Bacterial Cell-Surface Display of Semisynthetic Cyclic Peptides

ChemBioChem

Volumn 20, Issue 1, 2019, Pages 72-77

  Palei, Shubhendu ^a   Becher, Kira S ^a   Nienberg, Christian ^a   Jose, Joachim ^a   Mootz, Henning D ^a  

^a UNIVERSITY OF MÜNSTER   (Germany)

Author keywords

bacterial display; inteins; macrocycles; oxime ligation; semisynthesis

Indexed keywords

AMINO ACID; CYCLOPEPTIDE; OXIME;

ARTICLE; BACTERIAL CELL; CONTROLLED STUDY; CYCLIZATION; ESCHERICHIA COLI; FLUORESCENCE ACTIVATED CELL SORTING; FLUORESCENCE MICROSCOPY; GENOTYPE; NONHUMAN; PH; PHENOTYPE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN MODIFICATION; SITE DIRECTED MUTAGENESIS; WESTERN BLOTTING; BIOSYNTHESIS; CELL SURFACE DISPLAY; GENETICS; PEPTIDE LIBRARY; PROCEDURES; PROTEIN ENGINEERING; SYNTHESIS; TRANS SPLICING;

CELL SURFACE DISPLAY TECHNIQUES; CYCLIZATION; ESCHERICHIA COLI; OXIMES; PEPTIDE LIBRARY; PEPTIDES, CYCLIC; PROTEIN ENGINEERING; TRANS-SPLICING;

EID: 85055724875     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.201800552     Document Type: Article

References (34)

1. E. M. Driggers, S. P. Hale, J. Lee, N. K. Terrett, Nat. Rev. Drug Discovery 2008, 7, 608–624
2. Z. Qian, P. Upadhyaya, D. Pei, Methods Mol. Biol. 2015, 1248, 39–53
3. G. P. Smith, V. A. Petrenko, Chem. Rev. 1997, 97, 391–410
4. E. T. Boder, K. D. Wittrup, Nat. Biotechnol. 1997, 15, 553–557
5. T. Kawakami, A. Ohta, M. Ohuchi, H. Ashigai, H. Murakami, H. Suga, Nat. Chem. Biol. 2009, 5, 888–890
6. T. Passioura, H. Suga, Chem. Commun. 2017, 53, 1931–1940
7. Y. V. Schlippe, M. C. Hartman, K. Josephson, J. W. Szostak, J. Am. Chem. Soc. 2012, 134, 10469–10477
8. P. Timmerman, J. Beld, W. C. Puijk, R. H. Meloen, ChemBioChem 2005, 6, 821–824
9. C. Heinis, T. Rutherford, S. Freund, G. Winter, Nat. Chem. Biol. 2009, 5, 502–507
10. J. M. Smith, F. Vitali, S. A. Archer, R. Fasan, Angew. Chem. Int. Ed. 2011, 50, 5075–5080
11. Angew. Chem. 2011, 123, 5181–5186
12. A. E. Owens, I. de Paola, W. A. Hansen, Y. W. Liu, S. D. Khare, R. Fasan, J. Am. Chem. Soc. 2017, 139, 12559–12568
13. S. Ng, M. R. Jafari, R. Derda, ACS Chem. Biol. 2012, 7, 123–138
14. T. F. Woiwode, J. E. Haggerty, R. Katz, M. A. Gallop, R. W. Barrett, W. J. Dower, S. E. Cwirla, Chem. Biol. 2003, 10, 847–858
15. S. Palei, H. D. Mootz, ChemBioChem 2016, 17, 378–382
16. G. Volkmann, H. D. Mootz, Cell. Mol. Life Sci. 2013, 70, 1185–1206
17. N. H. Shah, T. W. Muir, Chem. Sci. 2014, 5, 446–461
18. J. H. Appleby-Tagoe, I. V. Thiel, Y. Wang, Y. Wang, H. D. Mootz, X. Q. Liu, J. Biol. Chem. 2011, 286, 34440–34447
19. J. Jose, R. M. Maas, M. G. Teese, J. Biotechnol. 2012, 161, 92–103
20. N. H. Shah, E. Eryilmaz, D. Cowburn, T. W. Muir, J. Am. Chem. Soc. 2013, 135, 18673–18681
21. T. Ando, S. Tsukiji, T. Tanaka, T. Nagamune, Chem. Commun. 2007, 4995–4997
22. G. Volkmann, X. Q. Liu, PLoS One 2009, 4, e8381
23. V. Schütz, H. D. Mootz, Angew. Chem. Int. Ed. 2014, 53, 4113–4117
24. Angew. Chem. 2014, 126, 4197–4201
25. D. Garbe, I. V. Thiel, H. D. Mootz, J. Pept. Sci. 2010, 16, 575–581
26. L. Wang, Z. Zhang, A. Brock, P. G. Schultz, Proc. Natl. Acad. Sci. USA 2003, 100, 56–61
27. A. Dirksen, T. M. Hackeng, P. E. Dawson, Angew. Chem. Int. Ed. 2006, 45, 7581–7584
28. Angew. Chem. 2006, 118, 7743–7746
29. T. Tanaka, T. Yamamoto, S. Tsukiji, T. Nagamune, ChemBioChem 2008, 9, 802–807
30. X. Bi, J. Yin, G. K. T. Nguyen, C. Rao, N. B. A. Halim, X. Hemu, J. P. Tam, C. F. Liu, Angew. Chem. Int. Ed. 2017, 56, 7822–7825
31. Angew. Chem. 2017, 129, 7930–7933
32. I. V. Thiel, G. Volkmann, S. Pietrokovski, H. D. Mootz, Angew. Chem. Int. Ed. 2014, 53, 1306–1310
33. Angew. Chem. 2014, 126, 1330–1334
34. A. L. Bachmann, H. D. Mootz, J. Biol. Chem. 2015, 290, 28792–28804