Download PDF
Synlett 2017; 28(15): 1913-1916
DOI: 10.1055/s-0036-1590795
cluster
© Georg Thieme Verlag Stuttgart · New York

Iminoboronate-Mediated Peptide Cyclization with Lysine Homologues

Kaicheng Li
Department of Chemistry, Merkert Chemistry Center, Boston College, 2609 Beacon Street, Chestnut Hill, MA 02467, USA   Email: jianmin.gao@bc.edu
,
Jianmin Gao  *
Department of Chemistry, Merkert Chemistry Center, Boston College, 2609 Beacon Street, Chestnut Hill, MA 02467, USA   Email: jianmin.gao@bc.edu
› Author AffiliationsThe financial support of this project is provided by the National Institutes of Health via grant GM102735
Further Information

Publication History

Received: 13 April 2017

Accepted after revision: 28 May 2017

Publication Date:
05 July 2017 (online)

    Permissions and Reprints All articles of this category


Published as part of the Cluster Recent Advances in Protein and Peptide Synthesis

Abstract

Cyclic peptides are attracting attention of medicinal chemists due to their increased stability in biological milieu as well as improved target binding affinities. Our laboratory has recently reported a powerful cyclization strategy that takes advantage of the spontaneous and reversible conjugation of lysine and a designed amino acid AB3 to give iminoboronates. Herein we report that Dap, a short chain homologue of lysine, displays significantly higher propensity to form imino­boronates and consequently improves the efficiency of peptide cyclization. Importantly, the preferential conjugation of AB3 to Dap allows a facile synthesis of cyclic peptides with free lysine residues.

Key words

peptide cyclization - reversible - iminoboronate - 2-APBA - Dap - pH

Supporting Information

    Supporting information for this article is available online at https://doi.org/10.1055/s-0036-1590795.
  • Supporting Information
 

  • References and Notes

  • 1 Baeriswyl V. Heinis C. ChemMedChem. 2013; 8: 377
    CrossrefPubMed
  • 2 White CJ. Yudin AK. Nat. Chem. 2011; 3: 509
    CrossrefPubMed
  • 3 Peraro L. Siegert TR. Kritzer JA. Methods Enzymol. 2016; 580: 303
  • 4 Malins LR. deGruyter JN. Robbins KJ. Scola PM. Eastgate MD. Ghadiri MR. Baran PS. J. Am. Chem. Soc. 2017; 139: 5233
    CrossrefPubMed
  • 5 McCarver SJ. Qiao JX. Carpenter J. Borzilleri RM. Poss MA. Eastgate MD. Miller MM. MacMillan DW. C. Angew. Chem. Int. Ed. 2017; 56: 728
    CrossrefPubMed
  • 6 Lawson KV. Rose TE. Harran PG. Proc. Natl. Acad. Sci., U.S.A. 2013; 110: E3753
    CrossrefPubMed
  • 7 Cromm PM. Schaubach S. Spiegel J. Fürstner A. Grossmann TN. Waldmann H. Nat. Commun. 2016; 7: 11300
    CrossrefPubMed
  • 8 Mendive-Tapia L. Preciado S. Garcia J. Ramon R. Kielland N. Albericio F. Lavilla R. Nat. Commun. 2015; 6: 7160
    CrossrefPubMed
  • 9 Zhang J. Mulumba M. Ong H. Lubell WD. Angew. Chem. Int. Ed. 2017; 56: 6284
    CrossrefPubMed
  • 10 Bowerman CJ. Nilsson BL. J. Am. Chem. Soc. 2010; 132: 9526
    CrossrefPubMed
  • 11 Qian Z. Xu X. Amacher JF. Madden DR. Cormet-Boyaka E. Pei D. Angew. Chem. Int. Ed. 2015; 54: 5874
    CrossrefPubMed
  • 12 Bandyopadhyay A. Gao J. J. Am. Chem. Soc. 2016; 138: 2098
    CrossrefPubMed
  • 13 Cal PM. Vicente JB. Pires E. Coelho AV. Veiros LF. Cordeiro C. Gois PM. J. Am. Chem. Soc. 2012; 134: 10299
    CrossrefPubMed
  • 14 Bandyopadhyay A. McCarthy KA. Kelly MA. Gao J. Nat. Commun. 2015; 6: 6561
    CrossrefPubMed
  • 15 Lan Y. Langlet-Bertin B. Abbate V. Vermeer LS. Kong X. Sullivan KE. Leborgne C. Scherman D. Hider RC. Drake AF. Bansal SS. Kichler A. Mason AJ. ChemBioChem. 2010; 11: 1266
    CrossrefPubMed
  • 16 Stubbs M. McSheehy PM. Griffiths JR. Bashford CL. Mol. Med. Today 2000; 6: 15
    CrossrefPubMed
  • 17 Weerakkody D. Moshnikova A. Thakur MS. Moshnikova V. Daniels J. Engelman DM. Andreev OA. Reshetnyak YK. Proc. Natl. Acad. Sci., U.S.A. 2013; 110: 5834
    CrossrefPubMed