhang, Green Chem. 2007, 9, 411-420;
V. R. Pattabiraman, J. W. Bode, Nature 2011, 480, 471-479;
M. C. Bryan, P. J. Dunn, D. Entwistle, F. Gallou, S. G. Koenig, J. D. Hayler, M. R. Hickey, S. Hughes, M. E. Kopach, G. Moine, P. Richardson, F. Roschangar, A. Steven, F. J. Weiberth, Green Chem. 2018, 20, 5082-5103.
 
G. W. Anderson, J. E. Zimmerman, F. M. Callahan, J. Am. Chem. Soc. 1964, 86, 1839-1842;
S. Nowshuddin, A. Ram Reddy, Tetrahedron: Asymmetry 2011, 22, 22-25.
 
Y. V. Mitin, Int. J. Pept. Protein Res. 1996, 48, 374-376;
V. V. S. Babu, R. V. R. Rao, Indian J. Chem. B 2005, 44, 2328-2332;
C. Meneses, S. L. Nicoll, L. Trembleau, J. Org. Chem. 2010, 75, 564-569.
P. Gagnon, X. Huang, E. Therrien, J. W. Keillor, Tetrahedron Lett. 2002, 43, 7717-7719.
 
N. L. Benoiton, Y. Lee, F. M. F. Chen, Int. J. Pept. Protein Res. 1988, 31, 443-446;
T. Noguchi, N. Tehara, Y. Uesugi, S. Jung, N. Imai, Chem. Lett. 2012, 41, 42-43;
T. Noguchi, S. Jung, N. Imai, Chem. Lett. 2012, 41, 577-579.
 
A. R. Katritzky, E. Todadze, J. Cusido, P. Angrish, A. A. Shestopalov, Chem. Biol. Drug Des. 2006, 68, 37-41;
A. R. Katritzky, P. Angrish, K. Suzuki, Synthesis 2006, 411-424;
A. R. Katritzky, E. Todadze, P. Angrish, B. Draghici, J. Org. Chem. 2007, 72, 5794-5801;
A. R. Katritzky, G. Meher, T. Narindoshvili, J. Org. Chem. 2008, 73, 7153-7158.
 
K. Hofmann, T. A. Thompson, H. Yajima, E. T. Schwartz, H. Inouye, J. Am. Chem. Soc. 1960, 82, 3715-3721;
T. Nagase, T. Fukami, Y. Urakawa, U. Kumagai, K. Ishikawa, Tetrahedron Lett. 1993, 34, 2495-2496.
Z. Z. Brown, C. E. Schafmeister, J. Am. Chem. Soc. 2008, 130, 14382-14383.
 
D. S. Kemp, S. W. Wang, J. Rebek, R. C. Mollan, C. Banquer, G. Subramanyam, Tetrahedron 1974, 30, 3955-3967;
D. S. Kemp, S. J. Wrobel, S. W. Wang, Z. Bernstein, J. Rebek, Tetrahedron 1974, 30, 3969-3980;
A. F. Hegarty, D. G. McCarthy, J. Am. Chem. Soc. 1980, 102, 4537-4538.
 
S.-T. Chen, K.-T. Wang, J. Chem. Soc. Chem. Commun. 1990, 1045-1047;
L. A. Andreeva, L. Y. Alfeeva, V. N. Potaman, V. N. Nezavibatko, Int. J. Pept. Protein Res. 1992, 39, 493-496;
C. Palomo, A. L. Palomo, F. Palomo, A. Mielgo, Org. Lett. 2002, 4, 4005-4008.
 
M. G. Ryadnov, N. Y. Kashparova, I. A. Kashparov, Y. V. Mitin, Bioorg. Khim. 1998, 24, 408-411;
M. G. Ryadnov, L. V. Klimenko, Y. V. Mitin, Bioorg. Khim. 1999, 25, 323-328;
C. Hashimoto, K. Takeguchi, M. Kodomari, Synlett 2011, 1427-1430.
M. V. Anuradha, B. Ravindranath, Tetrahedron 1997, 53, 1123-1130.
Y. Huang, W.-H. Feng, Chin. Chem. Lett. 2016, 27, 357-360.
S. H. van Leeuwen, P. J. L. M. Quaedflieg, Q. B. Broxterman, R. M. J. Liskamp, Tetrahedron Lett. 2002, 43, 9203-9207.
 
S. H. van Leeuwen, P. J. L. M. Quaedflieg, Q. B. Broxterman, Y. Milhajlovic, R. M. J. Liskamp, Tetrahedron Lett. 2005, 46, 653-656;
R. M. Lanigan, V. Karaluka, M. T. Sabatini, P. Starkov, M. Badland, L. Boulton, T. D. Sheppard, Chem. Commun. 2016, 52, 8846-8849.
Z. Li, H. Fu, H. Gong, Y. Zhao, Bioorg. Chem. 2004, 32, 170-177.
R. G. Denkewalter, R. Hirschmann, Am. Sci. 1969, 57, 389-409.
J. Spengler, C. Böttcher, F. Albericio, K. Burger, Chem. Rev. 2006, 106, 4728-4746.
 
J. R. Vaughan, J. Am. Chem. Soc. 1951, 73, 3547;
The molar cost of ClCO2iBu is 1/14 and 1/210 compared with that of EDCI and HBTU, respectively.
J. Kovacs, E. M. Holleran, K. Y. Hui, J. Org. Chem. 1980, 45, 1060-1065.
G. Verardo, A. Gorassini, J. Pept. Sci. 2013, 19, 315-324.
Selected recent reviews for flow synthesis, see:
M. Baumann, I. R. Baxendale, Beilstein J. Org. Chem. 2015, 11, 1194-1219;
J. Britton, C. L. Raston, Chem. Soc. Rev. 2017, 46, 1250-1271;
F. Fanelli, G. Parisi, L. Degennaro, R. Luisi, Beilstein J. Org. Chem. 2017, 13, 520-542;
R. Gérardy, N. Emmanuel, T. Toupy, V.-E. Kassin, N. N. Tshibalonza, M. Schmitz, J.-C. M. Monbaliu, Eur. J. Org. Chem. 2018, 2301-2351;
M. B. Plutschack, B. Pieber, K. Gilmore, P. H. Seeberger, Chem. Rev. 2017, 117, 11796-11893;
R. Porta, M. Benaglia, A. Puglisi, Org. Process Res. Dev. 2016, 20, 2-25;
I. Rossetti, M. Compagnoni, Chem. Eng. J. 2016, 296, 56-70;
C. A. Shukla, A. A. Kulkarni, Beilstein J. Org. Chem. 2017, 13, 960-987.
 
S. Ramesh, P. Cherkupally, B. G. de la Torre, T. Govender, H. G. Kruger, F. Albericio, Amino Acids 2014, 46, 2091-2104;
N. Ahmed, Chem. Biol. Drug Des. 2018, 91, 647-650;
S. Fuse, Y. Otake, H. Nakamura, Chem. Asian J. 2018, 13, 3818-3832;
C. P. Gordon, Org. Biomol. Chem. 2018, 16, 180-196.
 
S. Fuse, N. Tanabe, T. Takahashi, Chem. Commun. 2011, 47, 12661-12663;
S. Fuse, Y. Mifune, T. Takahashi, Angew. Chem. Int. Ed. 2014, 53, 851-855;
Angew. Chem. 2014, 126, 870-874;
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.
M. J. Jebrail, A. H. C. Ng, V. Rai, R. Hili, A. K. Yudin, A. R. Wheeler, Angew. Chem. Int. Ed. 2010, 49, 8625-8629;
Angew. Chem. 2010, 122, 8807-8811.
T. S. Chisholm, D. Clayton, L. J. Dowman, J. Sayers, R. J. Payne, J. Am. Chem. Soc. 2018, 140, 9020-9024.
 
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;
J.-i. Yoshida, Chem. Rec. 2010, 10, 332-341.
Y. Otake, H. Nakamura, S. Fuse, Angew. Chem. Int. Ed. 2018, 57, 11389-11393;
Angew. Chem. 2018, 130, 11559-11563.
Rapid mixing of organic-aqueous biphasic solution was required at the second mixer to avoid undesired racemization/epimerization; therefore, the V-shaped mixer was used in this study. We previously reported better mixing of the V-shaped mixer compared with that of the T-shaped mixer. See ref. [28].
 
Y. E. Jad, A. Kumar, A. El-Faham, B. G. de la Torre, F. Albericio, ACS Sustainable Chem. Eng. 2019, 7, 3671-3683;
K. G. Varnava, V. Sarojini, Chem. Asian J. 2019, 14, 1088-1097.
 
G. A. Acosta, M. del Fresno, M. Paradis-Bas, M. Rigau-DeLlobet, S. Cote, M. Royo, F. Albericio, J. Pept. Sci. 2009, 15, 629-633;
Y. E. Jad, G. A. Acosta, S. N. Khattab, B. G. de la Torre, T. Govender, H. G. Kruger, A. El-Faham, F. Albericio, Org. Biomol. Chem. 2015, 13, 2393-2398.
ClCO2iPr tends to undergo decarboxylation; therefore, its storage and transfer in large scale requires special care.
G. G. Smith, T. Sivakua, J. Org. Chem. 1983, 48, 627-634.
M. E. Khatib, M. Elagawany, E. Çalışkan, E. F. Davis, H. M. Faidallah, S. A. El-feky, A. R. Katritzky, Chem. Commun. 2013, 49, 2631-2633.
J. D. Goodreid, E. da Silveira dos Santos, R. A. Batey, Org. Lett. 2015, 17, 2182-2185.
J. Ivkovic, C. Lembacher-Fadum, R. Breinbauer, Org. Biomol. Chem. 2015, 13, 10456-10460.
Z. Liu, N. Yasuda, M. Simeone, R. A. Reamer, J. Org. Chem. 2014, 79, 11792-11796.

Auteurs

Shinichiro Fuse (S)

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

Koshiro Masuda (K)

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

Yuma Otake (Y)

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

Hiroyuki Nakamura (H)

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

Articles similaires

Photosynthesis Ribulose-Bisphosphate Carboxylase Carbon Dioxide Molecular Dynamics Simulation Cyanobacteria
Semiconductors Photosynthesis Polymers Carbon Dioxide Bacteria
Risk Assessment Plant Leaves Isomerism Humans Stereoisomerism
Animals Huntington Disease Mitochondria Neurons Mice

Classifications MeSH