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Volumn 11, Issue 12, 2016, Pages 1151-1163

Discovery and optimization of peptide macrocycles

Author keywords

Cyclic peptides; cyclotides; drug design; kalata B1; peptide macrocycles; stapled peptides

Indexed keywords

AMINO ACID; CYCLOPEPTIDE; CYCLOTIDE; DEFENSIN; EPITOPE; MACROCYCLIC COMPOUND; ORBITIDE DERIVATIVE; PEPTIDE DERIVATIVE; PEPTIDE MACROCYCLE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84994607957     PISSN: 17460441     EISSN: 1746045X     Source Type: Journal    
DOI: 10.1080/17460441.2016.1245720     Document Type: Review
Times cited : (68)

References (138)
  • 1
    • 84892163643 scopus 로고    scopus 로고
    • Macrocyclic drugs and clinical candidates: what can medicinal chemists learn from their properties?
    • F.Giordanetto, J.Kihlberg Macrocyclic drugs and clinical candidates:what can medicinal chemists learn from their properties? J Med Chem. 2014;57:278–295. DOI:10.1021/jm400887j
    • (2014) J Med Chem , vol.57 , pp. 278-295
    • Giordanetto, F.1    Kihlberg, J.2
  • 2
    • 0034461768 scopus 로고    scopus 로고
    • Drug-like properties and the causes of poor solubility and poor permeability
    • C.A.Lipinski. Drug-like properties and the causes of poor solubility and poor permeability. J Pharmacol Toxicol Methods. 2000;44:235–249. DOI:10.1016/S1056-8719(00)00107-6• A paper defining five key rules used in medicinal chemistry to guide the development of orally active small-molecule drugs.
    • (2000) J Pharmacol Toxicol Methods , vol.44 , pp. 235-249
    • Lipinski, C.A.1
  • 3
    • 0037030653 scopus 로고    scopus 로고
    • Molecular properties that influence the oral bioavailability of drug candidates
    • D.F.Veber, S.R.Johnson, H.Y.Cheng, et al. Molecular properties that influence the oral bioavailability of drug candidates. J Med Chem. 2002;45:2615–2623. DOI:10.1021/jm020017n• A paper defining the molecular properties that influence oral bioavailability independent of molecule size.
    • (2002) J Med Chem , vol.45 , pp. 2615-2623
    • Veber, D.F.1    Johnson, S.R.2    Cheng, H.Y.3
  • 4
    • 84871394690 scopus 로고    scopus 로고
    • The future of peptide‐based drugs
    • D.J.Craik, D.P.Fairlie, S.Liras, et al. The future of peptide‐based drugs. Chem Biol Drug Des. 2013;81:136–147. DOI:10.1111/cbdd.12055• A review highlighting the challenges and future directions of peptides as drugs.
    • (2013) Chem Biol Drug Des , vol.81 , pp. 136-147
    • Craik, D.J.1    Fairlie, D.P.2    Liras, S.3
  • 5
    • 84896512272 scopus 로고    scopus 로고
    • Disulfide-rich macrocyclic peptides as templates in drug design
    • S.E.Northfield, C.K.Wang, C.I.Schroeder, et al. Disulfide-rich macrocyclic peptides as templates in drug design. Euro J Med Chem. 2014;77:248–257. DOI:10.1016/j.ejmech.2014.03.011
    • (2014) Euro J Med Chem , vol.77 , pp. 248-257
    • Northfield, S.E.1    Wang, C.K.2    Schroeder, C.I.3
  • 6
    • 84934911599 scopus 로고    scopus 로고
    • Macrocyclic α-helical peptide drug discovery
    • London: RSC Drug Discovery Series
    • T.K.Sawyer, V.Guerlavais, K.Darlak, et al. Macrocyclic α-helical peptide drug discovery. In:Levin J, editor. Macrocycles in drug discovery. London:RSC Drug Discovery Series; 2015. p. 339–366.
    • (2015) Macrocycles in drug discovery
    • Sawyer, T.K.1    Guerlavais, V.2    Darlak, K.3
  • 7
    • 84864554104 scopus 로고    scopus 로고
    • Discovering the bacterial circular proteins: bacteriocins, cyanobactins, and pilins
    • M.Montalban-Lopez, M.Sanchez-Hidalgo, R.Cebrian, et al. Discovering the bacterial circular proteins:bacteriocins, cyanobactins, and pilins. J Biol Chem. 2012;287:27007–27013. DOI:10.1074/jbc.R112.354688
    • (2012) J Biol Chem , vol.287 , pp. 27007-27013
    • Montalban-Lopez, M.1    Sanchez-Hidalgo, M.2    Cebrian, R.3
  • 8
    • 84864551115 scopus 로고    scopus 로고
    • Circular proteins from plants and fungi
    • U.Göransson, R.Burman, S.Gunasekera, et al. Circular proteins from plants and fungi. J Biol Chem. 2012;287:27001–27006. DOI:10.1074/jbc.R111.300129
    • (2012) J Biol Chem , vol.287 , pp. 27001-27006
    • Göransson, U.1    Burman, R.2    Gunasekera, S.3
  • 9
    • 84864538873 scopus 로고    scopus 로고
    • θ-Defensins: cyclic peptides with endless potential
    • R.I.Lehrer, A.M.Cole, M.E.Selsted. θ-Defensins:cyclic peptides with endless potential. J Biol Chem. 2012;287:27014–27019. DOI:10.1074/jbc.R112.346098
    • (2012) J Biol Chem , vol.287 , pp. 27014-27019
    • Lehrer, R.I.1    Cole, A.M.2    Selsted, M.E.3
  • 10
    • 84919903118 scopus 로고    scopus 로고
    • Peptide macrocyclization catalyzed by a prolyl oligopeptidase involved in alpha-amanitin biosynthesis
    • H.Luo, S.Y.Hong, R.M.Sgambelluri, et al. Peptide macrocyclization catalyzed by a prolyl oligopeptidase involved in alpha-amanitin biosynthesis. Chem Biol. 2014;21:1610–1617. DOI:10.1016/j.chembiol.2014.10.015
    • (2014) Chem Biol , vol.21 , pp. 1610-1617
    • Luo, H.1    Hong, S.Y.2    Sgambelluri, R.M.3
  • 11
    • 57749113081 scopus 로고    scopus 로고
    • Distribution and evolution of circular miniproteins in flowering plants
    • C.W.Gruber, A.G.Elliott, D.C.Ireland, et al. Distribution and evolution of circular miniproteins in flowering plants. Plant Cell. 2008;20:2471–2483. DOI:10.1105/tpc.108.062331
    • (2008) Plant Cell , vol.20 , pp. 2471-2483
    • Gruber, C.W.1    Elliott, A.G.2    Ireland, D.C.3
  • 12
    • 0003064562 scopus 로고
    • Some molecular properties of kalatapeptide B-1. A uterotonic polypeptide isolated from Oldenlandia affinis DC
    • K.Sletten, L.Gran. Some molecular properties of kalatapeptide B-1. A uterotonic polypeptide isolated from Oldenlandia affinis DC. Medd Nor Farm Selsk. 1973;7:69–82.
    • (1973) Medd Nor Farm Selsk , vol.7 , pp. 69-82
    • Sletten, K.1    Gran, L.2
  • 13
    • 0033579483 scopus 로고    scopus 로고
    • Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif
    • D.J.Craik, N.L.Daly, T.Bond, et al. Plant cyclotides:A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. J Mol Biol. 1999;294:1327–1336. DOI:10.1006/jmbi.1999.3383• The original paper defining the cyclotide family of peptides.
    • (1999) J Mol Biol , vol.294 , pp. 1327-1336
    • Craik, D.J.1    Daly, N.L.2    Bond, T.3
  • 14
    • 38549134937 scopus 로고    scopus 로고
    • CyBase: A database of cyclic protein sequences and structures, with application in protein discovery and engineering
    • C.K.L.Wang, K.Quentin, L.Chiche, et al. CyBase:A database of cyclic protein sequences and structures, with application in protein discovery and engineering. Nucleic Acids Res. 2008;36:D206–210. DOI:10.1093/nar/gkm953
    • (2008) Nucleic Acids Res , vol.36 , pp. D206-D210
    • Wang, C.K.L.1    Quentin, K.2    Chiche, L.3
  • 15
    • 2442715239 scopus 로고    scopus 로고
    • Thermal, chemical, and enzymatic stability of the cyclotide Kalata B1: the importance of the cyclic cystine knot
    • M.L.Colgrave, D.J.Craik. Thermal, chemical, and enzymatic stability of the cyclotide Kalata B1:the importance of the cyclic cystine knot. Biochemistry. 2004;43:5965–5975. DOI:10.1021/bi049711q
    • (2004) Biochemistry , vol.43 , pp. 5965-5975
    • Colgrave, M.L.1    Craik, D.J.2
  • 16
    • 4444331457 scopus 로고    scopus 로고
    • The role of the cyclic peptide backbone in the anti-HIV activity of the cyclotide kalata B1
    • N.L.Daly, K.R.Gustafson, D.J.Craik. The role of the cyclic peptide backbone in the anti-HIV activity of the cyclotide kalata B1. FEBS Lett. 2004;574:69–72. DOI:10.1016/j.febslet.2004.08.007
    • (2004) FEBS Lett , vol.574 , pp. 69-72
    • Daly, N.L.1    Gustafson, K.R.2    Craik, D.J.3
  • 17
    • 0035933743 scopus 로고    scopus 로고
    • Circular proteins in plants: solution structure of a novel macrocyclic trypsin inhibitor from Momordica cochinchinensis
    • M.E.Felizmenio-Quimio, N.L.Daly, D.J.Craik. Circular proteins in plants:solution structure of a novel macrocyclic trypsin inhibitor from Momordica cochinchinensis. J Biol Chem. 2001;276:22875–22882. DOI:10.1074/jbc.M101666200
    • (2001) J Biol Chem , vol.276 , pp. 22875-22882
    • Felizmenio-Quimio, M.E.1    Daly, N.L.2    Craik, D.J.3
  • 18
    • 4444318429 scopus 로고    scopus 로고
    • Squash inhibitors: from structural motifs to macrocyclic knottins
    • L.Chiche, A.Heitz, J.C.Gelly, et al. Squash inhibitors:from structural motifs to macrocyclic knottins. Curr Protein Pept Sci. 2004;5:341–349. DOI:10.2174/1389203043379477
    • (2004) Curr Protein Pept Sci , vol.5 , pp. 341-349
    • Chiche, L.1    Heitz, A.2    Gelly, J.C.3
  • 19
    • 0034002318 scopus 로고    scopus 로고
    • New circulin macrocyclic polypeptides from Chassalia parvifolia
    • K.R.Gustafson, L.K.Walton, R.C.SowderJr., et al. New circulin macrocyclic polypeptides from Chassalia parvifolia. J Nat Prod. 2000;63:176–178. DOI:10.1021/np990432r
    • (2000) J Nat Prod , vol.63 , pp. 176-178
    • Gustafson, K.R.1    Walton, L.K.2    Sowder, R.C.3
  • 20
    • 0033529942 scopus 로고    scopus 로고
    • An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides
    • J.P.Tam, Y.A.Lu, J.L.Yang, et al. An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides. Proc Natl Acad Sci USA. 1999;96:8913–8918. DOI:10.1073/pnas.96.16.8913
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8913-8918
    • Tam, J.P.1    Lu, Y.A.2    Yang, J.L.3
  • 21
    • 33751073415 scopus 로고    scopus 로고
    • A novel suite of cyclotides from Viola odorata: Sequence variation and the implications for structure, function and stability
    • D.C.Ireland, M.L.Colgrave, D.J.Craik. A novel suite of cyclotides from Viola odorata:Sequence variation and the implications for structure, function and stability. Biochem J. 2006;400:1–12. DOI:10.1042/bj20060627
    • (2006) Biochem J , vol.400 , pp. 1-12
    • Ireland, D.C.1    Colgrave, M.L.2    Craik, D.J.3
  • 22
    • 34547511527 scopus 로고    scopus 로고
    • The cyclotide fingerprint in oldenlandia affinis: elucidation of chemically modified, linear and novel macrocyclic peptides
    • M.R.Plan, U.Göransson, R.J.Clark, et al. The cyclotide fingerprint in oldenlandia affinis:elucidation of chemically modified, linear and novel macrocyclic peptides. ChemBioChem. 2007;8:1001–1011. DOI:10.1002/cbic.200700097
    • (2007) ChemBioChem , vol.8 , pp. 1001-1011
    • Plan, M.R.1    Göransson, U.2    Clark, R.J.3
  • 23
    • 43949138210 scopus 로고    scopus 로고
    • Alanine scanning mutagenesis of the prototypic cyclotide reveals a cluster of residues essential for bioactivity
    • S.M.Simonsen, L.Sando, K.J.Rosengren, et al. Alanine scanning mutagenesis of the prototypic cyclotide reveals a cluster of residues essential for bioactivity. J Biol Chem. 2008;283:9805–9813. DOI:10.1074/jbc.M709303200
    • (2008) J Biol Chem , vol.283 , pp. 9805-9813
    • Simonsen, S.M.1    Sando, L.2    Rosengren, K.J.3
  • 25
    • 79955567660 scopus 로고    scopus 로고
    • Anticancer and chemosensitizing abilities of cycloviolacin 02 from Viola odorata and psyle cyclotides from Psychotria leptothyrsa
    • S.L.Gerlach, R.Rathinakumar, G.Chakravarty, et al. Anticancer and chemosensitizing abilities of cycloviolacin 02 from Viola odorata and psyle cyclotides from Psychotria leptothyrsa. Biopolymers. 2010;94:617–625. DOI:10.1002/bip.21435
    • (2010) Biopolymers , vol.94 , pp. 617-625
    • Gerlach, S.L.1    Rathinakumar, R.2    Chakravarty, G.3
  • 26
    • 0035845584 scopus 로고    scopus 로고
    • Biosynthesis and insecticidal properties of plant cyclotides: the cyclic knotted proteins from Oldenlandia affinis
    • C.Jennings, J.West, C.Waine, et al. Biosynthesis and insecticidal properties of plant cyclotides:the cyclic knotted proteins from Oldenlandia affinis. Proc Natl Acad Sci USA. 2001;98:10614–10619. DOI:10.1073/pnas.191366898
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10614-10619
    • Jennings, C.1    West, J.2    Waine, C.3
  • 27
    • 54349090107 scopus 로고    scopus 로고
    • The anthelmintic activity of the cyclotides: natural variants with enhanced activity
    • M.L.Colgrave, A.C.Kotze, D.C.Ireland, et al. The anthelmintic activity of the cyclotides:natural variants with enhanced activity. ChemBioChem. 2008;9:1939–1945. DOI:10.1002/cbic.200800174
    • (2008) ChemBioChem , vol.9 , pp. 1939-1945
    • Colgrave, M.L.1    Kotze, A.C.2    Ireland, D.C.3
  • 28
    • 47849105966 scopus 로고    scopus 로고
    • Backbone cyclised peptides from plants show molluscicidal activity against the rice pest Pomacea canaliculata (golden apple snail)
    • M.R.Plan, I.Saska, A.G.Cagauan, et al. Backbone cyclised peptides from plants show molluscicidal activity against the rice pest Pomacea canaliculata (golden apple snail). J Agric Food Chem. 2008;56:5237–5241. DOI:10.1021/jf800302f
    • (2008) J Agric Food Chem , vol.56 , pp. 5237-5241
    • Plan, M.R.1    Saska, I.2    Cagauan, A.G.3
  • 29
    • 39549108482 scopus 로고    scopus 로고
    • Plant cyclotides disrupt epithelial cells in the midgut of lepidopteran larvae
    • B.L.Barbeta, A.T.Marshall, A.D.Gillon, et al. Plant cyclotides disrupt epithelial cells in the midgut of lepidopteran larvae. Proc Natl Acad Sci USA. 2008;105:1221–1225. DOI:10.1073/pnas.0710338104
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 1221-1225
    • Barbeta, B.L.1    Marshall, A.T.2    Gillon, A.D.3
  • 30
    • 0037458652 scopus 로고    scopus 로고
    • Disulfide folding pathways of cystine knot proteins. Tying the knot within the circular backbone of the cyclotides
    • N.L.Daly, R.J.Clark, D.J.Craik. Disulfide folding pathways of cystine knot proteins. Tying the knot within the circular backbone of the cyclotides. J Biol Chem. 2003;278:6314–6322. DOI:10.1074/jbc.M210492200
    • (2003) J Biol Chem , vol.278 , pp. 6314-6322
    • Daly, N.L.1    Clark, R.J.2    Craik, D.J.3
  • 31
    • 0346220263 scopus 로고    scopus 로고
    • Disulfide mapping of the cyclotide kalata B1. Chemical proof of the cystic cystine knot motif
    • U.Göransson, D.J.Craik. Disulfide mapping of the cyclotide kalata B1. Chemical proof of the cystic cystine knot motif. J Biol Chem. 2003;278:48188–48196. DOI:10.1074/jbc.M308771200
    • (2003) J Biol Chem , vol.278 , pp. 48188-48196
    • Göransson, U.1    Craik, D.J.2
  • 32
    • 84903184066 scopus 로고    scopus 로고
    • Fmoc-based synthesis of disulfide-rich cyclic peptides
    • O.Cheneval, C.I.Schroeder, T.Durek, et al. Fmoc-based synthesis of disulfide-rich cyclic peptides. J Org Chem. 2014;79:5538–5544. DOI:10.1021/jo500699m•• A paper outlining a protocol for the efficient synthesis of disulfide rich cyclic peptides.
    • (2014) J Org Chem , vol.79 , pp. 5538-5544
    • Cheneval, O.1    Schroeder, C.I.2    Durek, T.3
  • 33
    • 32944465547 scopus 로고    scopus 로고
    • Structural plasticity of the cyclic-cystine-knot framework: implications for biological activity and drug design
    • R.J.Clark, N.L.Daly, D.J.Craik. Structural plasticity of the cyclic-cystine-knot framework:implications for biological activity and drug design. Biochem J. 2006;394:85–93. DOI:10.1042/BJ20051691
    • (2006) Biochem J , vol.394 , pp. 85-93
    • Clark, R.J.1    Daly, N.L.2    Craik, D.J.3
  • 34
    • 84881250938 scopus 로고    scopus 로고
    • In vivo activation of the p53 tumor suppressor pathway by an engineered cyclotide
    • Y.Ji, S.Majumder, M.Millard, et al. In vivo activation of the p53 tumor suppressor pathway by an engineered cyclotide. J Am Chem Soc. 2013;135:11623–11633. DOI:10.1021/ja405108p•• A paper reporting the development of a stable engineered cyclotide that antagonizes the intracellular p53 tumor suppressor pathway with nanomolar affinity, both in vitro and in vivo.
    • (2013) J Am Chem Soc , vol.135 , pp. 11623-11633
    • Ji, Y.1    Majumder, S.2    Millard, M.3
  • 35
    • 84955499376 scopus 로고    scopus 로고
    • Using the MCoTI-II cyclotide scaffold to design a stable cyclic peptide antagonist of SET, a protein overexpressed in human cancer
    • C.D’Souza, S.T.Henriques, C.K.Wang, et al. Using the MCoTI-II cyclotide scaffold to design a stable cyclic peptide antagonist of SET, a protein overexpressed in human cancer. Biochemistry. 2016;55:396–405. DOI:10.1021/acs.biochem.5b00529
    • (2016) Biochemistry , vol.55 , pp. 396-405
    • D’Souza, C.1    Henriques, S.T.2    Wang, C.K.3
  • 36
    • 84896538363 scopus 로고    scopus 로고
    • Molecular grafting onto a stable framework yields novel cyclic peptides for the treatment of multiple sclerosis
    • C.K.Wang, C.W.Gruber, M.Cemazar, et al. Molecular grafting onto a stable framework yields novel cyclic peptides for the treatment of multiple sclerosis. ACS Chem Biol. 2014;9:156–163. DOI:10.1021/cb400548s• A paper describing the stabilization of a myelin oligodendrocyte glycoprotein epitope grafted into a cyclotide and the subsequent inhibition of multiple sclerosis in mice.
    • (2014) ACS Chem Biol , vol.9 , pp. 156-163
    • Wang, C.K.1    Gruber, C.W.2    Cemazar, M.3
  • 37
    • 84861615565 scopus 로고    scopus 로고
    • Orally active peptidic bradykinin B1 receptor antagonists engineered from a cyclotide scaffold for inflammatory pain treatment
    • C.T.T.Wong, D.K.Rowlands, C.H.Wong, et al. Orally active peptidic bradykinin B1 receptor antagonists engineered from a cyclotide scaffold for inflammatory pain treatment. Angew Chem Int Ed. 2012;51:5620–5624. DOI:10.1002/anie.201200984
    • (2012) Angew Chem Int Ed , vol.51 , pp. 5620-5624
    • Wong, C.T.T.1    Rowlands, D.K.2    Wong, C.H.3
  • 38
    • 84939213771 scopus 로고    scopus 로고
    • Design of substrate-based BCR-ABL kinase inhibitors using the cyclotide scaffold
    • Y.H.Huang, S.T.Henriques, C.K.Wang, et al. Design of substrate-based BCR-ABL kinase inhibitors using the cyclotide scaffold. Sci Rep. 2015;5:12974. DOI:10.1038/srep12974• A paper reporting the design of an engineered cyclotide with inhibitory activity of BCR-ABL tyrosine kinase for the treatment of chronic myeloid leukemia.
    • (2015) Sci Rep , vol.5 , pp. 12974
    • Huang, Y.H.1    Henriques, S.T.2    Wang, C.K.3
  • 39
    • 84963668266 scopus 로고    scopus 로고
    • Design of a MCoTI-based cyclotide with angiotensin (1-7)-like activity
    • T.Aboye, C.J.Meeks, S.Majumder, et al. Design of a MCoTI-based cyclotide with angiotensin (1-7)-like activity. Molecules. 2016;21. DOI:10.3390/molecules21020152
    • (2016) Molecules , vol.21
    • Aboye, T.1    Meeks, C.J.2    Majumder, S.3
  • 40
    • 84870003472 scopus 로고    scopus 로고
    • Design, synthesis, structural and functional characterization of novel melanocortin agonists based on the cyclotide kalata B1
    • R.Eliasen, N.L.Daly, B.S.Wulff, et al. Design, synthesis, structural and functional characterization of novel melanocortin agonists based on the cyclotide kalata B1. J Biol Chem. 2012;287:40493–40501. DOI:10.1074/jbc.M112.395442
    • (2012) J Biol Chem , vol.287 , pp. 40493-40501
    • Eliasen, R.1    Daly, N.L.2    Wulff, B.S.3
  • 41
    • 84055177578 scopus 로고    scopus 로고
    • Engineering pro-angiogenic peptides using stable, disulfide-rich cyclic scaffolds
    • L.Y.Chan, S.Gunasekera, S.T.Henriques, et al. Engineering pro-angiogenic peptides using stable, disulfide-rich cyclic scaffolds. Blood. 2011;118:6709–6717. DOI:10.1182/blood-2011-06-359141
    • (2011) Blood , vol.118 , pp. 6709-6717
    • Chan, L.Y.1    Gunasekera, S.2    Henriques, S.T.3
  • 42
    • 84963553258 scopus 로고    scopus 로고
    • Oral activity of a nature-derived cyclic peptide for the treatment of multiple sclerosis
    • K.Thell, R.Hellinger, E.Sahin, et al. Oral activity of a nature-derived cyclic peptide for the treatment of multiple sclerosis. Proc Natl Acad Sci USA. 2016;113:3960–3965. DOI:10.1073/pnas.1519960113•• A study demonstrating the oral activity of an engineered cyclotide that silences T cell proliferation as an immunosuppressive molecule for the treatment of multiple sclerosis.
    • (2016) Proc Natl Acad Sci USA , vol.113 , pp. 3960-3965
    • Thell, K.1    Hellinger, R.2    Sahin, E.3
  • 43
    • 34748922922 scopus 로고    scopus 로고
    • The cyclic cystine knot miniprotein MCoTI-II is internalized into cells by macropinocytosis
    • K.P.Greenwood, N.L.Daly, D.L.Brown, et al. The cyclic cystine knot miniprotein MCoTI-II is internalized into cells by macropinocytosis. Int J Biochem Cell Biol. 2007;39:2252–2264. DOI:10.1016/j.biocel.2007.06.016
    • (2007) Int J Biochem Cell Biol , vol.39 , pp. 2252-2264
    • Greenwood, K.P.1    Daly, N.L.2    Brown, D.L.3
  • 44
    • 80054689774 scopus 로고    scopus 로고
    • Identification and characterization of a new family of cell-penetrating peptides: cyclic cell-penetrating peptides
    • L.Cascales, S.T.Henriques, M.C.Kerr, et al. Identification and characterization of a new family of cell-penetrating peptides:cyclic cell-penetrating peptides. J Biol Chem. 2011;286:36932–36943. DOI:10.1074/jbc.M111.264424
    • (2011) J Biol Chem , vol.286 , pp. 36932-36943
    • Cascales, L.1    Henriques, S.T.2    Kerr, M.C.3
  • 45
    • 80054094292 scopus 로고    scopus 로고
    • Cellular uptake of cyclotide MCoTI-I follows multiple endocytic pathways
    • J.Contreras, A.Y.O.Elnagar, S.F.Hamm-Alvarez, et al. Cellular uptake of cyclotide MCoTI-I follows multiple endocytic pathways. J Control Release. 2011;155:134–143. DOI:10.1016/j.jconrel.2011.08.030
    • (2011) J Control Release , vol.155 , pp. 134-143
    • Contreras, J.1    Elnagar, A.Y.O.2    Hamm-Alvarez, S.F.3
  • 46
    • 84939618893 scopus 로고    scopus 로고
    • The prototypic cyclotide Kalata B1 has a unique mechanism of entering cells
    • S.T.Henriques, Y.H.Huang, S.Chaousis, et al. The prototypic cyclotide Kalata B1 has a unique mechanism of entering cells. Chem Biol. 2015;22:1087–2097. DOI:10.1016/j.chembiol.2015.07.012• A paper describing the mechanism of cellular penetration of the cyclotide kalata B1.
    • (2015) Chem Biol , vol.22 , pp. 1087-2097
    • Henriques, S.T.1    Huang, Y.H.2    Chaousis, S.3
  • 47
    • 84911496240 scopus 로고    scopus 로고
    • Structural parameters modulating the cellular uptake of disulfide-rich cyclic cell-penetrating peptides: MCoTI-II and SFTI-1
    • C.D’Souza, S.T.Henriques, C.K.Wang, et al. Structural parameters modulating the cellular uptake of disulfide-rich cyclic cell-penetrating peptides:MCoTI-II and SFTI-1. Euro J Med Chem. 2014;88:10–18. DOI:10.1016/j.ejmech.2014.06.047
    • (2014) Euro J Med Chem , vol.88 , pp. 10-18
    • D’Souza, C.1    Henriques, S.T.2    Wang, C.K.3
  • 48
    • 84906318100 scopus 로고    scopus 로고
    • Butelase 1 is an Asx-specific ligase enabling peptide macrocyclization and synthesis
    • G.K.T.Nguyen, S.Wang, Y.Qiu, et al. Butelase 1 is an Asx-specific ligase enabling peptide macrocyclization and synthesis. Nat Chem Biol. 2014;10:732–738. DOI:10.1038/nchembio.1586
    • (2014) Nat Chem Biol , vol.10 , pp. 732-738
    • Nguyen, G.K.T.1    Wang, S.2    Qiu, Y.3
  • 49
    • 84951824827 scopus 로고    scopus 로고
    • Efficient backbone cyclization of linear peptides by a recombinant asparaginyl endopeptidase
    • K.S.Harris, T.Durek, Q.Kaas, et al. Efficient backbone cyclization of linear peptides by a recombinant asparaginyl endopeptidase. Nat Commun. 2015;6. DOI:10.1038/ncomms10199
    • (2015) Nat Commun , vol.6
    • Harris, K.S.1    Durek, T.2    Kaas, Q.3
  • 50
    • 0033569410 scopus 로고    scopus 로고
    • A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins
    • Y.Q.Tang, J.Yuan, G.Osapay, et al. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins. Science. 1999;286:498–502. DOI:10.1126/science.286.5439.498
    • (1999) Science , vol.286 , pp. 498-502
    • Tang, Y.Q.1    Yuan, J.2    Osapay, G.3
  • 51
    • 84870524827 scopus 로고    scopus 로고
    • Structural characterization of the cyclic cystine ladder motif of θ-defensins
    • A.C.Conibear, K.J.Rosengren, P.J.Harvey, et al. Structural characterization of the cyclic cystine ladder motif of θ-defensins. Biochemistry. 2012;51:9718–97126. DOI:10.1021/bi301363a
    • (2012) Biochemistry , vol.51 , pp. 9718-97126
    • Conibear, A.C.1    Rosengren, K.J.2    Harvey, P.J.3
  • 52
    • 84876206211 scopus 로고    scopus 로고
    • The cyclic cystine ladder in theta-defensins is important for structure and stability, but not antibacterial activity
    • A.C.Conibear, K.J.Rosengren, N.L.Daly, et al. The cyclic cystine ladder in theta-defensins is important for structure and stability, but not antibacterial activity. J Biol Chem. 2013;288:10830–10840. DOI:10.1074/jbc.M113.451047
    • (2013) J Biol Chem , vol.288 , pp. 10830-10840
    • Conibear, A.C.1    Rosengren, K.J.2    Daly, N.L.3
  • 53
    • 84928880850 scopus 로고    scopus 로고
    • The chemistry and biology of theta defensins
    • A.C.Conibear, D.J.Craik. The chemistry and biology of theta defensins. Angew Chem Int Ed Engl. 2014;53:10612–10623. DOI:10.1002/anie.201402167
    • (2014) Angew Chem Int Ed Engl , vol.53 , pp. 10612-10623
    • Conibear, A.C.1    Craik, D.J.2
  • 54
    • 79951818701 scopus 로고    scopus 로고
    • Rhesus macaque theta-defensin isoforms: expression, antimicrobial activities, and demonstration of a prominent role in neutrophil granule microbicidal activities
    • P.Tongaonkar, P.Tran, K.Roberts, et al. Rhesus macaque theta-defensin isoforms:expression, antimicrobial activities, and demonstration of a prominent role in neutrophil granule microbicidal activities. J Leukoc Biol. 2011;89:283–290. DOI:10.1189/jlb.0910535
    • (2011) J Leukoc Biol , vol.89 , pp. 283-290
    • Tongaonkar, P.1    Tran, P.2    Roberts, K.3
  • 55
    • 84870829224 scopus 로고    scopus 로고
    • Rhesus macaque theta defensins suppress inflammatory cytokines and enhance survival in mouse models of bacteremic sepsis
    • J.B.Schaal, D.Tran, P.Tran, et al. Rhesus macaque theta defensins suppress inflammatory cytokines and enhance survival in mouse models of bacteremic sepsis. PLoS One. 2012;7:e51337. DOI:10.1371/journal.pone.0051337
    • (2012) PLoS One , vol.7 , pp. e51337
    • Schaal, J.B.1    Tran, D.2    Tran, P.3
  • 56
    • 85006123495 scopus 로고    scopus 로고
    • Killing of staphylococci by θ-defensins involves membrane impairment and activation of autolytic enzymes
    • M.Wilmes, M.Stockem, G.Bierbaum, et al. Killing of staphylococci by θ-defensins involves membrane impairment and activation of autolytic enzymes. Antibiotics. 2014;3:617–631. DOI:10.3390/antibiotics3040617
    • (2014) Antibiotics , vol.3 , pp. 617-631
    • Wilmes, M.1    Stockem, M.2    Bierbaum, G.3
  • 57
    • 84948985602 scopus 로고    scopus 로고
    • Rhesus macaque theta-defensin RTD-1 inhibits proinflammatory cytokine secretion and gene expression by inhibiting the activation of NF-kappaB and MAPK pathways
    • P.Tongaonkar, K.K.Trinh, J.B.Schaal, et al. Rhesus macaque theta-defensin RTD-1 inhibits proinflammatory cytokine secretion and gene expression by inhibiting the activation of NF-kappaB and MAPK pathways. J Leukoc Biol. 2015;98:1061–1070. DOI:10.1189/jlb.3A0315-102R
    • (2015) J Leukoc Biol , vol.98 , pp. 1061-1070
    • Tongaonkar, P.1    Trinh, K.K.2    Schaal, J.B.3
  • 58
    • 70350278897 scopus 로고    scopus 로고
    • Rhesus theta-defensin prevents death in a mouse model of severe acute respiratory syndrome coronavirus pulmonary disease
    • C.L.Wohlford-Lenane, D.K.Meyerholz, S.Perlman, et al. Rhesus theta-defensin prevents death in a mouse model of severe acute respiratory syndrome coronavirus pulmonary disease. J Virol. 2009;83:11385–11390. DOI:10.1128/jvi.01363-09
    • (2009) J Virol , vol.83 , pp. 11385-11390
    • Wohlford-Lenane, C.L.1    Meyerholz, D.K.2    Perlman, S.3
  • 59
    • 84937622392 scopus 로고    scopus 로고
    • theta-Defensin RTD-1 improves insulin action and normalizes plasma glucose and FFA levels in diet-induced obese rats
    • Y.T.Oh, D.Tran, T.A.Buchanan, et al. theta-Defensin RTD-1 improves insulin action and normalizes plasma glucose and FFA levels in diet-induced obese rats. Am J Physiol Endocrinol Metab. 2015;309:e154–160. DOI:10.1152/ajpendo.00131.2015
    • (2015) Am J Physiol Endocrinol Metab , vol.309 , pp. e154-e160
    • Oh, Y.T.1    Tran, D.2    Buchanan, T.A.3
  • 60
    • 0037133343 scopus 로고    scopus 로고
    • Retrocyclin: A primate peptide that protects cells from infection by T- and M-tropic strains of HIV-1
    • A.M.Cole, T.Hong, L.M.Boo, et al. Retrocyclin:A primate peptide that protects cells from infection by T- and M-tropic strains of HIV-1. Proc Natl Acad Sci USA. 2002;99:1813–1818. DOI:10.1073/pnas.052706399
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1813-1818
    • Cole, A.M.1    Hong, T.2    Boo, L.M.3
  • 61
    • 10244279291 scopus 로고    scopus 로고
    • Theta-defensin pseudogenes in HIV-1-exposed, persistently seronegative female sex-workers from Thailand
    • C.Yang, L.Boone, T.X.Nguyen, et al. Theta-defensin pseudogenes in HIV-1-exposed, persistently seronegative female sex-workers from Thailand. Infect Genet Evol. 2005;5:11–15. DOI:10.1016/j.meegid.2004.05.006
    • (2005) Infect Genet Evol , vol.5 , pp. 11-15
    • Yang, C.1    Boone, L.2    Nguyen, T.X.3
  • 62
    • 84895074402 scopus 로고    scopus 로고
    • The cyclic cystine ladder of theta-defensins as a stable, bifunctional scaffold: a proof-of-concept study using the integrin-binding RGD motif
    • A.C.Conibear, A.Bochen, K.J.Rosengren, et al. The cyclic cystine ladder of theta-defensins as a stable, bifunctional scaffold:a proof-of-concept study using the integrin-binding RGD motif. ChemBioChem. 2014;15:451–459. DOI:10.1002/cbic.201300568• The first paper demonstrating the use of θ-defensins as a stable scaffold for the grafting of bioactive epitopes.
    • (2014) ChemBioChem , vol.15 , pp. 451-459
    • Conibear, A.C.1    Bochen, A.2    Rosengren, K.J.3
  • 63
    • 84871019068 scopus 로고    scopus 로고
    • Design of a novel cyclotide-based CXCR4 antagonist with anti-Human Immunodeficiency Virus (HIV)-1 activity
    • T.L.Aboye, H.Ha, S.Majumder, et al. Design of a novel cyclotide-based CXCR4 antagonist with anti-Human Immunodeficiency Virus (HIV)-1 activity. J Med Chem. 2012;55:10729–10734. DOI:10.1021/jm301468k
    • (2012) J Med Chem , vol.55 , pp. 10729-10734
    • Aboye, T.L.1    Ha, H.2    Majumder, S.3
  • 64
    • 84961316062 scopus 로고    scopus 로고
    • Approaches to the stabilization of bioactive epitopes by grafting and peptide cyclization
    • A.C.Conibear, S.Chaousis, T.Durek, et al. Approaches to the stabilization of bioactive epitopes by grafting and peptide cyclization. Biopolymers. 2016;106:89–100. DOI:10.1002/bip.22767
    • (2016) Biopolymers , vol.106 , pp. 89-100
    • Conibear, A.C.1    Chaousis, S.2    Durek, T.3
  • 65
    • 0344655676 scopus 로고    scopus 로고
    • High-resolution structure of a potent, cyclic proteinase inhibitor from sunflower seeds
    • S.Luckett, R.S.Garcia, J.J.Barker, et al. High-resolution structure of a potent, cyclic proteinase inhibitor from sunflower seeds. J Mol Biol. 1999;290:525–533. DOI:10.1006/jmbi.1999.2891
    • (1999) J Mol Biol , vol.290 , pp. 525-533
    • Luckett, S.1    Garcia, R.S.2    Barker, J.J.3
  • 66
    • 84899144819 scopus 로고    scopus 로고
    • Evolutionary origins of a bioactive peptide buried within preproalbumin
    • A.G.Elliott, C.Delay, H.Liu, et al. Evolutionary origins of a bioactive peptide buried within preproalbumin. Plant Cell. 2014;26:981–995. DOI:10.1105/tpc.114.123620
    • (2014) Plant Cell , vol.26 , pp. 981-995
    • Elliott, A.G.1    Delay, C.2    Liu, H.3
  • 67
    • 23844454955 scopus 로고    scopus 로고
    • Structural features and molecular evolution of bowman-birk protease inhibitors and their potential application
    • R.F.Qi, Z.W.Song, C.W.Chi. Structural features and molecular evolution of bowman-birk protease inhibitors and their potential application. Acta Biochim Biophys Sinica. 2005;37:283–292. DOI:10.1111/j.1745-7270.2005.00048.x
    • (2005) Acta Biochim Biophys Sinica , vol.37 , pp. 283-292
    • Qi, R.F.1    Song, Z.W.2    Chi, C.W.3
  • 68
    • 13444270416 scopus 로고    scopus 로고
    • Disulfide bond mutagenesis and the structure and function of the head-to-tail macrocyclic trypsin inhibitor SFTI-1
    • M.L.Korsinczky, R.J.Clark, D.J.Craik. Disulfide bond mutagenesis and the structure and function of the head-to-tail macrocyclic trypsin inhibitor SFTI-1. Biochemistry. 2005;44:1145–1153. DOI:10.1021/bi048297r
    • (2005) Biochemistry , vol.44 , pp. 1145-1153
    • Korsinczky, M.L.1    Clark, R.J.2    Craik, D.J.3
  • 69
    • 84857547296 scopus 로고    scopus 로고
    • Cyclotides as a basis for drug design
    • D.J.Craik, J.E.Swedberg, J.S.Mylne, et al. Cyclotides as a basis for drug design. Exp Opin Drug Disc. 2012;7:179–194. DOI:10.1517/17460441.2012.661554
    • (2012) Exp Opin Drug Disc , vol.7 , pp. 179-194
    • Craik, D.J.1    Swedberg, J.E.2    Mylne, J.S.3
  • 70
    • 84956889439 scopus 로고    scopus 로고
    • Cyclic thrombospondin-1 mimetics: grafting of a thrombospondin sequence into circular disulfide-rich frameworks to inhibit endothelial cell migration
    • L.Y.Chan, D.J.Craik, N.L.Daly. Cyclic thrombospondin-1 mimetics:grafting of a thrombospondin sequence into circular disulfide-rich frameworks to inhibit endothelial cell migration. Biosci Rep. 2015;35. DOI:10.1042/bsr20150210
    • (2015) Biosci Rep , vol.35
    • Chan, L.Y.1    Craik, D.J.2    Daly, N.L.3
  • 71
    • 84955289216 scopus 로고    scopus 로고
    • Inhibition of tau aggregation using a naturally-occurring cyclic peptide scaffold
    • C.K.Wang, S.E.Northfield, Y.H.Huang, et al. Inhibition of tau aggregation using a naturally-occurring cyclic peptide scaffold. Euro J Med Chem. 2016;109:342–349. DOI:10.1016/j.ejmech.2016.01.006
    • (2016) Euro J Med Chem , vol.109 , pp. 342-349
    • Wang, C.K.1    Northfield, S.E.2    Huang, Y.H.3
  • 72
    • 84937113459 scopus 로고    scopus 로고
    • Engineered protease inhibitors based on sunflower trypsin inhibitor-1 (SFTI-1) provide insights into the role of sequence and conformation in Laskowski mechanism inhibition
    • S.J.De Veer, J.E.Swedberg, M.Akcan, et al. Engineered protease inhibitors based on sunflower trypsin inhibitor-1 (SFTI-1) provide insights into the role of sequence and conformation in Laskowski mechanism inhibition. Biochem J. 2015;469:243–253. DOI:10.1042/bj20150412
    • (2015) Biochem J , vol.469 , pp. 243-253
    • De Veer, S.J.1    Swedberg, J.E.2    Akcan, M.3
  • 73
    • 84954367268 scopus 로고    scopus 로고
    • Engineering a constrained peptidic scaffold towards potent and selective furin inhibitors
    • H.Fittler, A.Depp, O.Avrutina, et al. Engineering a constrained peptidic scaffold towards potent and selective furin inhibitors. ChemBioChem. 2015;16:2441–2444. DOI:10.1002/cbic.201500447
    • (2015) ChemBioChem , vol.16 , pp. 2441-2444
    • Fittler, H.1    Depp, A.2    Avrutina, O.3
  • 74
    • 84952674008 scopus 로고    scopus 로고
    • Inhibition of kallikrein-related peptidases 7 and 5 by grafting serpin reactive-center loop sequences onto sunflower trypsin inhibitor-1 (SFTI-1)
    • C.Jendrny, A.G.Beck-Sickinger. Inhibition of kallikrein-related peptidases 7 and 5 by grafting serpin reactive-center loop sequences onto sunflower trypsin inhibitor-1 (SFTI-1). ChemBioChem. 2015;17:719–726. DOI:10.1002/cbic.201500539
    • (2015) ChemBioChem , vol.17 , pp. 719-726
    • Jendrny, C.1    Beck-Sickinger, A.G.2
  • 75
    • 67649547851 scopus 로고    scopus 로고
    • Substrate-guided design of a potent and selective kallikrein-related peptidase inhibitor for kallikrein 4
    • J.E.Swedberg, L.V.Nigon, J.C.Reid, et al. Substrate-guided design of a potent and selective kallikrein-related peptidase inhibitor for kallikrein 4. Chem Biol. 2009;16:633–643. DOI:10.1016/j.chembiol.2009.05.008
    • (2009) Chem Biol , vol.16 , pp. 633-643
    • Swedberg, J.E.1    Nigon, L.V.2    Reid, J.C.3
  • 76
    • 84937834232 scopus 로고    scopus 로고
    • Evaluating the cytotoxicity of flaxseed orbitides for potential cancer treatment
    • D.P.Okinyo-Owiti, Q.Dong, B.Ling, et al. Evaluating the cytotoxicity of flaxseed orbitides for potential cancer treatment. Toxicol Rep. 2015;2:1014–1018. DOI:10.1016/j.toxrep.2015.06.011
    • (2015) Toxicol Rep , vol.2 , pp. 1014-1018
    • Okinyo-Owiti, D.P.1    Dong, Q.2    Ling, B.3
  • 77
    • 0030775874 scopus 로고    scopus 로고
    • Cyclolinopeptide A (CLA) mediates its immunosuppressive activity through cyclophilin-dependent calcineurin inactivation
    • T.J.Gaymes, M.Cebrat, I.Z.Siemion, et al. Cyclolinopeptide A (CLA) mediates its immunosuppressive activity through cyclophilin-dependent calcineurin inactivation. FEBS Letters. 1997;418:224–227. DOI:10.1016/S0014-5793(97)01345-8
    • (1997) FEBS Letters , vol.418 , pp. 224-227
    • Gaymes, T.J.1    Cebrat, M.2    Siemion, I.Z.3
  • 78
    • 80052943523 scopus 로고    scopus 로고
    • Cyclolinopeptide derivatives modify methotrexate-induced suppression of the humoral immune response in mice
    • J.Katarzyńska, A.Mazur, E.Rudzińska, et al. Cyclolinopeptide derivatives modify methotrexate-induced suppression of the humoral immune response in mice. Euro J Med Chem. 2011;46:4608–4617. DOI:10.1016/j.ejmech.2011.07.040
    • (2011) Euro J Med Chem , vol.46 , pp. 4608-4617
    • Katarzyńska, J.1    Mazur, A.2    Rudzińska, E.3
  • 79
    • 0033598747 scopus 로고    scopus 로고
    • Production of cyclic peptides and proteins in vivo
    • C.P.Scott, E.Abel-Santos, M.Wall, et al. Production of cyclic peptides and proteins in vivo. Proc Natl Acad Sci USA. 1999;96:13638–13643. DOI:10.1073/pnas.96.24.13638
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13638-13643
    • Scott, C.P.1    Abel-Santos, E.2    Wall, M.3
  • 80
    • 84876512939 scopus 로고    scopus 로고
    • Emerging strategies to access peptide macrocycles from genetically encoded polypeptides
    • J.M.Smith, J.R.Frost, R.Fasan. Emerging strategies to access peptide macrocycles from genetically encoded polypeptides. J Org Chem. 2013;78:3525–3531. DOI:10.1021/jo400119s
    • (2013) J Org Chem , vol.78 , pp. 3525-3531
    • Smith, J.M.1    Frost, J.R.2    Fasan, R.3
  • 81
    • 84902176344 scopus 로고    scopus 로고
    • Selection-based discovery of druglike macrocyclic peptides
    • T.Passioura, T.Katoh, Y.Goto, et al. Selection-based discovery of druglike macrocyclic peptides. Annu Rev Biochem. 2014;83:727–752. DOI:10.1146/annurev-biochem-060713-035456
    • (2014) Annu Rev Biochem , vol.83 , pp. 727-752
    • Passioura, T.1    Katoh, T.2    Goto, Y.3
  • 82
    • 84906060855 scopus 로고    scopus 로고
    • Peptides come round: using SICLOPPS libraries for early stage drug discovery
    • K.R.Lennard, A.Tavassoli. Peptides come round:using SICLOPPS libraries for early stage drug discovery. Chemistry. 2014;20:10608–10614. DOI:10.1002/chem.201403117
    • (2014) Chemistry , vol.20 , pp. 10608-10614
    • Lennard, K.R.1    Tavassoli, A.2
  • 83
    • 25444448796 scopus 로고    scopus 로고
    • Engineering stable peptide toxins by means of backbone cyclization: stabilization of the alpha-conotoxin MII
    • R.J.Clark, H.Fischer, L.Dempster, et al. Engineering stable peptide toxins by means of backbone cyclization:stabilization of the alpha-conotoxin MII. Proc Natl Acad Sci USA. 2005;102:13767–13772. DOI:10.1073/pnas.0504613102
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13767-13772
    • Clark, R.J.1    Fischer, H.2    Dempster, L.3
  • 84
    • 77956502216 scopus 로고    scopus 로고
    • The engineering of an orally active conotoxin for the treatment of neuropathic pain
    • R.J.Clark, J.Jensen, S.T.Nevin, et al. The engineering of an orally active conotoxin for the treatment of neuropathic pain. Angew Chem Int Ed. 2010;49:6545–6548. DOI:10.1002/anie.201000620
    • (2010) Angew Chem Int Ed , vol.49 , pp. 6545-6548
    • Clark, R.J.1    Jensen, J.2    Nevin, S.T.3
  • 86
    • 77953010796 scopus 로고    scopus 로고
    • Establishing regiocontrol of disulfide bond isomers of alpha-conotoxin ImI via the synthesis of N-to-C cyclic analogs
    • C.J.Armishaw, J.L.Dutton, D.J.Craik, et al. Establishing regiocontrol of disulfide bond isomers of alpha-conotoxin ImI via the synthesis of N-to-C cyclic analogs. Biopolymers. 2010;94:307–313. DOI:10.1002/bip.21360
    • (2010) Biopolymers , vol.94 , pp. 307-313
    • Armishaw, C.J.1    Dutton, J.L.2    Craik, D.J.3
  • 87
    • 78649461899 scopus 로고    scopus 로고
    • Improving the stability of alpha-conotoxin AuIB through N-to-C cyclization: the effect of linker length on stability and activity at nicotinic acetylcholine receptors
    • C.J.Armishaw, A.A.Jensen, L.D.Balle, et al. Improving the stability of alpha-conotoxin AuIB through N-to-C cyclization:the effect of linker length on stability and activity at nicotinic acetylcholine receptors. Antioxid Redox Signal. 2011;14:65–76. DOI:10.1089/ars.2010.3458
    • (2011) Antioxid Redox Signal , vol.14 , pp. 65-76
    • Armishaw, C.J.1    Jensen, A.A.2    Balle, L.D.3
  • 88
    • 78649468386 scopus 로고    scopus 로고
    • Stabilization of alpha-conotoxin AuIB: influences of disulfide connectivity and backbone cyclization
    • E.S.Lovelace, S.Gunasekera, C.Alvarmo, et al. Stabilization of alpha-conotoxin AuIB:influences of disulfide connectivity and backbone cyclization. Antioxid Redox Signal. 2011;14:87–95. DOI:10.1089/ars.2009.3068
    • (2011) Antioxid Redox Signal , vol.14 , pp. 87-95
    • Lovelace, E.S.1    Gunasekera, S.2    Alvarmo, C.3
  • 89
    • 33750460621 scopus 로고    scopus 로고
    • Cyclic MrIA: A stable and potent cyclic conotoxin with a aovel topological fold that targets the norepinephrine transporter
    • E.S.Lovelace, C.J.Armishaw, M.L.Colgrave, et al. Cyclic MrIA:A stable and potent cyclic conotoxin with a aovel topological fold that targets the norepinephrine transporter. J Med Chem. 2006;49:6561–6568. DOI:10.1021/jm060299h
    • (2006) J Med Chem , vol.49 , pp. 6561-6568
    • Lovelace, E.S.1    Armishaw, C.J.2    Colgrave, M.L.3
  • 90
    • 84899086883 scopus 로고    scopus 로고
    • Biomimetic synthesis of cyclic peptides using novel thioester surrogates
    • X.Hemu, M.Taichi, Y.Qiu, et al. Biomimetic synthesis of cyclic peptides using novel thioester surrogates. Biopolymers. 2013;100:492–501. DOI:10.1002/bip.22308
    • (2013) Biopolymers , vol.100 , pp. 492-501
    • Hemu, X.1    Taichi, M.2    Qiu, Y.3
  • 91
    • 84962319120 scopus 로고    scopus 로고
    • Transforming conotoxins into cyclotides: backbone cyclization of P-superfamily conotoxins
    • M.Akcan, R.J.Clark, N.L.Daly, et al. Transforming conotoxins into cyclotides:backbone cyclization of P-superfamily conotoxins. Biopolymers. 2015;104:682–692. DOI:10.1002/bip.22699
    • (2015) Biopolymers , vol.104 , pp. 682-692
    • Akcan, M.1    Clark, R.J.2    Daly, N.L.3
  • 92
    • 84874966168 scopus 로고    scopus 로고
    • Cyclization of the antimicrobial peptide gomesin with native chemical ligation: influences on stability and bioactivity
    • L.Y.Chan, V.M.Zhang, Y.H.Huang, et al. Cyclization of the antimicrobial peptide gomesin with native chemical ligation:influences on stability and bioactivity. ChemBioChem. 2013;14:617–624. DOI:10.1002/cbic.201300034
    • (2013) ChemBioChem , vol.14 , pp. 617-624
    • Chan, L.Y.1    Zhang, V.M.2    Huang, Y.H.3
  • 93
    • 84864388688 scopus 로고    scopus 로고
    • Cyclisation increases the stability of the sea anemone peptide APETx2 but decreases its activity at acid-sensing ion channel 3
    • J.E.Jensen, M.Mobli, A.Brust, et al. Cyclisation increases the stability of the sea anemone peptide APETx2 but decreases its activity at acid-sensing ion channel 3. Marine Drugs. 2012;10:1511–1527. DOI:10.3390/md10071511
    • (2012) Marine Drugs , vol.10 , pp. 1511-1527
    • Jensen, J.E.1    Mobli, M.2    Brust, A.3
  • 94
    • 84979866905 scopus 로고    scopus 로고
    • Design, synthesis, and characterization of cyclic analogues of the iron regulatory peptide hormone hepcidin
    • R.J.Clark, G.C.Preza, C.C.Tan, et al. Design, synthesis, and characterization of cyclic analogues of the iron regulatory peptide hormone hepcidin. Biopolymers. 2013;100:519–526. DOI:10.1002/bip.22350
    • (2013) Biopolymers , vol.100 , pp. 519-526
    • Clark, R.J.1    Preza, G.C.2    Tan, C.C.3
  • 95
    • 0031574335 scopus 로고    scopus 로고
    • Solution structure and proposed binding mechanism of a novel potassium channel toxin κ-conotoxin PVIIA
    • M.J.Scanlon, D.Naranjo, L.Thomas, et al. Solution structure and proposed binding mechanism of a novel potassium channel toxin κ-conotoxin PVIIA. Structure. 1997;5:1585–1597. DOI:10.1016/S0969-2126(97)00307-9
    • (1997) Structure , vol.5 , pp. 1585-1597
    • Scanlon, M.J.1    Naranjo, D.2    Thomas, L.3
  • 96
    • 84983731362 scopus 로고    scopus 로고
    • Efficient enzymatic cyclization of an inhibitory cystine knot-containing peptide
    • S.Kwon, F.Bosmans, Q.Kaas, et al. Efficient enzymatic cyclization of an inhibitory cystine knot-containing peptide. Biotechnol Bioeng. 2016;113:2202–2212. DOI:10.1002/bit.25993
    • (2016) Biotechnol Bioeng , vol.113 , pp. 2202-2212
    • Kwon, S.1    Bosmans, F.2    Kaas, Q.3
  • 97
    • 21044441799 scopus 로고    scopus 로고
    • Rapid and quantitative cyclization of multiple peptide loops onto synthetic scaffolds for structural mimicry of protein surfaces
    • P.Timmerman, J.Beld, W.C.Puijk, et al. Rapid and quantitative cyclization of multiple peptide loops onto synthetic scaffolds for structural mimicry of protein surfaces. ChemBioChem. 2005;6:821–824. DOI:10.1002/cbic.200400374
    • (2005) ChemBioChem , vol.6 , pp. 821-824
    • Timmerman, P.1    Beld, J.2    Puijk, W.C.3
  • 98
    • 84860259724 scopus 로고    scopus 로고
    • Structurally diverse cyclisation linkers impose different backbone conformations in bicyclic peptides
    • S.Chen, J.Morales-Sanfrutos, A.Angelini, et al. Structurally diverse cyclisation linkers impose different backbone conformations in bicyclic peptides. ChemBioChem. 2012;13:1032–1038. DOI:10.1002/cbic.201200049
    • (2012) ChemBioChem , vol.13 , pp. 1032-1038
    • Chen, S.1    Morales-Sanfrutos, J.2    Angelini, A.3
  • 99
    • 84893436241 scopus 로고    scopus 로고
    • Peptide ligands stabilized by small molecules
    • S.Chen, D.Bertoldo, A.Angelini, et al. Peptide ligands stabilized by small molecules. Angew Chem Int Ed Engl. 2014;53:1602–1606. DOI:10.1002/anie.201309459•• An article highlighting the use of small organic molecules to stabilize peptide epitopes through noncovalent bonding interactions.
    • (2014) Angew Chem Int Ed Engl , vol.53 , pp. 1602-1606
    • Chen, S.1    Bertoldo, D.2    Angelini, A.3
  • 100
    • 84924705949 scopus 로고    scopus 로고
    • Encoded libraries of chemically modified peptides
    • C.Heinis, G.Winter. Encoded libraries of chemically modified peptides. Curr Opin Chem Biol. 2015;26:89–98. DOI:10.1016/j.cbpa.2015.02.008•• A review highlighting the development of peptides with topological constraints using DNA-encoded protein libraries.
    • (2015) Curr Opin Chem Biol , vol.26 , pp. 89-98
    • Heinis, C.1    Winter, G.2
  • 101
    • 67650305952 scopus 로고    scopus 로고
    • Phage-encoded combinatorial chemical libraries based on bicyclic peptides
    • C.Heinis, T.Rutherford, S.Freund, et al. Phage-encoded combinatorial chemical libraries based on bicyclic peptides. Nat Chem Biol. 2009;5:502–507. DOI:10.1038/nchembio.184
    • (2009) Nat Chem Biol , vol.5 , pp. 502-507
    • Heinis, C.1    Rutherford, T.2    Freund, S.3
  • 102
    • 84862834058 scopus 로고    scopus 로고
    • Bicyclic peptides with optimized ring size inhibit human plasma kallikrein and its orthologues while sparing paralogous proteases
    • V.Baeriswyl, H.Rapley, L.Pollaro, et al. Bicyclic peptides with optimized ring size inhibit human plasma kallikrein and its orthologues while sparing paralogous proteases. ChemMedChem. 2012;7:1173–1176. DOI:10.1002/cmdc.201200071
    • (2012) ChemMedChem , vol.7 , pp. 1173-1176
    • Baeriswyl, V.1    Rapley, H.2    Pollaro, L.3
  • 103
    • 84939781522 scopus 로고    scopus 로고
    • A synthetic factor XIIa inhibitor blocks selectively intrinsic coagulation initiation
    • V.Baeriswyl, S.Calzavarini, S.Chen, et al. A synthetic factor XIIa inhibitor blocks selectively intrinsic coagulation initiation. ACS Chem Biol. 2015;10:1861–1870. DOI:10.1021/acschembio.5b00103• An article outlining the use of a constrained bicyclic peptide to potently and selectively inhibit coagulation factor XIIa.
    • (2015) ACS Chem Biol , vol.10 , pp. 1861-1870
    • Baeriswyl, V.1    Calzavarini, S.2    Chen, S.3
  • 104
    • 84956702086 scopus 로고    scopus 로고
    • Phage selection of peptide macrocycles against β-catenin to interfere with Wnt signaling
    • D.Bertoldo, M.M.G.Khan, P.Dessen, et al. Phage selection of peptide macrocycles against β-catenin to interfere with Wnt signaling. ChemMedChem. 2016;11:834–839. DOI:10.1002/cmdc.201500557• A paper demonstrating the use of constrained bicyclic peptides to target β-catenin interfering with the Wnt signaling pathway involved in tumor formation.
    • (2016) ChemMedChem , vol.11 , pp. 834-839
    • Bertoldo, D.1    Khan, M.M.G.2    Dessen, P.3
  • 105
    • 84964285745 scopus 로고    scopus 로고
    • Bicyclic peptides conjugated to an albumin-binding tag diffuse efficiently into solid tumors
    • L.Pollaro, S.Raghunathan, J.Morales-Sanfrutos, et al. Bicyclic peptides conjugated to an albumin-binding tag diffuse efficiently into solid tumors. Mol Cancer Ther. 2015;14:151–161. DOI:10.1158/1535-7163.MCT-14-0534
    • (2015) Mol Cancer Ther , vol.14 , pp. 151-161
    • Pollaro, L.1    Raghunathan, S.2    Morales-Sanfrutos, J.3
  • 106
    • 84901015021 scopus 로고    scopus 로고
    • Exploration of the design principles of a cell-penetrating bicylic peptide scaffold
    • R.Wallbrecher, L.Depré, W.P.R.Verdurmen, et al. Exploration of the design principles of a cell-penetrating bicylic peptide scaffold. Bioconjugate Chem. 2014;25:955–964. DOI:10.1021/bc500107f•• An article highlighting the structural parameters for cell penetration of constrained bicyclic peptides.
    • (2014) Bioconjugate Chem , vol.25 , pp. 955-964
    • Wallbrecher, R.1    Depré, L.2    Verdurmen, W.P.R.3
  • 107
    • 0034697649 scopus 로고    scopus 로고
    • An all-hydrocarbon cross-linking system for enhancing the helicity and metabolic stability of peptides
    • C.E.Schafmeister, J.Po, G.L.Verdine. An all-hydrocarbon cross-linking system for enhancing the helicity and metabolic stability of peptides. J Am Chem Soc. 2000;122:5891–5892. DOI:10.1021/ja000563a• The first paper reporting the development of a stapled peptide.
    • (2000) J Am Chem Soc , vol.122 , pp. 5891-5892
    • Schafmeister, C.E.1    Po, J.2    Verdine, G.L.3
  • 108
    • 84892712887 scopus 로고    scopus 로고
    • Cambridge, MA: Aileron Therapeutics, Available from, Jul
    • Aileron therapeutics successfully completes first-ever stapled peptide clinical trial. Business Wire. Cambridge, MA:Aileron Therapeutics, 2013; [cited 2016 Jul12]. Available from:http://www.businesswire.com/news/home/20130507005467/en/Aileron-Therapeutics-Successfully-Completes-First-Ever-Stapled-Peptide
    • (2013) Business Wire
  • 109
    • 84974672694 scopus 로고    scopus 로고
    • Cambridge, MA: Aileron Therapeutics, Available from, Jul
    • Aileron therapeutics initiates phase 1 cancer study of ALRN-6924 in advanced hematologic and solid malignancies with wild type p53. Business Wire. Cambridge, MA:Aileron Therapeutics; 2015 [cited 2016 Jul12]. Available from:http://www.businesswire.com/news/home/20150212005199/en/Aileron-Therapeutics-Initiates-Phase-1-Cancer-Study
    • (2015) Business Wire
  • 110
    • 84874027448 scopus 로고    scopus 로고
    • Stabilizing the pro-apoptotic BimBH3 helix (BimSAHB) does not necessarily enhance affinity or biological activity
    • T.Okamoto, K.Zobel, A.Fedorova, et al. Stabilizing the pro-apoptotic BimBH3 helix (BimSAHB) does not necessarily enhance affinity or biological activity. ACS Chem Biol. 2013;8:297–302. DOI:10.1021/cb3005403
    • (2013) ACS Chem Biol , vol.8 , pp. 297-302
    • Okamoto, T.1    Zobel, K.2    Fedorova, A.3
  • 111
    • 84915763544 scopus 로고    scopus 로고
    • A versatile platform to analyze low-affinity and transient protein-protein interactions in living cells in real time
    • Y.C.Li, L.W.Rodewald, C.Hoppmann, et al. A versatile platform to analyze low-affinity and transient protein-protein interactions in living cells in real time. Cell Rep. 2014;9:1946–1958. DOI:10.1016/j.celrep.2014.10.058• A paper describing a method to analyze weak intracellular protein–protein interactions in real time and its application assessing the cellular permeability of selected stapled peptides.
    • (2014) Cell Rep , vol.9 , pp. 1946-1958
    • Li, Y.C.1    Rodewald, L.W.2    Hoppmann, C.3
  • 112
    • 84934996624 scopus 로고    scopus 로고
    • Hydrocarbon stapled peptides as modulators of biological function
    • P.M.Cromm, J.Spiegel, T.N.Grossmann. Hydrocarbon stapled peptides as modulators of biological function. ACS Chem Biol. 2015;10:1362–1375. DOI:10.1021/cb501020r• A review highlighting the development and applications of hydrocarbon stapled peptides in drug discovery.
    • (2015) ACS Chem Biol , vol.10 , pp. 1362-1375
    • Cromm, P.M.1    Spiegel, J.2    Grossmann, T.N.3
  • 113
    • 84920550526 scopus 로고    scopus 로고
    • Towards understanding cell penetration by stapled peptides
    • Q.Chu, R.E.Moellering, G.J.Hilinski, et al. Towards understanding cell penetration by stapled peptides. MedChemComm. 2015;6:111–119. DOI:10.1039/C4MD00131A• A paper investigating the structural features associated with cell-penetrating properties of stapled peptides.
    • (2015) MedChemComm , vol.6 , pp. 111-119
    • Chu, Q.1    Moellering, R.E.2    Hilinski, G.J.3
  • 114
    • 84875018420 scopus 로고    scopus 로고
    • Direct activation of full-length proapoptotic BAK
    • E.S.Leshchiner, C.R.Braun, G.H.Bird, et al. Direct activation of full-length proapoptotic BAK. Proc Natl Acad Sci USA. 2013;110:e986–995. DOI:10.1073/pnas.1214313110
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. e986-e995
    • Leshchiner, E.S.1    Braun, C.R.2    Bird, G.H.3
  • 115
    • 84896923199 scopus 로고    scopus 로고
    • Distinct BimBH3 (BimSAHB) stapled peptides for structural and cellular studies
    • G.H.Bird, E.Gavathiotis, J.L.LaBelle, et al. Distinct BimBH3 (BimSAHB) stapled peptides for structural and cellular studies. ACS Chem Biol. 2014;9:831–837. DOI:10.1021/cb4003305•• An article highlighting the key design considerations in the development of stapled peptides.
    • (2014) ACS Chem Biol , vol.9 , pp. 831-837
    • Bird, G.H.1    Gavathiotis, E.2    LaBelle, J.L.3
  • 116
    • 78249268240 scopus 로고    scopus 로고
    • A stapled p53 helix overcomes HDMX-mediated suppression of p53
    • F.Bernal, M.Wade, M.Godes, et al. A stapled p53 helix overcomes HDMX-mediated suppression of p53. Cancer Cell. 2010;18:411–422. DOI:10.1016/j.ccr.2010.10.024• A study using phage display in the development of a stapled peptide that selectively inhibits Mdm2/Mdm4 in the activation of the p53 tumor suppression protein.
    • (2010) Cancer Cell , vol.18 , pp. 411-422
    • Bernal, F.1    Wade, M.2    Godes, M.3
  • 117
    • 84875207784 scopus 로고    scopus 로고
    • Stapled peptides with improved potency and specificity that activate p53
    • C.J.Brown, S.T.Quah, J.Jong, et al. Stapled peptides with improved potency and specificity that activate p53. ACS Chem Biol. 2013;8:506–512. DOI:10.1021/cb3005148
    • (2013) ACS Chem Biol , vol.8 , pp. 506-512
    • Brown, C.J.1    Quah, S.T.2    Jong, J.3
  • 118
    • 84883432191 scopus 로고    scopus 로고
    • Stapled α-helical peptide drug development: a potent dual inhibitor of MDM2 and MDMX for p53-dependent cancer therapy
    • Y.S.Chang, B.Graves, V.Guerlavais, et al. Stapled α-helical peptide drug development:a potent dual inhibitor of MDM2 and MDMX for p53-dependent cancer therapy. Proc Natl Acad Sci USA. 2013;110:e3445–3454. DOI:10.1073/pnas.1303002110•• A paper reporting the use of a stapled peptide that targets the overexpression of inhibitory proteins MDM2 and MDMX to reactivate the p53 tumor suppressor protein in vivo.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. e3445-e3454
    • Chang, Y.S.1    Graves, B.2    Guerlavais, V.3
  • 119
    • 84880179036 scopus 로고    scopus 로고
    • Design of cell-permeable stapled peptides as HIV-1 integrase inhibitors
    • Y.Q.Long, S.X.Huang, Z.Zawahir, et al. Design of cell-permeable stapled peptides as HIV-1 integrase inhibitors. J Med Chem. 2013;56:5601–5612. DOI:10.1021/jm4006516
    • (2013) J Med Chem , vol.56 , pp. 5601-5612
    • Long, Y.Q.1    Huang, S.X.2    Zawahir, Z.3
  • 120
    • 79959492294 scopus 로고    scopus 로고
    • Design and structure of stapled peptides binding to estrogen receptors
    • C.Phillips, L.R.Roberts, M.Schade, et al. Design and structure of stapled peptides binding to estrogen receptors. J Am Chem Soc. 2011;133:9696–9699. DOI:10.1021/ja202946k
    • (2011) J Am Chem Soc , vol.133 , pp. 9696-9699
    • Phillips, C.1    Roberts, L.R.2    Schade, M.3
  • 121
    • 84983485960 scopus 로고    scopus 로고
    • Biophysical determinants for cellular uptake of hydrocarbon-stapled peptide helices
    • G.H.Bird, E.Mazzola, K.Opoku-Nsiah, et al. Biophysical determinants for cellular uptake of hydrocarbon-stapled peptide helices. Nat Chem Biol. 2016;12:845–852.•• A paper outlining the key design principles in the development of cell-permeable stapled peptides.
    • (2016) Nat Chem Biol
    • Bird, G.H.1    Mazzola, E.2    Opoku-Nsiah, K.3
  • 122
    • 84937518958 scopus 로고    scopus 로고
    • Structure-based design of inhibitors of protein–protein interactions: mimicking peptide binding epitopes
    • M.Pelay-Gimeno, A.Glas, O.Koch, et al. Structure-based design of inhibitors of protein–protein interactions:mimicking peptide binding epitopes. Angew Chem Int Ed. 2015;54:8896–8927. DOI:10.1002/anie.201412070• A review that outlines current approaches in the development of various classes of peptide mimetics targeting protein–protein interactions.
    • (2015) Angew Chem Int Ed , vol.54 , pp. 8896-8927
    • Pelay-Gimeno, M.1    Glas, A.2    Koch, O.3
  • 123
    • 84865696005 scopus 로고    scopus 로고
    • β-Hairpin protein epitope mimetic technology in drug discovery
    • D.Obrecht, E.Chevalier, K.Moehle, et al. β-Hairpin protein epitope mimetic technology in drug discovery. Drug Discov Today Technol. 2012;9:e63–69. DOI:10.1016/j.ddtec.2011.07.006
    • (2012) Drug Discov Today Technol , vol.9 , pp. e63-e69
    • Obrecht, D.1    Chevalier, E.2    Moehle, K.3
  • 124
    • 0342716088 scopus 로고    scopus 로고
    • Stabilization of a β-hairpin conformation in a cyclic peptide using the templating effect of a heterochiral diproline unit
    • J.Späth, F.Stuart, L.Jiang, et al. Stabilization of a β-hairpin conformation in a cyclic peptide using the templating effect of a heterochiral diproline unit. Helvetica Chimica Acta. 1998;81:1726–1738. DOI:10.1002/(SICI)1522-2675(19980909)81:9<1726::AID-HLCA1726>3.0.CO;2-H
    • (1998) Helvetica Chimica Acta , vol.81 , pp. 1726-1738
    • Späth, J.1    Stuart, F.2    Jiang, L.3
  • 125
    • 84882828219 scopus 로고    scopus 로고
    • Structural studies of β-hairpin peptidomimetic antibiotics that target LptD in Pseudomonas sp
    • J.Schmidt, K.Patora-Komisarska, K.Moehle, et al. Structural studies of β-hairpin peptidomimetic antibiotics that target LptD in Pseudomonas sp. Bioorg Med Chem. 2013;21:5806–5810. DOI:10.1016/j.bmc.2013.07.013
    • (2013) Bioorg Med Chem , vol.21 , pp. 5806-5810
    • Schmidt, J.1    Patora-Komisarska, K.2    Moehle, K.3
  • 126
    • 77149159117 scopus 로고    scopus 로고
    • Peptidomimetic antibiotics target outer-membrane biogenesis in Pseudomonas aeruginosa
    • N.Srinivas, P.Jetter, B.J.Ueberbacher, et al. Peptidomimetic antibiotics target outer-membrane biogenesis in Pseudomonas aeruginosa. Science. 2010;327:1010–1013. DOI:10.1126/science.1182749• A paper reporting the development of a β-hairpin peptidomimetic as an antimicrobial agent against the pathogen Pseudomonas spp. with a novel mode of action.
    • (2010) Science , vol.327 , pp. 1010-1013
    • Srinivas, N.1    Jetter, P.2    Ueberbacher, B.J.3
  • 127
    • 84970045821 scopus 로고    scopus 로고
    • Synthesis and antimicrobial activity against Pseudomonas aeruginosa of macrocyclic β-hairpin peptidomimetic antibiotics containing N-methylated amino acids
    • S.U.Vetterli, K.Moehle, J.A.Robinson. Synthesis and antimicrobial activity against Pseudomonas aeruginosa of macrocyclic β-hairpin peptidomimetic antibiotics containing N-methylated amino acids. Bioorg Med Chem. 2016. DOI:10.1016/j.bmc.2016.05.027
    • (2016) Bioorg Med Chem
    • Vetterli, S.U.1    Moehle, K.2    Robinson, J.A.3
  • 128
    • 84959010285 scopus 로고    scopus 로고
    • A peptidomimetic antibiotic targets outer membrane proteins and disrupts selectively the outer membrane in escherichia coli
    • M.Urfer, J.Bogdanovic, F.Lo Monte, et al. A peptidomimetic antibiotic targets outer membrane proteins and disrupts selectively the outer membrane in escherichia coli. J Biol Chem. 2016;291:1921–1932. DOI:10.1074/jbc.M115.691725•• An article describing the development of a β-hairpin peptidomimetic that selectively targets outer membrane β-barrel proteins in E. coli.
    • (2016) J Biol Chem , vol.291 , pp. 1921-1932
    • Urfer, M.1    Bogdanovic, J.2    Lo Monte, F.3
  • 129
    • 4544342753 scopus 로고    scopus 로고
    • Using a beta-hairpin to mimic an alpha-helix: cyclic peptidomimetic inhibitors of the p53-HDM2 protein-protein interaction
    • R.Fasan, R.L.Dias, K.Moehle, et al. Using a beta-hairpin to mimic an alpha-helix:cyclic peptidomimetic inhibitors of the p53-HDM2 protein-protein interaction. Angew Chem Int Ed Engl. 2004;43:2109–2112. DOI:10.1002/anie.200353242
    • (2004) Angew Chem Int Ed Engl , vol.43 , pp. 2109-2112
    • Fasan, R.1    Dias, R.L.2    Moehle, K.3
  • 130
    • 33644896783 scopus 로고    scopus 로고
    • Structure-activity studies in a family of beta-hairpin protein epitope mimetic inhibitors of the p53-HDM2 protein-protein interaction
    • R.Fasan, R.L.Dias, K.Moehle, et al. Structure-activity studies in a family of beta-hairpin protein epitope mimetic inhibitors of the p53-HDM2 protein-protein interaction. ChemBioChem. 2006;7:515–526. DOI:10.1002/cbic.200500452
    • (2006) ChemBioChem , vol.7 , pp. 515-526
    • Fasan, R.1    Dias, R.L.2    Moehle, K.3
  • 131
    • 84907923894 scopus 로고    scopus 로고
    • Cyclic penta- and hexaleucine peptides without N-methylation are orally absorbed
    • T.A.Hill, R.-J.Lohman, H.N.Hoang, et al. Cyclic penta- and hexaleucine peptides without N-methylation are orally absorbed. ACS Med Chem Lett. 2014;5:1148–1151. DOI:10.1021/ml5002823
    • (2014) ACS Med Chem Lett , vol.5 , pp. 1148-1151
    • Hill, T.A.1    Lohman, R.-J.2    Hoang, H.N.3
  • 132
    • 84911489309 scopus 로고    scopus 로고
    • Improving on nature: making a cyclic heptapeptide orally bioavailable
    • D.S.Nielsen, H.N.Hoang, R.-J.Lohman, et al. Improving on nature:making a cyclic heptapeptide orally bioavailable. Angew Chem Int Ed. 2014;53:12059–12063. DOI:10.1002/anie.201405364•• A study that investigates the effects of heterocyclic constraints, intermolecular hydrogen bonds, and side-chain interactions in the development of orally bioavailable cyclic peptides.
    • (2014) Angew Chem Int Ed , vol.53 , pp. 12059-12063
    • Nielsen, D.S.1    Hoang, H.N.2    Lohman, R.-J.3
  • 133
    • 80054853098 scopus 로고    scopus 로고
    • On-resin N-methylation of cyclic peptides for discovery of orally bioavailable scaffolds
    • T.R.White, C.M.Renzelman, A.C.Rand, et al. On-resin N-methylation of cyclic peptides for discovery of orally bioavailable scaffolds. Nat Chem Biol. 2011;7:810–817. DOI:10.1038/nchembio.664• A paper describing a method for on-resin N-methylation and its application for the development of orally bioavailable N-methylated cyclic peptides.
    • (2011) Nat Chem Biol , vol.7 , pp. 810-817
    • White, T.R.1    Renzelman, C.M.2    Rand, A.C.3
  • 134
    • 84864182405 scopus 로고    scopus 로고
    • Intestinal permeability of cyclic peptides: common key backbone motifs identified
    • J.G.Beck, J.Chatterjee, B.Laufer, et al. Intestinal permeability of cyclic peptides:common key backbone motifs identified. J Am Chem Soc. 2012;134:12125–12133. DOI:10.1021/ja303200d• Along with reference 135, highlights the backbone structural characteristics of orally bioavailable cyclic peptides containing both N-methylated and D-amino acid residues.
    • (2012) J Am Chem Soc , vol.134 , pp. 12125-12133
    • Beck, J.G.1    Chatterjee, J.2    Laufer, B.3
  • 135
    • 84944711138 scopus 로고    scopus 로고
    • cis-peptide bonds: A key for intestinal permeability of peptides?
    • U.K.Marelli, O.Ovadia, A.O.Frank, et al. cis-peptide bonds:A key for intestinal permeability of peptides? Chem Euro J. 2015;21:15148–15152. DOI:10.1002/chem.201501600
    • (2015) Chem Euro J , vol.21 , pp. 15148-15152
    • Marelli, U.K.1    Ovadia, O.2    Frank, A.O.3
  • 136
    • 84945190129 scopus 로고    scopus 로고
    • Flexibility versus rigidity for orally bioavailable cyclic hexapeptides
    • D.S.Nielsen, R.-J.Lohman, H.N.Hoang, et al. Flexibility versus rigidity for orally bioavailable cyclic hexapeptides. ChemBioChem. 2015;16:2289–2293. DOI:10.1002/cbic.201500441
    • (2015) ChemBioChem , vol.16 , pp. 2289-2293
    • Nielsen, D.S.1    Lohman, R.-J.2    Hoang, H.N.3
  • 137
    • 84935898517 scopus 로고    scopus 로고
    • Probing the physicochemical boundaries of cell permeability and oral bioavailability in lipophilic macrocycles inspired by natural products
    • A.T.Bockus, K.W.Lexa, C.R.Pye, et al. Probing the physicochemical boundaries of cell permeability and oral bioavailability in lipophilic macrocycles inspired by natural products. J Med Chem. 2015;58:4581–4589. DOI:10.1021/acs.jmedchem.5b00128
    • (2015) J Med Chem , vol.58 , pp. 4581-4589
    • Bockus, A.T.1    Lexa, K.W.2    Pye, C.R.3
  • 138
    • 84942288094 scopus 로고    scopus 로고
    • Going out on a limb: delineating the effects of beta-branching, N-methylation, and side chain size on the passive permeability, solubility, and flexibility of sanguinamide A analogues
    • A.T.Bockus, J.A.Schwochert, C.R.Pye, et al. Going out on a limb:delineating the effects of beta-branching, N-methylation, and side chain size on the passive permeability, solubility, and flexibility of sanguinamide A analogues. J Med Chem. 2015;58:7409–7418. DOI:10.1021/acs.jmedchem.5b00919
    • (2015) J Med Chem , vol.58 , pp. 7409-7418
    • Bockus, A.T.1    Schwochert, J.A.2    Pye, C.R.3


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