메뉴 건너뛰기




Volumn 14, Issue 7, 2008, Pages 2100-2111

Folding control in cyclic peptides through N-methylation pattern selection: Formation of antiparallel β-sheet dimers, double reverse turns and supramolecular helices by 3α,γ cyclic peptides

Author keywords

Beta sheets; Foldamers; Helical structures; Peptides; Self assembly

Indexed keywords

ALKYLATION; AMINATION; AMINO ACIDS; FUNCTIONAL POLYMERS; HYDROGEN; HYDROGEN BONDS; METHYLATION; OLIGOMERS; ORGANIC ACIDS; PEPTIDES; PROTEINS; STEREOCHEMISTRY; SUPRAMOLECULAR CHEMISTRY;

EID: 53849146070     PISSN: 09476539     EISSN: 15213765     Source Type: Journal    
DOI: 10.1002/chem.200701059     Document Type: Article
Times cited : (49)

References (146)
  • 4
    • 0035816535 scopus 로고    scopus 로고
    • d) R. Langer, Science 2001, 293, 58-59;
    • (2001) Science , vol.293 , pp. 58-59
    • Langer, R.1
  • 8
    • 0037629769 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 2002, 41, 688-714.
    • (2002) Angew. Chem. Int. Ed , vol.41 , pp. 688-714
  • 13
    • 53849129164 scopus 로고    scopus 로고
    • For examples of reversible folding properties of foldamers induced by changes in temperature, solvent, pH or light, see: a A. Khan, C. Kaisher, S. Hecht, Angew. Chem. 2006, 118, 1912-1915;
    • For examples of reversible folding properties of foldamers induced by changes in temperature, solvent, pH or light, see: a) A. Khan, C. Kaisher, S. Hecht, Angew. Chem. 2006, 118, 1912-1915;
  • 14
    • 33745431935 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 2006, 45, 1878-1881;
    • (2006) Angew. Chem. Int. Ed , vol.45 , pp. 1878-1881
  • 16
    • 0347985382 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 2003, 42, 6021-6024;
    • (2003) Angew. Chem. Int. Ed , vol.42 , pp. 6021-6024
  • 18
    • 0037715341 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 2003, 42, 2738-2740;
    • (2003) Angew. Chem. Int. Ed , vol.42 , pp. 2738-2740
  • 22
    • 0033555217 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 1999, 38, 233-236;
    • (1999) Angew. Chem. Int. Ed , vol.38 , pp. 233-236
  • 23
    • 34247882692 scopus 로고    scopus 로고
    • For some examples of foldamer-based reactivity, see: a
    • For some examples of foldamer-based reactivity, see: a) R. A. Smaldone, J. Moore, J. Am. Chem. Soc. 2007, 129, 5444-5450;
    • (2007) J. Moore, J. Am. Chem. Soc , vol.129 , pp. 5444-5450
    • Smaldone, R.A.1
  • 28
    • 9444226868 scopus 로고    scopus 로고
    • D. Seebach, A. K. Beck, D. J. Bierbaum, Chemistry & Biodiversity. 2004, 1, 1111-1239; Biodiversity. 2004, 1, 1111-1239.
    • b) D. Seebach, A. K. Beck, D. J. Bierbaum, Chemistry & Biodiversity. 2004, 1, 1111-1239; Biodiversity. 2004, 1, 1111-1239.
  • 29
    • 0033516710 scopus 로고    scopus 로고
    • For some examples of γ-peptide foldamers, see: a
    • For some examples of γ-peptide foldamers, see: a) S. Hanessian, X. Lou, R. Schaum, Tetrahedron Lett. 1999, 40, 4925-4929;
    • (1999) Tetrahedron Lett , vol.40 , pp. 4925-4929
    • Hanessian, S.1    Lou, X.2    Schaum, R.3
  • 33
    • 0037450183 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 2003, 42, 776-778;
    • (2003) Angew. Chem. Int. Ed , vol.42 , pp. 776-778
  • 39
    • 33846111292 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 2007, 46, 214-217;
    • (2007) Angew. Chem. Int. Ed , vol.46 , pp. 214-217
  • 42
    • 0344944630 scopus 로고    scopus 로고
    • and references therein
    • M. Stefani, C. M. Dobson, J. Mol. Med. 2003, 81, 678-699, and references therein.
    • (2003) J. Mol. Med , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 44
    • 16844369868 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 2005, 44, 1968-1971;
    • (2005) Angew. Chem. Int. Ed , vol.44 , pp. 1968-1971
  • 47
    • 20144388657 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 2005, 44, 1965-1968.
    • (2005) Angew. Chem. Int. Ed , vol.44 , pp. 1965-1968
  • 51
    • 24944476369 scopus 로고    scopus 로고
    • Self-Assembly of Cyclic Peptides in Hydrogen-Bonded Nanotubes
    • Marcel Dekker Inc
    • a) R. J. Brea, J. R. Granja, Self-Assembly of Cyclic Peptides in Hydrogen-Bonded Nanotubes, In Dekker Encyclopedia of Nanoscience and Nanotechnology, Marcel Dekker Inc., 2004, pp. 3439-3457;
    • (2004) Dekker Encyclopedia of Nanoscience and Nanotechnology , pp. 3439-3457
    • Brea, R.J.1    Granja, J.R.2
  • 53
    • 0037099441 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 2002, 41, 2446-2461;
    • (2002) Angew. Chem. Int. Ed , vol.41 , pp. 2446-2461
  • 55
    • 0035857549 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 2001, 40, 988-1011;
    • (2001) Angew. Chem. Int. Ed , vol.40 , pp. 988-1011
  • 57
    • 0037264039 scopus 로고    scopus 로고
    • For an example of biotechnological applications of nanotubes, see
    • For an example of biotechnological applications of nanotubes, see: C. R. Martin, P. Kohli, Nature Reviews Drug Discovery 2003, 2, 29-37.
    • (2003) Nature Reviews Drug Discovery , vol.2 , pp. 29-37
    • Martin, C.R.1    Kohli, P.2
  • 58
    • 0028174318 scopus 로고
    • For transmembrane transport of molecules or ions by peptide nanotubes, see
    • a) For transmembrane transport of molecules or ions by peptide nanotubes, see: M. R. Ghadiri, J. R. Granja, L. K. Buehler, Nature 1994, 369, 301-304;
    • (1994) Nature , vol.369 , pp. 301-304
    • Ghadiri, M.R.1    Granja, J.R.2    Buehler, L.K.3
  • 61
    • 0035796637 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 2001, 40, 2503-2506;
    • (2001) Angew. Chem. Int. Ed , vol.40 , pp. 2503-2506
  • 63
    • 0035796637 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 2001, 40, 2503-2506;
    • (2001) Angew. Chem. Int. Ed , vol.40 , pp. 2503-2506
  • 67
    • 0032651702 scopus 로고    scopus 로고
    • for photoswitchable materials based on self-assembled peptides, see
    • c) for photoswitchable materials based on self-assembled peptides, see: C. Steinem, A. Janshoff, M. S. Vollmer, M. R. Ghadiri, Langmuir 1999, 15, 3956-3964;
    • (1999) Langmuir , vol.15 , pp. 3956-3964
    • Steinem, C.1    Janshoff, A.2    Vollmer, M.S.3    Ghadiri, M.R.4
  • 69
    • 0033152135 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 1999, 38, 1598-1601;
    • (1999) Angew. Chem. Int. Ed , vol.38 , pp. 1598-1601
  • 70
    • 1842410757 scopus 로고    scopus 로고
    • for size-selective ion sensing based on SAM-supported peptide nanotubes, see: K. Motesharei, M. R. Ghadiri, J. Am. Chem. Soc. 1997, 119, 11306-11312;
    • d) for size-selective ion sensing based on SAM-supported peptide nanotubes, see: K. Motesharei, M. R. Ghadiri, J. Am. Chem. Soc. 1997, 119, 11306-11312;
  • 72
    • 20344399178 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 2005, 44, 3297-3301;
    • (2005) Angew. Chem. Int. Ed , vol.44 , pp. 3297-3301
  • 73
    • 32044443628 scopus 로고    scopus 로고
    • for potential applications in molecular electronics, see
    • f) for potential applications in molecular electronics, see: N. Ashkenasy, W. S. Horne, M. R. Ghadiri, Small 2006, 2, 99-102.
    • (2006) Small , vol.2 , pp. 99-102
    • Ashkenasy, N.1    Horne, W.S.2    Ghadiri, M.R.3
  • 77
    • 0000687330 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 2001, 40, 2163-2166;
    • (2001) Angew. Chem. Int. Ed , vol.40 , pp. 2163-2166
  • 82
    • 53849137247 scopus 로고    scopus 로고
    • for eight-residue α,γ-CPs, see: M. Amorín, L. Castedo, J. R. Granja, Chem. Eur. J. 2005, 11, 6539-6547;
    • b) for eight-residue α,γ-CPs, see: M. Amorín, L. Castedo, J. R. Granja, Chem. Eur. J. 2005, 11, 6539-6547;
  • 83
    • 27144476831 scopus 로고    scopus 로고
    • for four-residue α,γ-CPs, see: M. Amorín, R. J. Brea, L. Castedo, J. R. Granja, Org. Lett. 2005, 7, 4681-4684;
    • c) for four-residue α,γ-CPs, see: M. Amorín, R. J. Brea, L. Castedo, J. R. Granja, Org. Lett. 2005, 7, 4681-4684;
  • 84
    • 53849101780 scopus 로고    scopus 로고
    • for larger-size α,γ-CPs, see: R. J. Brea, L. Castedo, J. R. Granja, Chem. Com. 2007, 3267-3269.
    • d) for larger-size α,γ-CPs, see: R. J. Brea, L. Castedo, J. R. Granja, Chem. Com. 2007, 3267-3269.
  • 85
    • 53849127445 scopus 로고    scopus 로고
    • For α,γ-CP heterodimer formation and applications in electron- and energy-transfer processes, see
    • For α,γ-CP heterodimer formation and applications in electron- and energy-transfer processes, see: R. J. Brea, M. Amorín, L. Castedo, J. R. Granja, Angew. Chem. 2005, 117, 5856-5859;
    • (2005) Angew. Chem , vol.117 , pp. 5856-5859
    • Brea, R.J.1    Amorín, M.2    Castedo, L.3    Granja, J.R.4
  • 86
    • 24944550968 scopus 로고    scopus 로고
    • Angew. Chem. Int. Ed. 2005, 44, 5710-5713;
    • (2005) Angew. Chem. Int. Ed , vol.44 , pp. 5710-5713
  • 88
    • 0032500342 scopus 로고    scopus 로고
    • The flexibility of its 30-membered ring has been blamed for the non-association of an N-methylated cyclic decapeptide composed of alternating D- and L-α-amino acids
    • The flexibility of its 30-membered ring has been blamed for the non-association of an N-methylated cyclic decapeptide composed of alternating D- and L-α-amino acids: T. D. Clark, J. M. Buriak, K. Kobayashi, M. P. Isler, D. E. McRee, M. R. Ghadiri, J. Am. Chem. Soc. 1998, 120, 8949-8962.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 8949-8962
    • Clark, T.D.1    Buriak, J.M.2    Kobayashi, K.3    Isler, M.P.4    McRee, D.E.5    Ghadiri, M.R.6
  • 89
    • 0035804941 scopus 로고    scopus 로고
    • as ion pair receptors, For peptides made of alternating &alpha-amino acid and 3-aminobenzoic acid derivatives: as ion channels, a
    • For peptides made of alternating &alpha-amino acid and 3-aminobenzoic acid derivatives: as ion channels, a) H. Ishida, Z. Qi, M. Sokabe, K. Donowaki, Y. Inoue, J. Org. Chem. 2001, 66, 2978-2989; as ion pair receptors,
    • (2001) J. Org. Chem , vol.66 , pp. 2978-2989
    • Ishida, H.1    Qi, Z.2    Sokabe, M.3    Donowaki, K.4    Inoue, Y.5
  • 91
    • 0025299887 scopus 로고    scopus 로고
    • Alkylation of the amide nitrogen reduces the energy difference between the cis and trans forms: D. E. Stewart, A. Sarkar, J. E. Wampler, J. Mol. Biol. 1990, 214, 253-260;
    • a) Alkylation of the amide nitrogen reduces the energy difference between the cis and trans forms: D. E. Stewart, A. Sarkar, J. E. Wampler, J. Mol. Biol. 1990, 214, 253-260;
  • 92
    • 0019128779 scopus 로고    scopus 로고
    • N-modified amino acids would influence polypeptides containing them by adopting an extended conformation and ensuring the adoption of a similar conformation by their N-terminal neighbours: P. Manavalan, F. A. Momany, Biopolymers 1980, 19, 1943-1973; but also promoting the formation of β-turns
    • b) N-modified amino acids would influence polypeptides containing them by adopting an extended conformation and ensuring the adoption of a similar conformation by their N-terminal neighbours: P. Manavalan, F. A. Momany, Biopolymers 1980, 19, 1943-1973; but also promoting the formation of β-turns:
  • 94
    • 33845309676 scopus 로고    scopus 로고
    • and references therein. For a recent study of structural behaviour of N-methylated cyclic peptide, see
    • For a recent study of structural behaviour of N-methylated cyclic peptide, see: J. Chatterjee, D. Mierke, H. Kessler, J. Am. Chem. Soc. 2006, 128, 15164-15172, and references therein.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 15164-15172
    • Chatterjee, J.1    Mierke, D.2    Kessler, H.3
  • 96
    • 53849098504 scopus 로고    scopus 로고
    • Even in the case of CPs formed of alternate L- and D-α-Aas, hydrogen bonding between antiparallel CPs is thermodynamically more favoured than hydrogen bonding between parallel CPs: K. Kobayashi, J. R. Granja, M. R. Ghadiri, Angew. Chem. 1995, 107, 79-81;
    • Even in the case of CPs formed of alternate L- and D-α-Aas, hydrogen bonding between antiparallel CPs is thermodynamically more favoured than hydrogen bonding between parallel CPs: K. Kobayashi, J. R. Granja, M. R. Ghadiri, Angew. Chem. 1995, 107, 79-81;
  • 99
    • 53849114268 scopus 로고    scopus 로고
    • sat, the integral ratio at saturation, was also optimized in the fitting process.
    • sat, the integral ratio at saturation, was also optimized in the fitting process.
  • 107
    • 33846979505 scopus 로고    scopus 로고
    • For a recent study on dimerization constants of α,γ-CPs by fluorescence measurements, see
    • For a recent study on dimerization constants of α,γ-CPs by fluorescence measurements, see: R. J. Brea, M. E. Vázquez, M. Mosquera, L. Castedo, J. R. Granja, J. Am. Chem. Soc. 2007, 129, 1653-1657.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 1653-1657
    • Brea, R.J.1    Vázquez, M.E.2    Mosquera, M.3    Castedo, L.4    Granja, J.R.5
  • 110
    • 53849142431 scopus 로고    scopus 로고
    • MeN-γ- Ach.
    • MeN-γ- Ach.
  • 111
    • 0025299887 scopus 로고    scopus 로고
    • Alkylation of the amide nitrogen reduces the energy difference between the cis and trans forms to approximately 2.1 kJmol-1 as against around 10.9 kJmol-1 for conventional amino acids: D. E. Stewart, A. Sarkar, J. E. Wampler, J. Mol. Biol. 1990, 214, 253-260;
    • -1 for conventional amino acids: D. E. Stewart, A. Sarkar, J. E. Wampler, J. Mol. Biol. 1990, 214, 253-260;
  • 112
    • 0019128779 scopus 로고    scopus 로고
    • N-modified amino acids would influence the polypeptides containing them by adopting an extended conformation and ensuring the adoption of a similar conformation by their N-terminal neighbours: P. Manavalan, F. A. Momany, Biopolymers 1980, 19, 1943-1973;
    • b) N-modified amino acids would influence the polypeptides containing them by adopting an extended conformation and ensuring the adoption of a similar conformation by their N-terminal neighbours: P. Manavalan, F. A. Momany, Biopolymers 1980, 19, 1943-1973;
  • 113
    • 0028852791 scopus 로고    scopus 로고
    • but also by c promoting the formation of β-turns: W. Braun, J. Kallen, V. Mikol, M. D. Walkinshaw, K. Wüthrich, FASEB 1995, 9, 63-72;
    • but also by c) promoting the formation of β-turns: W. Braun, J. Kallen, V. Mikol, M. D. Walkinshaw, K. Wüthrich, FASEB 1995, 9, 63-72;
  • 116
    • 53849098328 scopus 로고    scopus 로고
    • Chemical shifts of NH protons involved in strong hydrogen-bonding interactions stay unchanged with temperature change, while the chemical shifts of solvent-exposed NH protons (no hydrogen bonding involved) change with the temperature. T. Cierpici, J. Otlewski, J. Biomol. NMR 2001, 21, 249-261
    • Chemical shifts of NH protons involved in strong hydrogen-bonding interactions stay unchanged with temperature change, while the chemical shifts of solvent-exposed NH protons (no hydrogen bonding involved) change with the temperature. T. Cierpici, J. Otlewski, J. Biomol. NMR 2001, 21, 249-261.
  • 119
    • 0021779081 scopus 로고
    • Eds, C. B. Anfinsen, J. T. Edsall, F. M. Richards, Academic Press, New York
    • c) G. D. Rose, L. M. Gierasch, J. A. Smith, in Turns in Peptides and Proteins, Vol. 37 (Eds.: C. B. Anfinsen, J. T. Edsall, F. M. Richards), Academic Press, New York, 1985, pp. 1-109;
    • (1985) Turns in Peptides and Proteins , vol.37 , pp. 1-109
    • Rose, G.D.1    Gierasch, L.M.2    Smith, J.A.3
  • 123
    • 0028316393 scopus 로고    scopus 로고
    • It has been shown that D-α-amino acids induce type II' β-turns in solution, see: a V. Bobde, C. Sadasivan, S. Durani, Int. J. Peptide Protein Res. 1994, 44, 209-218;
    • It has been shown that D-α-amino acids induce type II' β-turns in solution, see: a) V. Bobde, C. Sadasivan, S. Durani, Int. J. Peptide Protein Res. 1994, 44, 209-218;
  • 126
    • 33646023145 scopus 로고    scopus 로고
    • b Hairpins design by insertion of β-, γ- and δ-amino acid residues at the position i+2, see: R. S. Roy, H. N. Gopi, S. Raghothama, I. L. Karle, P. Balaram, Chem. Eur. J. 2006, 12, 3295-3302;
    • b Hairpins design by insertion of β-, γ- and δ-amino acid residues at the position i+2, see: R. S. Roy, H. N. Gopi, S. Raghothama, I. L. Karle, P. Balaram, Chem. Eur. J. 2006, 12, 3295-3302;
  • 134
    • 0000336227 scopus 로고    scopus 로고
    • ac), L. A. LaPlanche, H. B. Thompson, M. T. Rogers, J. Phys. Chem. 1965, 69, 1482.
    • ac), L. A. LaPlanche, H. B. Thompson, M. T. Rogers, J. Phys. Chem. 1965, 69, 1482.
  • 137
    • 53849141123 scopus 로고    scopus 로고
    • Nonius BV, Delft (The Netherlands) 1997-2000.
    • Nonius BV, Delft (The Netherlands) 1997-2000.
  • 141
    • 84942435207 scopus 로고    scopus 로고
    • A. L. Spek, PLATON, University of Utrecht (The Netherlands) (2001); P. van der Sluis, A. L. Spek, Acta Crystallogr. Sect. A 1990, 46, 194-201.
    • A. L. Spek, PLATON, University of Utrecht (The Netherlands) (2001); P. van der Sluis, A. L. Spek, Acta Crystallogr. Sect. A 1990, 46, 194-201.
  • 143
    • 53849148192 scopus 로고    scopus 로고
    • G. M. Sheldrick, Institute für Anorganische Chemie, Universität Göttingen, Göttingen Germany
    • G. M. Sheldrick, Institute für Anorganische Chemie, Universität Göttingen, Göttingen (Germany).
  • 145
    • 53849109118 scopus 로고    scopus 로고
    • Bruker AXS, Madison USA
    • Bruker AXS, Madison (USA).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.