Rescue of misfolded proteins and stabilization by small molecules

Methods in Molecular Biology

Volumn 648, Issue , 2010, Pages 313-324

  Stevens, Raymond C ^a   Sancho, Javier ^a   Martinez, Aurora ^a  

^a NONE

Author keywords

Compound libraries; Cytoplasmatic and membrane proteins; Denaturation; Experimental screening; High throughput; Melting temperature; Microscale fluorescence; Misfolding diseases; Protein stability; Thermal shift

Indexed keywords

CHAPERONE; MEMBRANE PROTEIN; LIGAND;

BINDING AFFINITY; CONTROLLED STUDY; FLUORESCENCE; GENETIC TRANSCRIPTION; HIGH THROUGHPUT SCREENING; IN VITRO STUDY; NONHUMAN; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN MISFOLDING; PROTEIN STABILITY; PROTEIN SYNTHESIS; RNA TRANSLATION; ARTICLE; BIOASSAY; DRUG EFFECT; FLUOROMETRY; METABOLISM; METHODOLOGY; MOLECULAR LIBRARY; SOLUBILITY; TEMPERATURE;

BIOLOGICAL ASSAY; FLUORESCENCE; FLUOROMETRY; HIGH-THROUGHPUT SCREENING ASSAYS; LIGANDS; MEMBRANE PROTEINS; PROTEIN BIOSYNTHESIS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; SMALL MOLECULE LIBRARIES; SOLUBILITY; TEMPERATURE; TRANSCRIPTION, GENETIC;

EID: 79952035065     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-60761-756-3_22     Document Type: Chapter

References (25)

1. Sanchez-Ruiz JM (2007) Ligand effects on protein thermodynamic stability. Biophys Chem 126:43–49
2. Cremades N, Sancho J, Freire E (2006) The native-state ensemble of proteins provides clues for folding, misfolding and function. Trends Biochem Sci 31:494–496
3. Maclean DS, Qian Q, Middaugh CR (2002) Stabilization of proteins by low molecular weight multi-ions. J Pharm Sci 91:2220–2229
4. Meyer JD, Ho B, Manning MC (2002) Effects of conformation on the chemical stability of pharmaceutically relevant polypeptides. Pharm Biotechnol 13:85–107
5. Ericsson UB, Hallberg BM, Detitta GT, Dekker N, Nordlund P (2006) Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal Biochem 357:289–298
6. Niesen FH, Berglund H, Vedadi M (2007) The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nat Protoc 2:2212–2221
7. Alexandrov AI, Mileni M, Chien EY, Hanson MA, Stevens RC (2008) Microscale fluorescent thermal stability assay for membrane proteins. Structure 16:351–359
8. Nayar R, Manning MC (2002) High throughput formulation: strategies for rapid development of stable protein products. Pharm Biotechnol 13:177–198
9. Ulloa-Aguirre A, Janovick JA, Brothers SP, Conn PM (2004) Pharmacologic rescue of conformationally-defective proteins: implications for the treatment of human disease. Traffic 5:821–837
10. Loo TW, Clarke DM (2007) Chemical and pharmacological chaperones as new therapeutic agents. Expert Rev Mol Med 9:1–18
11. Pedemonte N, Lukacs GL, Du K, Caci E, Zegarra-Moran O, Galietta LJ, Verkman AS (2005) Small-molecule correctors of defective DeltaF508-CFTR cellular processing identified by high-throughput screening. J Clin Invest 115:2564–2571
12. Tropak MB, Blanchard JE, Withers SG, Brown ED, Mahuran D (2007) High-throughput screening for human lysosomal beta-N-Acetyl hexosaminidase inhibitors acting as pharmacological chaperones. Chem Biol 14:153–164
13. Pey AL, Ying M, Cremades N, Velazquez-Campoy A, Scherer T, Thony B, Sancho J, Martinez A (2008) Identification of pharmacological chaperones as potential therapeutic agents to treat phenylketonuria. J Clin Invest 118:2858–2867
14. McInnes C (2007) Virtual screening strategies in drug discovery. Curr Opin Chem Biol 11:494–502
15. Tanrikulu Y, Schneider G (2008) Pseudoreceptor models in drug design: bridging ligand-and receptor-based virtual screening. Nat Rev Drug Discov 7:667–677
16. Hanson MA, Cherezov V, Griffith MT, Roth CB, Jaakola VP, Chien EY, Velasquez J, Kuhn P, Stevens RC (2008) A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor. Structure 16:897–905
17. Desviat LR, Perez B, Ugarte M (2003) Investigation of folding and degradation of in vitro synthesized mutant proteins in the cytosol. Methods Mol Biol 232:257–263
18. Martinez A, Calvo AC, Teigen K, Pey AL (2008) Chapter 3 Rescuing proteins of low kinetic stability by chaperones and natural ligands: phenylketonuria, a case study. Prog Nucleic Acid Res Mol Biol 83:89–134
19. Hanson MA, Stevens RC (2009) Discovery of new GPCR biology: one receptor structure at a time. Structure 17:8–14
20. Martínez A, Knappskog PM, Olafsdottir S, Døskeland AP, Eiken HG, Svebak RM, Bozzini M, Apold J, Flatmark T (1995) Expression of recombinant human phenylalanine hydroxylase as fusion protein in Escherichia coli circumvents proteolytic degradation by host cell proteases Isolation and characterization of the wild-type enzyme. Biochem J 306:589–597
21. Rosenbaum DM, Cherezov V, Hanson MA, Rasmussen SG, Thian FS, Kobilka TS, Choi HJ, Yao XJ, Weis WI, Stevens RC, Kobilka BK (2007) GPCR engineering yields high-resolution structural insights into beta2-adrenergic receptor function. Science 318:1266–1273
22. Irun MP, Maldonado S, Sancho J (2001) Stabilization of apoflavodoxin by replacing hydrogen-bonded charged Asp or Glu residues by the neutral isosteric Asn or Gln. Protein Eng 14:173–181
23. Senisterra GA, Soo Hong B, Park HW, Vedadi M (2008) Application of high-throughput isothermal denaturation to assess protein stability and screen for ligands. J Biomol Screen 13:337–342
24. Thony B, Calvo AC, Scherer T, Svebak RM, Haavik J, Blau N, Martinez A (2008) Tetrahydrobiopterin shows chaperone activity for tyrosine hydroxylase. J Neurochem 106:672–681
25. Thony B, Ding Z, Martinez A (2004) Tetrahydrobiopterin protects phenylalanine hydroxylase activity in vivo: implications for tetrahydrobiopterin-responsive hyperphenyla-laninemia. FEBS Lett 577:507–511