Exploration of backbone space in foldamers containing α- and β-amino acid residues: Developing protease-resistant oligomers that bind tightly to the BH3-recognition cleft of Bcl-xL

ChemBioChem

Volumn 8, Issue 8, 2007, Pages 903-916

  Sadowsky, Jack D ^a   Murray, Justin K ^a   Tomita, York ^b   Gellman, Samuel H ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

^b GEORGETOWN UNIVERSITY   (United States)

Author keywords

Foldamers; Helical structures; Parallel synthesis; Peptidomimetics; Protein protein interactions

Indexed keywords

ALPHA AMINO ACID; BETA AMINO ACID; BH3 PROTEIN; CARBON; CHYMOTRYPSIN; OLIGOMER; PRONASE; PROTEIN BCL XL; PROTEINASE; TRYPSIN; AMINO ACID; BAX PROTEIN (53 86); BAX PROTEIN (53-86); ONCOPROTEIN; PEPTIDE FRAGMENT; PEPTIDE HYDROLASE; PEPTIDE LIBRARY; PROTEIN BCL X; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; APOPTOSIS; ARTICLE; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; FLUORESCENCE POLARIZATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MOLECULAR RECOGNITION; MUTATIONAL ANALYSIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN CROSS LINKING; PROTEIN DEGRADATION; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; BINDING COMPETITION; CHEMICAL STRUCTURE; CHEMISTRY; PROTEIN FOLDING; TIME;

AMINO ACIDS; BCL-X PROTEIN; BINDING SITES; BINDING, COMPETITIVE; MOLECULAR STRUCTURE; PEPTIDE FRAGMENTS; PEPTIDE HYDROLASES; PEPTIDE LIBRARY; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTO-ONCOGENE PROTEINS; TIME FACTORS;

EID: 34447558127     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.200600546     Document Type: Article

References (13)

1. a) M. R. Arkin, J. A. Wells, Nat. Rev. Drug Discovery 2004, 3, 301-317;
2. b) A. G. Cochran, Chem. Biol. 2000, 7, R85-R94;
3. c) T. R. Gadek, J. B. Nicholas, Biochem. Pharmacol. 2003, 65, 1-8;
4. d) T. Berg, Angew. Chem. 2003, 115, 2566-2586;
5. Angew. Chem. Int. Ed. 2003, 42, 2462-2481;
6. e) H. Yin, A. D. Hamilton, Angew. Chem. 2005, 44, 4200-4235;
7. Angew. Chem. Int. Ed. 2005, 44, 4130-4163;
8. f) J. K. Murray, S. H. Gellman, Biopolymers (Pept. Sci.) 2007; DOI 10.002/bip 20741.
9. a) W. E. Stites, Chem. Rev. 1997, 97, 1233-1250;
10. b) A. A. Bogan, K. S. Thorn, J. Mol. Biol. 1998, 280, 1-9.
11. a) C. Thanos, M. Randal, J. A. Wells, J. Am. Chem. Soc. 2003, 125, 15 280-15 281;
12. b) L. T. Vassilev, B. T. Vu, B. Graves, D. Carvajal, F. Podlaski, Z. Filipovic, N. Kong, U. Kammlott, C. Lukacs, C. Klein, N. Fotouhi, E. A. Liu, Science 2004, 303, 844-848;
13. c) K. Ding, Y. Lu, Z. Nikolovska-Coleska, G. Wang, S. Qiu, S. Shangary, W. Gao, D. Qin, J. Stuckey, K. Krajewski, P. P. Roller, S. Wang, J. Med. Chem. 2006, 49, 3432-3435;