메뉴 건너뛰기




Volumn 129, Issue 1, 2007, Pages 139-154

(α/β+α)-peptide antagonists of BH3 domain/Bcl-x L recognition: Toward general strategies for foldamer-based inhibition of protein-protein interactions

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BIOASSAY; ENZYME INHIBITION; FLUORESCENCE; MOLECULAR STRUCTURE; SURFACE CHEMISTRY;

EID: 33846042156     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0662523     Document Type: Article
Times cited : (152)

References (88)
  • 10
    • 20444486559 scopus 로고    scopus 로고
    • (c) Oltersdorf, T.; et al. Nature 2005, 435, 677-681.
    • (2005) Nature , vol.435 , pp. 677-681
    • Oltersdorf, T.1
  • 14
    • 0035542909 scopus 로고    scopus 로고
    • A review of several foldamer architectures: Hill, D. J.; Mio, M. J.; Prince, R. B.; Hughes, T. S.; Moore, J. S. Chem. Rev. 2001, 101, 3893-4011.
    • A review of several foldamer architectures: Hill, D. J.; Mio, M. J.; Prince, R. B.; Hughes, T. S.; Moore, J. S. Chem. Rev. 2001, 101, 3893-4011.
  • 15
    • 0842329029 scopus 로고    scopus 로고
    • α/β-Peptide secondary structures: (a) Hayen, A.; Schmitt, M. A.; Ngassa, F. N.; Thomasson, K. A.; Gellman, S. H. Angew. Chem., Int. Ed. 2004, 43, 505-510.
    • α/β-Peptide secondary structures: (a) Hayen, A.; Schmitt, M. A.; Ngassa, F. N.; Thomasson, K. A.; Gellman, S. H. Angew. Chem., Int. Ed. 2004, 43, 505-510.
  • 26
    • 0036710477 scopus 로고    scopus 로고
    • L inhibition: (a) Baell, J. B.; Huang, D. C. S. Biochem. Pharmacol. 2002, 64, 851-863.
    • L inhibition: (a) Baell, J. B.; Huang, D. C. S. Biochem. Pharmacol. 2002, 64, 851-863.
  • 28
    • 1442310957 scopus 로고    scopus 로고
    • L interactions: Petros, A. M.; Olejniczak, E. T.; Fesik, S. W. Biochim. Biophys. Acta 2004, 1644, 83-94.
    • L interactions: Petros, A. M.; Olejniczak, E. T.; Fesik, S. W. Biochim. Biophys. Acta 2004, 1644, 83-94.
  • 33
    • 0030614915 scopus 로고    scopus 로고
    • L: Sattler, M.; Liang, H.; Nettesheim, D.; Meadows, R. P.; Harlan, J. E.; Eberstadt, M.; Yoon, H. S.; Shuker, S. B.; Chang, B. S.; Minn, A. J.; Thompson, C. B.; Fesik, S. W. Science 1997, 275, 983-986.
    • L: Sattler, M.; Liang, H.; Nettesheim, D.; Meadows, R. P.; Harlan, J. E.; Eberstadt, M.; Yoon, H. S.; Shuker, S. B.; Chang, B. S.; Minn, A. J.; Thompson, C. B.; Fesik, S. W. Science 1997, 275, 983-986.
  • 34
    • 17744396094 scopus 로고    scopus 로고
    • L: Petros, A. M.; Nettesheim, D. G.; Wang, Y.; Olejniczak, E. T.; Meadows, R. P.; Mack, J.; Swift, K.; Matayoshi, E. D.; Zhang, H.; Thompson, C. B.; Fesik, S. W. Protein Sci. 2000, 9, 2528-2534.
    • L: Petros, A. M.; Nettesheim, D. G.; Wang, Y.; Olejniczak, E. T.; Meadows, R. P.; Mack, J.; Swift, K.; Matayoshi, E. D.; Zhang, H.; Thompson, C. B.; Fesik, S. W. Protein Sci. 2000, 9, 2528-2534.
  • 35
    • 33846054309 scopus 로고    scopus 로고
    • L: Liu, X.; Dai, S.; Zhu, Y.; Marrack, P.; Kappler, J. W. Immunity 2003, 19, 341-352.
    • L: Liu, X.; Dai, S.; Zhu, Y.; Marrack, P.; Kappler, J. W. Immunity 2003, 19, 341-352.
  • 42
    • 0030995823 scopus 로고    scopus 로고
    • The structures of α/β- and β-peptide helices that could serve as α-helix-mimetic scaffolds are derived from high-resolution foldamer structures: (a) Appella, D. H, Christianson, L. A, Klein, D. A, Powell, D. R, Huang, X, Barchi, J. J, Gellman, S. H. Nature 1997, 387, 381-384
    • The structures of α/β- and β-peptide helices that could serve as α-helix-mimetic scaffolds are derived from high-resolution foldamer structures: (a) Appella, D. H.; Christianson, L. A.; Klein, D. A.; Powell, D. R.; Huang, X.; Barchi, J. J.; Gellman, S. H. Nature 1997, 387, 381-384.
  • 43
    • 0033532930 scopus 로고    scopus 로고
    • Appella, D. H.; Christianson, L. A.; Karle, I. L.; Powell, D. R.; Gellman, S. H. J. Am. Chem. Soc. 1999, 121, 6206. See also ref 8a.
    • (b) Appella, D. H.; Christianson, L. A.; Karle, I. L.; Powell, D. R.; Gellman, S. H. J. Am. Chem. Soc. 1999, 121, 6206. See also ref 8a.
  • 52
    • 7444262377 scopus 로고    scopus 로고
    • The sensitivity of competition FP assays to weakly binding compounds is dependent upon the binding affinity of the fluorescent probe for the protein target. For example, see: Nikolovska-Coleska, Z, Wang, R, Fang, X, Pan, H, Tomita, Y, Li, P, Roller, P. P, Krajewski, K, Saito, N. G, Stuckey, J. A, Wang, S. Anal. Biochem. 2004, 332, 261
    • The sensitivity of competition FP assays to weakly binding compounds is dependent upon the binding affinity of the fluorescent probe for the protein target. For example, see: Nikolovska-Coleska, Z.; Wang, R.; Fang, X.; Pan, H.; Tomita, Y.; Li, P.; Roller, P. P.; Krajewski, K.; Saito, N. G.; Stuckey, J. A.; Wang, S. Anal. Biochem. 2004, 332, 261.
  • 56
    • 33846119579 scopus 로고    scopus 로고
    • L] = 20 nM.
    • L] = 20 nM.
  • 67
    • 0000372879 scopus 로고    scopus 로고
    • and references therein
    • Stites, W. E. Chem. Rev. 1997, 97, 1233-1250 and references therein.
    • (1997) Chem. Rev , vol.97 , pp. 1233-1250
    • Stites, W.E.1
  • 69
    • 33846085435 scopus 로고    scopus 로고
    • L may be qualitatively predictive of the actual structure of the complex.
    • L may be qualitatively predictive of the actual structure of the complex.
  • 70
    • 33846053447 scopus 로고    scopus 로고
    • The other low-energy docked complexes (defined as those having scoring energies within 4 kcal/mol of the lowest energy complex) did not differ greatly from the lowest-energy complex shown in Figure 6. We performed a second round of docking calculations starting with an orientation of 24 in the BH3-binding pocket of Bcl-xL that was rotated ∼180° (i.e, the positions of the N-terminus and C-terminus were swapped) relative to that shown in Figure 6. This experiment resulted in low-energy complexes that had scoring energies > 30 kcal/mol higher than complexes from the first round. All of the low-energy complexes from the second round, however, showed 24 oriented in the BH3-recognition cleft in a manner similar to that in Figure 6 i.e, 24 had rotated ∼180° back to the orientation found in the first round of docking, but side chain/Bcl-xL contacts were diminished due to translation of the oligomer out of the Bcl-xL c
    • L cleft.
  • 72
    • 33846088767 scopus 로고    scopus 로고
    • L stoichiometry was 0.7:1 in the detergent-containing buffer and 1.0:1 in buffer lacking detergent.
    • L stoichiometry was 0.7:1 in the detergent-containing buffer and 1.0:1 in buffer lacking detergent.
  • 82
    • 0029953285 scopus 로고    scopus 로고
    • 3-Amino acid synthesis: (a) Seebach, D.; Overhand, M.; Kuehnle, F. N. M.; Martinoni, B.; Oberer, L.; Hommel, U.; Widmer, H. Helv. Chim. Acta 1996, 79, 913-941.
    • 3-Amino acid synthesis: (a) Seebach, D.; Overhand, M.; Kuehnle, F. N. M.; Martinoni, B.; Oberer, L.; Hommel, U.; Widmer, H. Helv. Chim. Acta 1996, 79, 913-941.
  • 84
    • 0242515860 scopus 로고    scopus 로고
    • 2-Amino acid synthesis: (c) Lee, H.-S.; Park, J.-S.; Kim, B. M.; Gellman, S. H. J. Org. Chem. 2003, 68, 1575-1578.
    • 2-Amino acid synthesis: (c) Lee, H.-S.; Park, J.-S.; Kim, B. M.; Gellman, S. H. J. Org. Chem. 2003, 68, 1575-1578.
  • 85
    • 0035838894 scopus 로고    scopus 로고
    • Cyclic β-amino acid synthesis: (d) LePlae, P. R.; Umezawa, N.; Lee, H.-S.; Gellman, S. H. J. Org. Chem. 2001, 66, 5629.
    • Cyclic β-amino acid synthesis: (d) LePlae, P. R.; Umezawa, N.; Lee, H.-S.; Gellman, S. H. J. Org. Chem. 2001, 66, 5629.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.