메뉴 건너뛰기




Volumn 96, Issue 5, 2017, Pages 476-485

Macrocyclization of a potent PACE4 inhibitor: Benefits and limitations

Author keywords

Cyclization; PACE4 inhibitors; Peptides stability; Proprotein convertases; Prostate cancer

Indexed keywords

3 MERCAPTOPROPIONIC ACID; 4 AMIDINOBENZYLAMIDE; AMIDE; ANTINEOPLASTIC AGENT; CARBOXYLIC ACID; FURIN; PACE4 INHIBITOR; PEPTIDES AND PROTEINS; PROTEIN INHIBITOR; PROTEIN PACE4; UNCLASSIFIED DRUG; ENZYME INHIBITOR; PCSK6 PROTEIN, HUMAN; SERINE PROTEINASE;

EID: 85018759979     PISSN: 01719335     EISSN: 16181298     Source Type: Journal    
DOI: 10.1016/j.ejcb.2017.04.001     Document Type: Article
Times cited : (7)

References (50)
  • 1
    • 84954553885 scopus 로고    scopus 로고
    • Synthesis of linear and cyclic opioid-based peptide analogs containing multiple N-methylated amino acid residues
    • Adamska, A., Kolesinska, B., Kluczyk, A., Kaminski, Z.J., Janecka, A., Synthesis of linear and cyclic opioid-based peptide analogs containing multiple N-methylated amino acid residues. J. Pept. Sci. 21 (2015), 807–810.
    • (2015) J. Pept. Sci. , vol.21 , pp. 807-810
    • Adamska, A.1    Kolesinska, B.2    Kluczyk, A.3    Kaminski, Z.J.4    Janecka, A.5
  • 3
    • 84878782419 scopus 로고    scopus 로고
    • Cell-penetrating peptides: 20 years later, where do we stand?
    • Bechara, C., Sagan, S., Cell-penetrating peptides: 20 years later, where do we stand?. FEBS Lett. 587 (2013), 1693–1702.
    • (2013) FEBS Lett. , vol.587 , pp. 1693-1702
    • Bechara, C.1    Sagan, S.2
  • 6
    • 84996561930 scopus 로고    scopus 로고
    • Design of cyclized selective melanotropins
    • Cai, M., Hruby, V.J., Design of cyclized selective melanotropins. Biopolymers 106 (2016), 876–883.
    • (2016) Biopolymers , vol.106 , pp. 876-883
    • Cai, M.1    Hruby, V.J.2
  • 8
    • 84991665874 scopus 로고    scopus 로고
    • Dual-targeting anti-angiogenic cyclic peptides as potential drug leads for cancer therapy
    • Chan, L.Y., Craik, D.J., Daly, N.L., Dual-targeting anti-angiogenic cyclic peptides as potential drug leads for cancer therapy. Sci. Rep., 6, 2016, 35347.
    • (2016) Sci. Rep. , vol.6 , pp. 35347
    • Chan, L.Y.1    Craik, D.J.2    Daly, N.L.3
  • 9
    • 84938921989 scopus 로고    scopus 로고
    • The interplay of disulfide bonds, alpha-helicity, and hydrophobic interactions leads to ultrahigh proteolytic stability of peptides
    • Chen, Y., Yang, C., Li, T., Zhang, M., Liu, Y., Gauthier, M.A., Zhao, Y., Wu, C., The interplay of disulfide bonds, alpha-helicity, and hydrophobic interactions leads to ultrahigh proteolytic stability of peptides. Biomacromolecules 16 (2015), 2347–2355.
    • (2015) Biomacromolecules , vol.16 , pp. 2347-2355
    • Chen, Y.1    Yang, C.2    Li, T.3    Zhang, M.4    Liu, Y.5    Gauthier, M.A.6    Zhao, Y.7    Wu, C.8
  • 10
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction
    • Cheng, Y., Prusoff, W.H., Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction. Biochem. Pharmacol. 22 (1973), 3099–3108.
    • (1973) Biochem. Pharmacol. , vol.22 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.H.2
  • 11
    • 84860380797 scopus 로고    scopus 로고
    • On the cutting edge of proprotein convertase pharmacology: from molecular concepts to clinical applications
    • Couture, F., D'Anjou, F., Day, R., On the cutting edge of proprotein convertase pharmacology: from molecular concepts to clinical applications. Biomol. Concepts 2 (2011), 421–438.
    • (2011) Biomol. Concepts , vol.2 , pp. 421-438
    • Couture, F.1    D'Anjou, F.2    Day, R.3
  • 12
    • 84869191516 scopus 로고    scopus 로고
    • Role of proprotein convertases in prostate cancer progression
    • Couture, F., D'Anjou, F., Desjardins, R., Boudreau, F., Day, R., Role of proprotein convertases in prostate cancer progression. Neoplasia 14 (2012), 1032–1042.
    • (2012) Neoplasia , vol.14 , pp. 1032-1042
    • Couture, F.1    D'Anjou, F.2    Desjardins, R.3    Boudreau, F.4    Day, R.5
  • 16
    • 0036363433 scopus 로고    scopus 로고
    • N-terminal acylation of somatostatin analog with long chain fatty acids enhances its stability and anti-proliferative activity in human breast adenocarcinoma cells
    • Dasgupta, P., Singh, A., Mukherjee, R., N-terminal acylation of somatostatin analog with long chain fatty acids enhances its stability and anti-proliferative activity in human breast adenocarcinoma cells. Biol. Pharm. Bull. 25 (2002), 29–36.
    • (2002) Biol. Pharm. Bull. , vol.25 , pp. 29-36
    • Dasgupta, P.1    Singh, A.2    Mukherjee, R.3
  • 17
    • 0035496220 scopus 로고    scopus 로고
    • The development of androgen-independent prostate cancer
    • Feldman, B.J., Feldman, D., The development of androgen-independent prostate cancer. Nat. Rev. Cancer 1 (2001), 34–45.
    • (2001) Nat. Rev. Cancer , vol.1 , pp. 34-45
    • Feldman, B.J.1    Feldman, D.2
  • 18
    • 19544393760 scopus 로고    scopus 로고
    • Cutting back on pro-protein convertases: the latest approaches to pharmacological inhibition
    • Fugere, M., Day, R., Cutting back on pro-protein convertases: the latest approaches to pharmacological inhibition. Trends Pharmacol. Sci. 26 (2005), 294–301.
    • (2005) Trends Pharmacol. Sci. , vol.26 , pp. 294-301
    • Fugere, M.1    Day, R.2
  • 20
    • 1842530457 scopus 로고    scopus 로고
    • N-terminal His(7)-modification of glucagon-like peptide-1(7–36) amide generates dipeptidyl peptidase IV-stable analogues with potent antihyperglycaemic activity
    • Green, B.D., Mooney, M.H., Gault, V.A., Irwin, N., Bailey, C.J., Harriott, P., Greer, B., O'Harte, F.P., Flatt, P.R., N-terminal His(7)-modification of glucagon-like peptide-1(7–36) amide generates dipeptidyl peptidase IV-stable analogues with potent antihyperglycaemic activity. J. Endocrinol. 180 (2004), 379–388.
    • (2004) J. Endocrinol. , vol.180 , pp. 379-388
    • Green, B.D.1    Mooney, M.H.2    Gault, V.A.3    Irwin, N.4    Bailey, C.J.5    Harriott, P.6    Greer, B.7    O'Harte, F.P.8    Flatt, P.R.9
  • 22
    • 9644281041 scopus 로고    scopus 로고
    • Proprotein convertase models based on the crystal structures of furin and kexin: explanation of their specificity
    • Henrich, S., Lindberg, I., Bode, W., Than, M.E., Proprotein convertase models based on the crystal structures of furin and kexin: explanation of their specificity. J. Mol. Biol. 345 (2005), 211–227.
    • (2005) J. Mol. Biol. , vol.345 , pp. 211-227
    • Henrich, S.1    Lindberg, I.2    Bode, W.3    Than, M.E.4
  • 23
    • 84903274441 scopus 로고    scopus 로고
    • miR-124 exhibits antiproliferative and antiaggressive effects on prostate cancer cells through PACE4 pathway
    • Kang, S., Zhao, Y., Hu, K., Xu, C., Wang, L., Liu, J., Yao, A., Zhang, H., Cao, F., miR-124 exhibits antiproliferative and antiaggressive effects on prostate cancer cells through PACE4 pathway. Prostate 74 (2014), 1095–1106.
    • (2014) Prostate , vol.74 , pp. 1095-1106
    • Kang, S.1    Zhao, Y.2    Hu, K.3    Xu, C.4    Wang, L.5    Liu, J.6    Yao, A.7    Zhang, H.8    Cao, F.9
  • 25
    • 0036083664 scopus 로고    scopus 로고
    • Proprotein convertases in tumor progression and malignancy: novel targets in cancer therapy
    • Khatib, A.M., Siegfried, G., Chretien, M., Metrakos, P., Seidah, N.G., Proprotein convertases in tumor progression and malignancy: novel targets in cancer therapy. Am. J. Pathol. 160 (2002), 1921–1935.
    • (2002) Am. J. Pathol. , vol.160 , pp. 1921-1935
    • Khatib, A.M.1    Siegfried, G.2    Chretien, M.3    Metrakos, P.4    Seidah, N.G.5
  • 26
    • 84956885792 scopus 로고    scopus 로고
    • Applications and challenges for use of cell-penetrating peptides as delivery vectors for peptide and protein cargos
    • Kristensen, M., Birch, D., Morck Nielsen, H., Applications and challenges for use of cell-penetrating peptides as delivery vectors for peptide and protein cargos. Int. J. Mol. Sci., 17, 2016.
    • (2016) Int. J. Mol. Sci. , vol.17
    • Kristensen, M.1    Birch, D.2    Morck Nielsen, H.3
  • 29
    • 85031110806 scopus 로고    scopus 로고
    • Clinically localized prostate cancer in 2017: a review of comparative effectiveness
    • Lavery, H.J., Cooperberg, M.R., Clinically localized prostate cancer in 2017: a review of comparative effectiveness. Urol. Oncol., 2016.
    • (2016) Urol. Oncol.
    • Lavery, H.J.1    Cooperberg, M.R.2
  • 30
    • 15244363744 scopus 로고    scopus 로고
    • Synthesis, characterization, and pharmacokinetic studies of PEGylated glucagon-like peptide-1
    • Lee, S.H., Lee, S., Youn, Y.S., Na, D.H., Chae, S.Y., Byun, Y., Lee, K.C., Synthesis, characterization, and pharmacokinetic studies of PEGylated glucagon-like peptide-1. Bioconjug. Chem. 16 (2005), 377–382.
    • (2005) Bioconjug. Chem. , vol.16 , pp. 377-382
    • Lee, S.H.1    Lee, S.2    Youn, Y.S.3    Na, D.H.4    Chae, S.Y.5    Byun, Y.6    Lee, K.C.7
  • 31
    • 84973326483 scopus 로고    scopus 로고
    • Anti-tumor activity of benzylideneacetophenone derivatives via proteasomal inhibition in prostate cancer cells
    • Lee, Y.H., Yun, J., Jung, J.C., Oh, S., Jung, Y.S., Anti-tumor activity of benzylideneacetophenone derivatives via proteasomal inhibition in prostate cancer cells. Pharmazie 71 (2016), 274–279.
    • (2016) Pharmazie , vol.71 , pp. 274-279
    • Lee, Y.H.1    Yun, J.2    Jung, J.C.3    Oh, S.4    Jung, Y.S.5
  • 32
    • 84924264140 scopus 로고    scopus 로고
    • PACE4 inhibitors and their peptidomimetic analogs block prostate cancer tumor progression through quiescence induction, increased apoptosis and impaired neovascularisation
    • Levesque, C., Couture, F., Kwiatkowska, A., Desjardins, R., Guerin, B., Neugebauer, W.A., Day, R., PACE4 inhibitors and their peptidomimetic analogs block prostate cancer tumor progression through quiescence induction, increased apoptosis and impaired neovascularisation. Oncotarget 6 (2015), 3680–3693.
    • (2015) Oncotarget , vol.6 , pp. 3680-3693
    • Levesque, C.1    Couture, F.2    Kwiatkowska, A.3    Desjardins, R.4    Guerin, B.5    Neugebauer, W.A.6    Day, R.7
  • 34
  • 35
    • 0014454095 scopus 로고
    • Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors
    • Morrison, J.F., Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors. Biochim. Biophys. Acta 185 (1969), 269–286.
    • (1969) Biochim. Biophys. Acta , vol.185 , pp. 269-286
    • Morrison, J.F.1
  • 36
    • 34249794573 scopus 로고    scopus 로고
    • Preparation of amidines by amidoxime reduction with potassium formate
    • Nadrah, K., Dolenc, M.S., Preparation of amidines by amidoxime reduction with potassium formate. SYNLETT, 2007, 1257–1258.
    • (2007) SYNLETT , pp. 1257-1258
    • Nadrah, K.1    Dolenc, M.S.2
  • 38
    • 84929359754 scopus 로고    scopus 로고
    • Endothelin-A receptor antagonists in prostate cancer treatment – a meta-analysis
    • Qiao, L., Liang, Y., Li, N., Hu, X., Luo, D., Gu, J., Lu, Y., Zheng, Q., Endothelin-A receptor antagonists in prostate cancer treatment – a meta-analysis. Int. J. Clin. Exp. Med. 8 (2015), 3465–3473.
    • (2015) Int. J. Clin. Exp. Med. , vol.8 , pp. 3465-3473
    • Qiao, L.1    Liang, Y.2    Li, N.3    Hu, X.4    Luo, D.5    Gu, J.6    Lu, Y.7    Zheng, Q.8
  • 39
    • 55549121307 scopus 로고    scopus 로고
    • Targeting stat3 signaling in human prostate cancer cells using tyrosine kinase inhibitors
    • Qureshi, K., Lee, S., Lou, W., Trump, D., Gao, A., Targeting stat3 signaling in human prostate cancer cells using tyrosine kinase inhibitors. J. Clin. Oncol., 22, 2004, 3138.
    • (2004) J. Clin. Oncol. , vol.22 , pp. 3138
    • Qureshi, K.1    Lee, S.2    Lou, W.3    Trump, D.4    Gao, A.5
  • 41
    • 84989902469 scopus 로고    scopus 로고
    • Cyclic peptides for protein–protein interaction targets: applications to human disease
    • Rubin, S., Qvit, N., Cyclic peptides for protein–protein interaction targets: applications to human disease. Crit. Rev. Eukaryot. Gene Expr. 26 (2016), 199–221.
    • (2016) Crit. Rev. Eukaryot. Gene Expr. , vol.26 , pp. 199-221
    • Rubin, S.1    Qvit, N.2
  • 42
    • 84985920364 scopus 로고    scopus 로고
    • Oral administration of peptide-based drugs: beyond Lipinski's rule
    • Santos, G.B., Ganesan, A., Emery, F.S., Oral administration of peptide-based drugs: beyond Lipinski's rule. ChemMedChem 11 (2016), 2245–2251.
    • (2016) ChemMedChem , vol.11 , pp. 2245-2251
    • Santos, G.B.1    Ganesan, A.2    Emery, F.S.3
  • 43
    • 84860383419 scopus 로고    scopus 로고
    • The biology and therapeutic targeting of the proprotein convertases
    • Seidah, N.G., Prat, A., The biology and therapeutic targeting of the proprotein convertases. Nat. Rev. Drug Discov. 11 (2012), 367–383.
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 367-383
    • Seidah, N.G.1    Prat, A.2
  • 44
    • 84889424048 scopus 로고    scopus 로고
    • Peptides: Chemistry and Biology
    • Wiley-VCH
    • Sewald, N., Jakubke, H.-N., Peptides: Chemistry and Biology. 2009, Wiley-VCH.
    • (2009)
    • Sewald, N.1    Jakubke, H.-N.2
  • 45
    • 20144384859 scopus 로고    scopus 로고
    • Abbreviated nomenclature for cyclic and branched homo- and hetero-detic peptides
    • Spengler, J., Jimenez, J.C., Burger, K., Giralt, E., Albericio, F., Abbreviated nomenclature for cyclic and branched homo- and hetero-detic peptides. J. Pept. Res. 65 (2005), 550–555.
    • (2005) J. Pept. Res. , vol.65 , pp. 550-555
    • Spengler, J.1    Jimenez, J.C.2    Burger, K.3    Giralt, E.4    Albericio, F.5
  • 47
    • 17244364283 scopus 로고    scopus 로고
    • Proteases universally recognize beta strands in their active sites
    • Tyndall, J.D., Nall, T., Fairlie, D.P., Proteases universally recognize beta strands in their active sites. Chem. Rev. 105 (2005), 973–999.
    • (2005) Chem. Rev. , vol.105 , pp. 973-999
    • Tyndall, J.D.1    Nall, T.2    Fairlie, D.P.3
  • 48
    • 0034700141 scopus 로고    scopus 로고
    • The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters
    • Wender, P.A., Mitchell, D.J., Pattabiraman, K., Pelkey, E.T., Steinman, L., Rothbard, J.B., The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. Proc. Natl. Acad. Sci. U. S. A. 97 (2000), 13003–13008.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 13003-13008
    • Wender, P.A.1    Mitchell, D.J.2    Pattabiraman, K.3    Pelkey, E.T.4    Steinman, L.5    Rothbard, J.B.6
  • 49
    • 33745107170 scopus 로고    scopus 로고
    • Strategies to improve plasma half life time of peptide and protein drugs
    • Werle, M., Bernkop-Schnurch, A., Strategies to improve plasma half life time of peptide and protein drugs. Amino Acids 30 (2006), 351–367.
    • (2006) Amino Acids , vol.30 , pp. 351-367
    • Werle, M.1    Bernkop-Schnurch, A.2
  • 50
    • 84896714985 scopus 로고    scopus 로고
    • No improvement noted in overall or cause-specific survival for men presenting with metastatic prostate cancer over a 20-year period
    • Wu, J.N., Fish, K.M., Evans, C.P., Devere White, R.W., Dall'Era, M.A., No improvement noted in overall or cause-specific survival for men presenting with metastatic prostate cancer over a 20-year period. Cancer 120 (2014), 818–823.
    • (2014) Cancer , vol.120 , pp. 818-823
    • Wu, J.N.1    Fish, K.M.2    Evans, C.P.3    Devere White, R.W.4    Dall'Era, M.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.