메뉴 건너뛰기




Volumn 7, Issue 16, 2015, Pages 2121-2130

Beyond cyclosporine A: Conformation-dependent passive membrane permeabilities of cyclic peptide natural products

Author keywords

cyclic peptide; cyclosporine; PAMPA; permeability

Indexed keywords

CYCLOASPEPTIDE A; CYCLOPEPTIDE; CYCLOSPORIN A; CYCLOSPORIN B; CYCLOSPORIN D; CYCLOSPORINE C; CYCLOSPORINE E; CYCLOSPORINE H; DAPTOMYCIN; DESMETHYLDESTRUXIN B; DESTRUXIN A; DESTRUXIN B; DESTRUXIN B2; DESTRUXIN E CHLOROHYDRIN; DESTRUXIN E2 CHLOROHYDRIN; DIDEMNIN A; ENNIATIN; ENNIATIN H; ENNIATIN I; ENNIATIN J1; ENNIATIN MK1; GUANGOMIDE A; GUANGOMIDE B; MIRABAMIDE C; PATELLAMIDE C; SCLEROTIOTIDE F; SCYTALIDAMIDE; TENTOXIN; UNCLASSIFIED DRUG; UNINDEXED DRUG; VERRUCAMIDE B; ARTIFICIAL MEMBRANE; BIOLOGICAL PRODUCT; CYCLOSPORIN;

EID: 84942253842     PISSN: 17568919     EISSN: 17568927     Source Type: Journal    
DOI: 10.4155/fmc.15.78     Document Type: Article
Times cited : (126)

References (59)
  • 2
    • 79957575162 scopus 로고    scopus 로고
    • Analysis of the human endogenous coregulator complexome
    • Malovannaya A, Lanz RB, Jung SY et al. Analysis of the human endogenous coregulator complexome. Cell 145(5), 787-799 (2011).
    • (2011) Cell , vol.145 , Issue.5 , pp. 787-799
    • Malovannaya, A.1    Lanz, R.B.2    Jung, S.Y.3
  • 3
    • 19944395483 scopus 로고    scopus 로고
    • Potent inhibition of Huntingtin aggregation and cytotoxicity by a disulfide bondfree single-domain intracellular antibody
    • Colby DW, Chu Y, Cassady JP et al. Potent inhibition of Huntingtin aggregation and cytotoxicity by a disulfide bondfree single-domain intracellular antibody. Proc. Natl Acad. Sci. USA 101(51), 17616-17621 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , Issue.51 , pp. 17616-17621
    • Colby, D.W.1    Chu, Y.2    Cassady, J.P.3
  • 4
    • 84907812263 scopus 로고    scopus 로고
    • Factor XII: A drug target for safe interference with thrombosis and inflammation
    • Kenne E, Renne T. Factor XII: A drug target for safe interference with thrombosis and inflammation. Drug Discov. Today 19(9), 1459-1464 (2014).
    • (2014) Drug Discov. Today , vol.19 , Issue.9 , pp. 1459-1464
    • Kenne, E.1    Renne, T.2
  • 5
    • 84865455090 scopus 로고    scopus 로고
    • The future of antibodies as cancer drugs
    • Reichert JM, Dhimolea E. The future of antibodies as cancer drugs. Drug Discov. Today 17(17-18), 954-963 (2012).
    • (2012) Drug Discov. Today , vol.17 , Issue.17-18 , pp. 954-963
    • Reichert, J.M.1    Dhimolea, E.2
  • 6
    • 84902176344 scopus 로고    scopus 로고
    • Selection-based discovery of druglike macrocyclic peptides
    • Passioura T, Katoh T, Goto Y, Suga H. Selection-based discovery of druglike macrocyclic peptides. Annu. Rev. Biochem. 83, 727-752 (2014).
    • (2014) Annu. Rev. Biochem. , vol.83 , pp. 727-752
    • Passioura, T.1    Katoh, T.2    Goto, Y.3    Suga, H.4
  • 7
    • 84863121468 scopus 로고    scopus 로고
    • Design of triazole-stapled BCL9 alpha-helical peptides to target the beta-catenin/B-cell CLL/lymphoma 9 (BCL9) protein-protein interaction
    • Kawamoto SA, Coleska A, Ran X, Yi H, Yang CY, Wang S. Design of triazole-stapled BCL9 alpha-helical peptides to target the beta-catenin/B-cell CLL/lymphoma 9 (BCL9) protein-protein interaction. J. Med. Chem. 55(3), 1137-1146 (2012).
    • (2012) J. Med. Chem. , vol.55 , Issue.3 , pp. 1137-1146
    • Kawamoto, S.A.1    Coleska, A.2    Ran, X.3    Yi, H.4    Yang, C.Y.5    Wang, S.6
  • 8
    • 79951723092 scopus 로고    scopus 로고
    • Synthesis of cell-permeable stapled peptide dual inhibitors of the p53-Mdm2/Mdmx interactions via photoinduced cycloaddition
    • Madden MM, Muppidi A, Li Z, Li X, Chen J, Lin Q. Synthesis of cell-permeable stapled peptide dual inhibitors of the p53-Mdm2/Mdmx interactions via photoinduced cycloaddition. Bioorg. Med. Chem. Lett. 21(5), 1472-1475 (2011).
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , Issue.5 , pp. 1472-1475
    • Madden, M.M.1    Muppidi, A.2    Li, Z.3    Li, X.4    Chen, J.5    Lin, Q.6
  • 9
    • 70449671729 scopus 로고    scopus 로고
    • Direct inhibition of the NOTCH transcription factor complex
    • Moellering RE, Cornejo M, Davis TN et al. Direct inhibition of the NOTCH transcription factor complex. Nature 462(7270), 182-188 (2009).
    • (2009) Nature , vol.462 , Issue.7270 , pp. 182-188
    • Moellering, R.E.1    Cornejo, M.2    Davis, T.N.3
  • 10
    • 68549098042 scopus 로고    scopus 로고
    • Investigation of the relative cellular permeability of DNA-binding pyrrole-imidazole polyamides
    • Liu B, Kodadek T. Investigation of the relative cellular permeability of DNA-binding pyrrole-imidazole polyamides. J. Med. Chem. 52(15), 4604-4612 (2009).
    • (2009) J. Med. Chem. , vol.52 , Issue.15 , pp. 4604-4612
    • Liu, B.1    Kodadek, T.2
  • 11
    • 84906327241 scopus 로고    scopus 로고
    • Comprehensive analysis of loops at protein-protein interfaces for macrocycle design
    • Gavenonis J, Sheneman BA, Siegert TR, Eshelman MR. Comprehensive analysis of loops at protein-protein interfaces for macrocycle design. Nat. Chem. Biol. 10(9), 716-722 (2014).
    • (2014) Nat. Chem. Biol. , vol.10 , Issue.9 , pp. 716-722
    • Gavenonis, J.1    Sheneman, B.A.2    Siegert, T.R.3    Eshelman, M.R.4
  • 12
    • 84877753039 scopus 로고    scopus 로고
    • Flexizyme-mediated genetic reprogramming as a tool for noncanonical peptide synthesis and drug discovery
    • Passioura T, Suga H. Flexizyme-mediated genetic reprogramming as a tool for noncanonical peptide synthesis and drug discovery. Chem. Eur. J. 19(21), 6530-6536 (2013).
    • (2013) Chem. Eur. J. , vol.19 , Issue.21 , pp. 6530-6536
    • Passioura, T.1    Suga, H.2
  • 13
    • 84863485794 scopus 로고    scopus 로고
    • Peptide bicycles that inhibit the Grb2 SH2 domain
    • Quartararo JS, Wu P, Kritzer JA. Peptide bicycles that inhibit the Grb2 SH2 domain. Chembiochem 13(10), 1490-1496 (2012).
    • (2012) Chembiochem , vol.13 , Issue.10 , pp. 1490-1496
    • Quartararo, J.S.1    Wu, P.2    Kritzer, J.A.3
  • 14
    • 9444236174 scopus 로고    scopus 로고
    • Small peptides as potent mimetics of the protein hormone erythropoietin
    • Wrighton NC, Farrell FX, Chang R et al. Small peptides as potent mimetics of the protein hormone erythropoietin. Science 273(5274), 458-464 (1996).
    • (1996) Science , vol.273 , Issue.5274 , pp. 458-464
    • Wrighton, N.C.1    Farrell, F.X.2    Chang, R.3
  • 15
    • 0034461768 scopus 로고    scopus 로고
    • Drug-like properties and the causes of poor solubility and poor permeability
    • Lipinski CA. Drug-like properties and the causes of poor solubility and poor permeability. J. Pharmacol. Toxicol. Methods 44(1), 235-249 (2000).
    • (2000) J. Pharmacol. Toxicol. Methods , vol.44 , Issue.1 , pp. 235-249
    • Lipinski, C.A.1
  • 16
    • 46449115901 scopus 로고    scopus 로고
    • The exploration of macrocycles for drug discovery [mdash] an underexploited structural class
    • Driggers EM, Hale SP, Lee J, Terrett NK. The exploration of macrocycles for drug discovery [mdash] an underexploited structural class. Nat. Rev. Drug Discov. 7(7), 608-624 (2008).
    • (2008) Nat. Rev. Drug Discov. , vol.7 , Issue.7 , pp. 608-624
    • Driggers, E.M.1    Hale, S.P.2    Lee, J.3    Terrett, N.K.4
  • 17
    • 84864679725 scopus 로고    scopus 로고
    • Macrocycles in new drug discovery
    • Mallinson J, Collins I. Macrocycles in new drug discovery. Future Med. Chem. 4(11), 1409-1438 (2012).
    • (2012) Future Med. Chem. , vol.4 , Issue.11 , pp. 1409-1438
    • Mallinson, J.1    Collins, I.2
  • 18
    • 84906322796 scopus 로고    scopus 로고
    • Drug discovery: Tools and rules for macrocycles
    • Heinis C. Drug discovery: tools and rules for macrocycles. Nat. Chem. Biol. 10(9), 696-698 (2014).
    • (2014) Nat. Chem. Biol. , vol.10 , Issue.9 , pp. 696-698
    • Heinis, C.1
  • 20
    • 84892163643 scopus 로고    scopus 로고
    • Macrocyclic drugs and clinical candidates: What can medicinal chemists learn from their properties?
    • Giordanetto F, Kihlberg J. Macrocyclic drugs and clinical candidates: what can medicinal chemists learn from their properties? J. Med. Chem. 57(2), 278-295 (2013).
    • (2013) J. Med. Chem. , vol.57 , Issue.2 , pp. 278-295
    • Giordanetto, F.1    Kihlberg, J.2
  • 21
    • 84878789554 scopus 로고    scopus 로고
    • Form and function in cyclic peptide natural products: A pharmacokinetic perspective
    • Bockus AT, McEwen CM, Lokey RS. Form and function in cyclic peptide natural products: A pharmacokinetic perspective. Curr. Top. Med. Chem. 13(1873-4294), 821-836 (2013).
    • (2013) Curr. Top. Med. Chem. , vol.13 , Issue.1873-4294 , pp. 821-836
    • Bockus, A.T.1    McEwen, C.M.2    Lokey, R.S.3
  • 22
    • 33644698797 scopus 로고    scopus 로고
    • Long-term levothyroxine treatment decreases the oral bioavailability of cyclosporin A by inducing P-glycoprotein in small intestine
    • Jin M, Shimada T, Shintani M, Yokogawa K, Nomura M, Miyamoto K. Long-term levothyroxine treatment decreases the oral bioavailability of cyclosporin A by inducing P-glycoprotein in small intestine. Drug Metab. Pharmacokinet. 20(5), 324-330 (2005).
    • (2005) Drug Metab. Pharmacokinet. , vol.20 , Issue.5 , pp. 324-330
    • Jin, M.1    Shimada, T.2    Shintani, M.3    Yokogawa, K.4    Nomura, M.5    Miyamoto, K.6
  • 23
    • 84862025745 scopus 로고    scopus 로고
    • Use of 3D properties to characterize beyond rule-of-5 property space for passive permeation
    • Guimaraes CR, Mathiowetz AM, Shalaeva M, Goetz G, Liras S. Use of 3D properties to characterize beyond rule-of-5 property space for passive permeation. J. Chem. Inf. Comput. Sci. 52(4), 882-890 (2012).
    • (2012) J. Chem. Inf. Comput. Sci. , vol.52 , Issue.4 , pp. 882-890
    • Guimaraes, C.R.1    Mathiowetz, A.M.2    Shalaeva, M.3    Goetz, G.4    Liras, S.5
  • 24
    • 84909586310 scopus 로고    scopus 로고
    • Oral druggable space beyond the rule of 5: Insights from drugs and clinical candidates
    • Doak BC, Over B, Giordanetto F, Kihlberg J. Oral druggable space beyond the rule of 5: insights from drugs and clinical candidates. Chem. Biol. 21(9), 1115-1142 (2014).
    • (2014) Chem. Biol. , vol.21 , Issue.9 , pp. 1115-1142
    • Doak, B.C.1    Over, B.2    Giordanetto, F.3    Kihlberg, J.4
  • 26
    • 0032568397 scopus 로고    scopus 로고
    • Physicochemical high throughput screening: Parallel artificial membrane permeation assay in the description of passive absorption processes
    • Kansy M, Senner F, Gubernator K. Physicochemical high throughput screening: parallel artificial membrane permeation assay in the description of passive absorption processes. J. Med. Chem. 41(7), 1007-1010 (1998).
    • (1998) J. Med. Chem. , vol.41 , Issue.7 , pp. 1007-1010
    • Kansy, M.1    Senner, F.2    Gubernator, K.3
  • 27
    • 80054853098 scopus 로고    scopus 로고
    • On-resin N-methylation of cyclic peptides for discovery of orally bioavailable scaffolds
    • White TR, Renzelman CM, Rand AC et al. On-resin N-methylation of cyclic peptides for discovery of orally bioavailable scaffolds. Nat. Chem. Biol. 7(11), 810-817 (2011).
    • (2011) Nat. Chem. Biol. , vol.7 , Issue.11 , pp. 810-817
    • White, T.R.1    Renzelman, C.M.2    Rand, A.C.3
  • 28
    • 0030804754 scopus 로고    scopus 로고
    • Comparison of Neoral and Sandimmun for induction and maintenance immunosuppression after kidney transplantation
    • Senel FM, Yildirim S, Karakayali H, Moray G, Haberal M. Comparison of Neoral and Sandimmun for induction and maintenance immunosuppression after kidney transplantation. Transplant Int. 10(5), 357-361 (1997).
    • (1997) Transplant Int. , vol.10 , Issue.5 , pp. 357-361
    • Senel, F.M.1    Yildirim, S.2    Karakayali, H.3    Moray, G.4    Haberal, M.5
  • 31
    • 0029782010 scopus 로고    scopus 로고
    • Proton transport across transient single-file water pores in a lipid membrane studied by molecular dynamics simulations
    • Marrink SJ, Jahnig F, Berendsen HJ. Proton transport across transient single-file water pores in a lipid membrane studied by molecular dynamics simulations. Biophys. J. 71(2), 632-647 (1996).
    • (1996) Biophys. J. , vol.71 , Issue.2 , pp. 632-647
    • Marrink, S.J.1    Jahnig, F.2    Berendsen, H.J.3
  • 32
    • 0035811455 scopus 로고    scopus 로고
    • Utilization of an intramolecular hydrogen bond to increase the CNS penetration of an NK(1) receptor antagonist
    • Ashwood VA, Field MJ, Horwell DC et al. Utilization of an intramolecular hydrogen bond to increase the CNS penetration of an NK(1) receptor antagonist. J. Med. Chem. 44(14), 2276-2285 (2001).
    • (2001) J. Med. Chem. , vol.44 , Issue.14 , pp. 2276-2285
    • Ashwood, V.A.1    Field, M.J.2    Horwell, D.C.3
  • 33
    • 0037413559 scopus 로고    scopus 로고
    • Discovery of a thieno[2,3-d] pyrimidine-2,4-dione bearing a p-methoxyureidophenyl moiety at the 6-position: A highly potent and orally bioavailable non-peptide antagonist for the human luteinizing hormone-releasing hormone receptor
    • Sasaki S, Cho N, Nara Y et al. Discovery of a thieno[2,3-d] pyrimidine-2,4-dione bearing a p-methoxyureidophenyl moiety at the 6-position: A highly potent and orally bioavailable non-peptide antagonist for the human luteinizing hormone-releasing hormone receptor. J. Med. Chem. 46(1), 113-124 (2003).
    • (2003) J. Med. Chem. , vol.46 , Issue.1 , pp. 113-124
    • Sasaki, S.1    Cho, N.2    Nara, Y.3
  • 34
    • 33644644973 scopus 로고    scopus 로고
    • Testing the conformational hypothesis of passive membrane permeability using synthetic cyclic peptide diastereomers
    • Rezai T, Yu B, Millhauser G, Jacobson M, Lokey R. Testing the conformational hypothesis of passive membrane permeability using synthetic cyclic peptide diastereomers. J. Am. Chem. Soc. 128(8), 2510-2511 (2006).
    • (2006) J. Am. Chem. Soc. , vol.128 , Issue.8 , pp. 2510-2511
    • Rezai, T.1    Yu, B.2    Millhauser, G.3    Jacobson, M.4    Lokey, R.5
  • 35
    • 33750482579 scopus 로고    scopus 로고
    • Conformational flexibility, internal hydrogen bonding, and passive membrane permeability: Successful in silico prediction of the relative permeabilities of cyclic peptides
    • Rezai T, Bock J, Zhou M, Kalyanaraman C, Lokey R, Jacobson M. Conformational flexibility, internal hydrogen bonding, and passive membrane permeability: Successful in silico prediction of the relative permeabilities of cyclic peptides. J. Am. Chem. Soc. 128(43), 14073-14080 (2006).
    • (2006) J. Am. Chem. Soc. , vol.128 , Issue.43 , pp. 14073-14080
    • Rezai, T.1    Bock, J.2    Zhou, M.3    Kalyanaraman, C.4    Lokey, R.5    Jacobson, M.6
  • 36
    • 79952361347 scopus 로고    scopus 로고
    • HNK2 receptor antagonists. The use of intramolecular hydrogen bonding to increase solubility and membrane permeability
    • Ettorre A, D'Andrea P, Mauro S et al. hNK2 receptor antagonists. The use of intramolecular hydrogen bonding to increase solubility and membrane permeability. Bioorg. Med. Chem. Lett. 21(6), 1807-1809 (2011).
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , Issue.6 , pp. 1807-1809
    • Ettorre, A.1    D'Andrea, P.2    Mauro, S.3
  • 37
    • 79953811147 scopus 로고    scopus 로고
    • The effect of multiple N-methylation on intestinal permeability of cyclic hexapeptides
    • Ovadia O, Greenberg S, Chatterjee J et al. The effect of multiple N-methylation on intestinal permeability of cyclic hexapeptides. Mol. Pharmacol. 8(2), 479-487 (2011).
    • (2011) Mol. Pharmacol. , vol.8 , Issue.2 , pp. 479-487
    • Ovadia, O.1    Greenberg, S.2    Chatterjee, J.3
  • 38
    • 84859788959 scopus 로고    scopus 로고
    • Predicting and improving the membrane permeability of peptidic small molecules
    • Rafi S, Hearn B, Vedantham P, Jacobson M, Renslo A. Predicting and improving the membrane permeability of peptidic small molecules. J. Med. Chem. 55(7), 3163-3169 (2012).
    • (2012) J. Med. Chem. , vol.55 , Issue.7 , pp. 3163-3169
    • Rafi, S.1    Hearn, B.2    Vedantham, P.3    Jacobson, M.4    Renslo, A.5
  • 39
    • 33845309676 scopus 로고    scopus 로고
    • N-methylated cyclic pentaalanine peptides as template structures
    • Chatterjee J, Mierke D, Kessler H. N-methylated cyclic pentaalanine peptides as template structures. J. Am. Chem. Soc. 128(47), 15164-15172 (2006).
    • (2006) J. Am. Chem. Soc. , vol.128 , Issue.47 , pp. 15164-15172
    • Chatterjee, J.1    Mierke, D.2    Kessler, H.3
  • 40
    • 57349171593 scopus 로고    scopus 로고
    • N-methylation of peptides: A new perspective in medicinal chemistry
    • Chatterjee J, Gilon C, Hoffman A, Kessler H. N-methylation of peptides: A new perspective in medicinal chemistry. Acc. Chem. Res. 41(10), 1331-1342 (2008).
    • (2008) Acc. Chem. Res. , vol.41 , Issue.10 , pp. 1331-1342
    • Chatterjee, J.1    Gilon, C.2    Hoffman, A.3    Kessler, H.4
  • 41
    • 84935898517 scopus 로고    scopus 로고
    • Probing the physicochemical boundaries of cell permeability and oral bioavailability in lipophilic macrocycles inspired by natural products
    • Epub ahead of print
    • Bockus AT, Lexa KW, Pye CR et al. Probing the physicochemical boundaries of cell permeability and oral bioavailability in lipophilic macrocycles inspired by natural products. J. Med. Chem. doi:10.1021/acs.jmedchem.5b00128 (2015) (Epub ahead of print).
    • (2015) J. Med. Chem.
    • Bockus, A.T.1    Lexa, K.W.2    Pye, C.R.3
  • 43
    • 0030569509 scopus 로고    scopus 로고
    • Study of structure-activity correlation in destruxins, a class of cyclodepsipeptides possessing suppressive effect on the generation of hepatitis B virus surface antigen in human hepatoma cells
    • Yeh SF, Pan W, Ong G-T et al. Study of structure-activity correlation in destruxins, a class of cyclodepsipeptides possessing suppressive effect on the generation of hepatitis B virus surface antigen in human hepatoma cells. Biochem. Biophys. Res. Commun. 229(1), 65-72 (1996).
    • (1996) Biochem. Biophys. Res. Commun. , vol.229 , Issue.1 , pp. 65-72
    • Yeh, S.F.1    Pan, W.2    Ong, G.-T.3
  • 44
    • 0021923153 scopus 로고
    • Peptide conformations. Part 31. The conformation of cyclosporin a in the crystal and in solution
    • Loosli H-R, Kessler H, Oschkinat H, Weber H-P, Petcher TJ, Widmer A. Peptide conformations. Part 31. The conformation of cyclosporin a in the crystal and in solution. Helv. Chim. Acta 68(3), 682-704 (1985).
    • (1985) Helv. Chim. Acta , vol.68 , Issue.3 , pp. 682-704
    • Loosli, H.-R.1    Kessler, H.2    Oschkinat, H.3    Weber, H.-P.4    Petcher, T.J.5    Widmer, A.6
  • 45
    • 0025366997 scopus 로고
    • Complexation and medium effects on the conformation of cyclosporin A studied by NMR spectroscopy and molecular dynamics calculations
    • Kessler H, Gehrke M, Lautz J, Kock M, Seebach D, Thaler A. Complexation and medium effects on the conformation of cyclosporin A studied by NMR spectroscopy and molecular dynamics calculations. Biochem. Pharmacol. 40(1), 169-173 (1990).
    • (1990) Biochem. Pharmacol. , vol.40 , Issue.1 , pp. 169-173
    • Kessler, H.1    Gehrke, M.2    Lautz, J.3    Kock, M.4    Seebach, D.5    Thaler, A.6
  • 47
    • 1242295214 scopus 로고    scopus 로고
    • Solution conformations of cyclosporins and magnesium-cyclosporin complexes determined by vibrational circular dichroism
    • Bodack LA, Freedman TB, Chowdhry BZ, Nafie LA. Solution conformations of cyclosporins and magnesium-cyclosporin complexes determined by vibrational circular dichroism. Biopolymers 73(2), 163-177 (2004).
    • (2004) Biopolymers , vol.73 , Issue.2 , pp. 163-177
    • Bodack, L.A.1    Freedman, T.B.2    Chowdhry, B.Z.3    Nafie, L.A.4
  • 48
    • 77956509382 scopus 로고    scopus 로고
    • Unambiguous assignment of vibrational spectra of cyclosporins A and H
    • Qu ZW, Zhu H, May V. Unambiguous assignment of vibrational spectra of cyclosporins A and H. J. Phys. Chem. A 114(36), 9768-9773 (2010).
    • (2010) J. Phys. Chem. A , vol.114 , Issue.36 , pp. 9768-9773
    • Qu, Z.W.1    Zhu, H.2    May, V.3
  • 50
    • 0017072249 scopus 로고
    • Cyclosporin A, a peptide metabolite from trichoderma polysporum (Link ex Pers.) Rifai, with a remarkable immunosuppressive activity
    • Ruegger A, Kuhn M, Lichti H et al. [Cyclosporin A, a peptide metabolite from trichoderma polysporum (Link ex Pers.) Rifai, with a remarkable immunosuppressive activity]. Helv. Chim. Acta 59(4), 1075-1092 (1976).
    • (1976) Helv. Chim. Acta , vol.59 , Issue.4 , pp. 1075-1092
    • Ruegger, A.1    Kuhn, M.2    Lichti, H.3
  • 52
    • 84921484823 scopus 로고    scopus 로고
    • Cell-permeable cyclic peptides from synthetic libraries inspired by natural products
    • Hewitt WM, Leung SS, Pye CR et al. Cell-permeable cyclic peptides from synthetic libraries inspired by natural products. J. Am. Chem. Soc. 137(2), 715-721 (2015).
    • (2015) J. Am. Chem. Soc. , vol.137 , Issue.2 , pp. 715-721
    • Hewitt, W.M.1    Leung, S.S.2    Pye, C.R.3
  • 53
    • 84911489309 scopus 로고    scopus 로고
    • Improving on nature: Making a cyclic heptapeptide orally bioavailable
    • Nielsen DS, Hoang HN, Lohman RJ et al. Improving on nature: making a cyclic heptapeptide orally bioavailable. Angew. Chem. Int. Ed. Engl. 53(45), 12059-12063 (2014).
    • (2014) Angew. Chem. Int. Ed. Engl. , vol.53 , Issue.45 , pp. 12059-12063
    • Nielsen, D.S.1    Hoang, H.N.2    Lohman, R.J.3
  • 55
    • 0026031596 scopus 로고
    • Cyclosporine analogues
    • Jeffery JR. Cyclosporine analogues. Clin. Biochem. 24(1), 15-21 (1991).
    • (1991) Clin. Biochem. , vol.24 , Issue.1 , pp. 15-21
    • Jeffery, J.R.1
  • 56
  • 57
    • 22644450415 scopus 로고    scopus 로고
    • Crystal structures of cyclosporin derivatives: O-Acetyl-(4R)-4-(E-2-butyl)-4,Ndimethyl-L-threonyl-cyclosporin A and O-Acetyl-(4R)-4-[E-2-(4-bromobutyl)]-4,N-dimethyl-L-threonyl-cyclosporin A
    • Bohumil K, Alexandr J, Svetlana P et al. Crystal structures of cyclosporin derivatives: O-Acetyl-(4R)-4-(E-2-butyl)-4,Ndimethyl-L-threonyl-cyclosporin A and O-Acetyl-(4R)-4-[E-2-(4-bromobutyl)]-4,N-dimethyl-L-threonyl-cyclosporin A. Collect. Czech. Chem. Commun. 64(1), 89-98 (1999).
    • (1999) Collect. Czech. Chem. Commun. , vol.64 , Issue.1 , pp. 89-98
    • Bohumil, K.1    Alexandr, J.2    Svetlana, P.3
  • 59
    • 84867025688 scopus 로고    scopus 로고
    • Optimizing PK properties of cyclic peptides: The effect of side chain substitutions on permeability and clearance
    • Rand AC, Leung SSF, Eng H et al. Optimizing PK properties of cyclic peptides: The effect of side chain substitutions on permeability and clearance. Med. Chem. Comm. 3(10), 1282-1289 (2012).
    • (2012) Med. Chem. Comm. , vol.3 , Issue.10 , pp. 1282-1289
    • Rand, A.C.1    Leung, S.S.F.2    Eng, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.