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Volumn 129, Issue 9, 2007, Pages 2548-2558

Cyclic modular β-sheets

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CROSSLINKING; MAGNETIC ANISOTROPY; PROTEIN FOLDING; SYNTHESIS (CHEMICAL); WATER;

EID: 33847628368     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0667965     Document Type: Article
Times cited : (47)

References (96)
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    • A similar approach to linking cyclic β-hairpins was described by Overhand and coworkers, who linked gramicidin S peptides through 4-aminoproline turn residues. Grotenbreg, G. M.; Witte, M. D.; van Hooft, P. A. V.; Spalburg, E.; Reiss, P.; Noort, D.; de Neeling, A. J.; Koert, U.; van der Marel, G. A.; Overkleeft, H. S.; Overhand, M. Org. Biomol. Chem. 2005, 3, 233-238.
    • A similar approach to linking cyclic β-hairpins was described by Overhand and coworkers, who linked gramicidin S peptides through 4-aminoproline turn residues. Grotenbreg, G. M.; Witte, M. D.; van Hooft, P. A. V.; Spalburg, E.; Reiss, P.; Noort, D.; de Neeling, A. J.; Koert, U.; van der Marel, G. A.; Overkleeft, H. S.; Overhand, M. Org. Biomol. Chem. 2005, 3, 233-238.
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    • For examples of other cyclic peptides inspired by gramicidin S, see: (a) Ando, S, Takiguchi, H, Izumiya, N. Bull. Chem. Soc. Jpn. 1983, 56, 3781-3785
    • For examples of other cyclic peptides inspired by gramicidin S, see: (a) Ando, S.; Takiguchi, H.; Izumiya, N. Bull. Chem. Soc. Jpn. 1983, 56, 3781-3785.
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    • β-Amyloid is a 40- or 42-residue peptide that self-associates into fibrils through β-sheet interactions. For recent structural studies of β-amyloid, see: (a) Petkova, A. T.; Ishii, Y.; Balbach, J. J.; Antzutkin, O. N.; Leapman, R. D.; Delaglio, F.; Tycko, R. Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 16742-16747.
    • β-Amyloid is a 40- or 42-residue peptide that self-associates into fibrils through β-sheet interactions. For recent structural studies of β-amyloid, see: (a) Petkova, A. T.; Ishii, Y.; Balbach, J. J.; Antzutkin, O. N.; Leapman, R. D.; Delaglio, F.; Tycko, R. Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 16742-16747.
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    • MIP-2 forms a dimer containing a six-stranded antiparallel β-sheet. Shao, W.; Jerva, L. F.; West, J.; Lolis, E.; Schweitzer, B. I. Biochemistry 1998, 37, 8303-8313.
    • MIP-2 forms a dimer containing a six-stranded antiparallel β-sheet. Shao, W.; Jerva, L. F.; West, J.; Lolis, E.; Schweitzer, B. I. Biochemistry 1998, 37, 8303-8313.
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    • For statistical studies of the frequency of amino acids in β-sheets, see: a
    • For statistical studies of the frequency of amino acids in β-sheets, see: (a) Chou, P. Y.; Fasman, G. D. Biochemistry 1974, 13, 211-222.
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    • For statistical studies of side-chain pairings in β-sheets, see: a
    • For statistical studies of side-chain pairings in β-sheets, see: (a) Lifson, S.; Sander, C. J. Mol. Biol. 1980, 139, 627-639.
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    • Most of the standard peptide synthesis procedures described in this paper were obtained from the Peptide Synthesis Protocols section of the Novabiochem catalog, which is an excellent guide for peptide synthesis
    • Most of the standard peptide synthesis procedures described in this paper were obtained from the "Peptide Synthesis Protocols" section of the Novabiochem catalog, which is an excellent guide for peptide synthesis.
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    • We have also prepared cyclic modular β-sheets 1 with Ellman's alkylsulfonamide safety-catch resin, which permits simultaneous cyclization and cleavage from the resin: (a) Backes, B. J, Ellman, J. A. J. Org. Chem. 1999, 64, 2322-2330
    • We have also prepared cyclic modular β-sheets 1 with Ellman's alkylsulfonamide "safety-catch" resin, which permits simultaneous cyclization and cleavage from the resin: (a) Backes, B. J.; Ellman, J. A. J. Org. Chem. 1999, 64, 2322-2330.
  • 72
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    • The Fmoc* (2,7-di-tert-butyl-9-fluorenylmethoxycarbonyl) group was developed as a base-labile protecting group that imparts sufficient solubility to Hao and its precursors in organic solvents. Stigers, K. D.; Koutroulis, M. R.; Chung, D. M.; Nowick, J. S. J. Org. Chem. 2000, 65, 3858-3860.
    • The Fmoc* (2,7-di-tert-butyl-9-fluorenylmethoxycarbonyl) group was developed as a base-labile protecting group that imparts sufficient solubility to Hao and its precursors in organic solvents. Stigers, K. D.; Koutroulis, M. R.; Chung, D. M.; Nowick, J. S. J. Org. Chem. 2000, 65, 3858-3860.
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    • 1H NMR resonances) in the buffered solutions; these compounds were therefore studied without buffer.
    • 1H NMR resonances) in the buffered solutions; these compounds were therefore studied without buffer.
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    • 1H NMR spectra of the cyclic modular β-sheets were referenced to the cationic internal standard DSA, which is less prone to association with cationic peptides than the popular anionic internal standard DSS. Nowick, J. S.; Khakshoor, O.; Hashemzadeh, M.; Brower, J. O. Org. Lett. 2003, 5, 3511-3513.
    • 1H NMR spectra of the cyclic modular β-sheets were referenced to the cationic internal standard DSA, which is less prone to association with cationic peptides than the popular anionic internal standard DSS. Nowick, J. S.; Khakshoor, O.; Hashemzadeh, M.; Brower, J. O. Org. Lett. 2003, 5, 3511-3513.
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    • This alternate conformation may involve a cis-amide linkage between the Hao hydrazide group and δOrn2
    • This alternate conformation may involve a cis-amide linkage between the Hao hydrazide group and δOrn2.
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    • Random coil reference peptides such as these help to account for the effects of specific neighboring residues on α-proton chemical shifts. For other examples of reference peptides for the unfolded state of a peptide β-hairpin, see ref 6b and Butterfield, S. M, Waters, M. L. J. Am. Chem. Soc. 2003, 125, 9580-9581
    • Random coil reference peptides such as these help to account for the effects of specific neighboring residues on α-proton chemical shifts. For other examples of reference peptides for the unfolded state of a peptide β-hairpin, see ref 6b and Butterfield, S. M.; Waters, M. L. J. Am. Chem. Soc. 2003, 125, 9580-9581.
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    • δOm pro-S δ-proton. The large anisotropy may also reflect the formation of a more highly ordered structure through stronger hydrogen bonding in a noncompetitive organic solvent.
    • δOm pro-S δ-proton. The large anisotropy may also reflect the formation of a more highly ordered structure through stronger hydrogen bonding in a noncompetitive organic solvent.
  • 88
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    • The sLED pulse sequence was used in the PFG NMR diffusion studies of the cyclic modular β-sheets (ref 40b).
    • The sLED pulse sequence was used in the PFG NMR diffusion studies of the cyclic modular β-sheets (ref 40b).
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    • The diffusion coefficient of 2 is slightly lower than would be expected for a simple dimer of 1b and may reflect some minor additional self-association. For discussions of the relationship between diffusion coefficients and molecular weight, see: (a) Teller, D. C.; Swanson, E.; DeHaen, C. Methods Enzymol. 1979, 61, 103-124.
    • The diffusion coefficient of 2 is slightly lower than would be expected for a simple dimer of 1b and may reflect some minor additional self-association. For discussions of the relationship between diffusion coefficients and molecular weight, see: (a) Teller, D. C.; Swanson, E.; DeHaen, C. Methods Enzymol. 1979, 61, 103-124.
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    • Other studies have demonstrated the importance of aromatic-aromatic interactions in β-hairpin stability. For examples, see ref 6a, d, and k
    • Other studies have demonstrated the importance of aromatic-aromatic interactions in β-hairpin stability. For examples, see ref 6a, d, and k.
  • 95
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    • A study by Nowick and coworkers suggests that aromatic interactions are not important in intermolecular β-sheet interactions. Chung, D. M.; Dou, Y.; Baldi, P.; Nowick, J. S. J. Am. Chem. Soc. 2005, 127, 9998-9999.
    • A study by Nowick and coworkers suggests that aromatic interactions are not important in intermolecular β-sheet interactions. Chung, D. M.; Dou, Y.; Baldi, P.; Nowick, J. S. J. Am. Chem. Soc. 2005, 127, 9998-9999.
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    • The interaction between the phenylalanine residue at position 4 and Hao is similar to the aromatic rescue of glycine in β-sheets reported by Merkel and Regan: Merkel, J. S.; Regan, L. Fold. Des. 1998, 3, 449-455.
    • The interaction between the phenylalanine residue at position 4 and Hao is similar to the "aromatic rescue of glycine in β-sheets" reported by Merkel and Regan: Merkel, J. S.; Regan, L. Fold. Des. 1998, 3, 449-455.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.