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Volumn 2, Issue , 2012, Pages 20-25

Inhibitory effects of choline-O-sulfate on amyloid formation of human islet amyloid polypeptide

Author keywords

Aggregation inhibitor; Amyloid formation; CD; Choline O sulfate; COS; HFIP; HIAPP; Islet amyloid polypeptide; NDSB; Osmolyte; TEM; ThT

Indexed keywords

2 (TRIMETHYLAMMONIO)ETHYLSULFATE; ACETYLCHOLINE; AMYLIN; AMYLOID; BETAINE; CARNITINE; CHOLINE DERIVATIVE; CHOLINE O SULFATE; NDSB 195; NDSB 201; NDSB 211; NDSB 221; NDSB 256; NON DETERGENT SULFOBETAINE DERIVATIVE; THIOFLAVINE; UNCLASSIFIED DRUG;

EID: 84861212656     PISSN: 22115463     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fob.2012.02.001     Document Type: Article
Times cited : (27)

References (45)
  • 1
    • 70350337659 scopus 로고    scopus 로고
    • Role of naturally occurring osmolytes in protein folding and stability
    • Kumar R. Role of naturally occurring osmolytes in protein folding and stability. Arch. Biochem. Biophys. 2009, 491:1-6.
    • (2009) Arch. Biochem. Biophys. , vol.491 , pp. 1-6
    • Kumar, R.1
  • 2
    • 0032855889 scopus 로고    scopus 로고
    • Thermoprotection by glycine betaine and choline
    • Caldas T., Demont-Caulet N., Ghazi A., Richarme G. Thermoprotection by glycine betaine and choline. Microbiology 1999, 145(Pt 9):2543-2548.
    • (1999) Microbiology , vol.145 , Issue.PART 9 , pp. 2543-2548
    • Caldas, T.1    Demont-Caulet, N.2    Ghazi, A.3    Richarme, G.4
  • 3
    • 0033180252 scopus 로고    scopus 로고
    • Extrinsic protein stabilization by the naturally occurring osmolytes β-hydroxyectoine and betaine
    • Knapp S., Ladenstein R., Galinski E.A. Extrinsic protein stabilization by the naturally occurring osmolytes β-hydroxyectoine and betaine. Extremophiles 1999, 3:191-198.
    • (1999) Extremophiles , vol.3 , pp. 191-198
    • Knapp, S.1    Ladenstein, R.2    Galinski, E.A.3
  • 4
    • 0035955743 scopus 로고    scopus 로고
    • Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses
    • Diamant S., Eliahu N., Rosenthal D., Goloubinoff P. Chemical chaperones regulate molecular chaperones in vitro and in cells under combined salt and heat stresses. J. Biol. Chem. 2001, 276:39586-39591.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39586-39591
    • Diamant, S.1    Eliahu, N.2    Rosenthal, D.3    Goloubinoff, P.4
  • 6
    • 0031160039 scopus 로고    scopus 로고
    • Optimizing multiplex and LA-PCR with betaine
    • Hengen P.N. Optimizing multiplex and LA-PCR with betaine. Trends Biochem. Sci. 1997, 22:225-226.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 225-226
    • Hengen, P.N.1
  • 8
    • 0029752741 scopus 로고    scopus 로고
    • Strategy for controlling preferential amplification and avoiding false negatives in PCR typing
    • Weissensteiner T., Lanchbury J.S. Strategy for controlling preferential amplification and avoiding false negatives in PCR typing. Biotechniques 1996, 21:1102-1108.
    • (1996) Biotechniques , vol.21 , pp. 1102-1108
    • Weissensteiner, T.1    Lanchbury, J.S.2
  • 9
    • 66149143156 scopus 로고    scopus 로고
    • The osmolyte betaine promotes protein misfolding and disruption of protein aggregates
    • Natalello A., Liu J., Ami D., Doglia S.M., de Marco A. The osmolyte betaine promotes protein misfolding and disruption of protein aggregates. Proteins 2009, 75:509-517.
    • (2009) Proteins , vol.75 , pp. 509-517
    • Natalello, A.1    Liu, J.2    Ami, D.3    Doglia, S.M.4    de Marco, A.5
  • 10
    • 79251618192 scopus 로고    scopus 로고
    • Protein and DNA destabilization by osmolytes: the other side of the coin
    • Singh L.R., Poddar N.K., Dar T.A., Kumar R., Ahmad F. Protein and DNA destabilization by osmolytes: the other side of the coin. Life Sci. 2011, 88:117-125.
    • (2011) Life Sci. , vol.88 , pp. 117-125
    • Singh, L.R.1    Poddar, N.K.2    Dar, T.A.3    Kumar, R.4    Ahmad, F.5
  • 11
    • 24044483249 scopus 로고    scopus 로고
    • Trehalose differentially inhibits aggregation and neurotoxicity of β-amyloid 40 and 42
    • Liu R., Barkhordarian H., Emadi S., Park C.B., Sierks M.R. Trehalose differentially inhibits aggregation and neurotoxicity of β-amyloid 40 and 42. Neurobiol. Dis. 2005, 20:74-81.
    • (2005) Neurobiol. Dis. , vol.20 , pp. 74-81
    • Liu, R.1    Barkhordarian, H.2    Emadi, S.3    Park, C.B.4    Sierks, M.R.5
  • 12
    • 40249092819 scopus 로고    scopus 로고
    • Inhibition of β-amyloid peptide aggregation and neurotoxicity by α-d-mannosylglycerate, a natural extremolyte
    • Ryu J., Kanapathipillai M., Lentzen G., Park C.B. Inhibition of β-amyloid peptide aggregation and neurotoxicity by α-d-mannosylglycerate, a natural extremolyte. Peptides 2008, 29:578-584.
    • (2008) Peptides , vol.29 , pp. 578-584
    • Ryu, J.1    Kanapathipillai, M.2    Lentzen, G.3    Park, C.B.4
  • 13
    • 24044449002 scopus 로고    scopus 로고
    • Ectoine and hydroxyectoine inhibit aggregation and neurotoxicity of Alzheimer's β-amyloid
    • Kanapathipillai M., Lentzen G., Sierks M., Park C.B. Ectoine and hydroxyectoine inhibit aggregation and neurotoxicity of Alzheimer's β-amyloid. FEBS Lett. 2005, 579:4775-4780.
    • (2005) FEBS Lett. , vol.579 , pp. 4775-4780
    • Kanapathipillai, M.1    Lentzen, G.2    Sierks, M.3    Park, C.B.4
  • 14
    • 78751550063 scopus 로고    scopus 로고
    • Chemical and pharmacological chaperones: application for recombinant protein production and protein folding diseases
    • Rajan R.S., Tsumoto K., Tokunaga M., Tokunaga H., Kita Y., Arakawa T. Chemical and pharmacological chaperones: application for recombinant protein production and protein folding diseases. Curr. Med. Chem. 2011, 18:1-15.
    • (2011) Curr. Med. Chem. , vol.18 , pp. 1-15
    • Rajan, R.S.1    Tsumoto, K.2    Tokunaga, M.3    Tokunaga, H.4    Kita, Y.5    Arakawa, T.6
  • 16
    • 0017397471 scopus 로고
    • Further studies on the formation of choline sulfate by bacteria
    • Fitzgerald J.W., Luschinski P.C. Further studies on the formation of choline sulfate by bacteria. Can. J. Microbiol. 1977, 23:483-490.
    • (1977) Can. J. Microbiol. , vol.23 , pp. 483-490
    • Fitzgerald, J.W.1    Luschinski, P.C.2
  • 17
    • 0008727826 scopus 로고
    • Identification and determination by fast atom bombardment mass spectrometry of the compatible solute choline-O-sulphate in Limonium species and other halophytes
    • Hanson A.D., Gage D.A. Identification and determination by fast atom bombardment mass spectrometry of the compatible solute choline-O-sulphate in Limonium species and other halophytes. Aust. J. Plant Physiol. 1991, 18:317-327.
    • (1991) Aust. J. Plant Physiol. , vol.18 , pp. 317-327
    • Hanson, A.D.1    Gage, D.A.2
  • 18
    • 0000145972 scopus 로고
    • Comparative physiological evidence that β-alanine betaine and choline-O-sulfate act as compatible osmolytes in halophytic Limonium species
    • Hanson A.D., Rathinasabapathi B., Chamberlin B., Gage D.A. Comparative physiological evidence that β-alanine betaine and choline-O-sulfate act as compatible osmolytes in halophytic Limonium species. Plant Physiol. 1991, 97:1199-1205.
    • (1991) Plant Physiol. , vol.97 , pp. 1199-1205
    • Hanson, A.D.1    Rathinasabapathi, B.2    Chamberlin, B.3    Gage, D.A.4
  • 19
  • 20
    • 0027168389 scopus 로고
    • Choline: its role in the growth of filamentous fungi and the regulation of mycelial morphology
    • Markham P., Robson G.D., Bainbridge B.W., Trinci A.P. Choline: its role in the growth of filamentous fungi and the regulation of mycelial morphology. FEMS Microbiol. Rev. 1993, 10:287-300.
    • (1993) FEMS Microbiol. Rev. , vol.10 , pp. 287-300
    • Markham, P.1    Robson, G.D.2    Bainbridge, B.W.3    Trinci, A.P.4
  • 21
    • 0030447841 scopus 로고    scopus 로고
    • Osmoprotectants in Halomonas elongata: high-affinity betaine transport system and choline-betaine pathway
    • Cánovas D., Vargas C., Csonka L.N., Ventosa A., Nieto J.J. Osmoprotectants in Halomonas elongata: high-affinity betaine transport system and choline-betaine pathway. J. Bacteriol. 1996, 178:7221-7226.
    • (1996) J. Bacteriol. , vol.178 , pp. 7221-7226
    • Cánovas, D.1    Vargas, C.2    Csonka, L.N.3    Ventosa, A.4    Nieto, J.J.5
  • 22
    • 0028835463 scopus 로고
    • Isolation and characterization of adenylate kinase (adk) mutations in Salmonella typhimurium which block the ability of glycine betaine to function as an osmoprotectant
    • Gutierrez J.A., Csonka L.N. Isolation and characterization of adenylate kinase (adk) mutations in Salmonella typhimurium which block the ability of glycine betaine to function as an osmoprotectant. J. Bacteriol. 1995, 177:390-400.
    • (1995) J. Bacteriol. , vol.177 , pp. 390-400
    • Gutierrez, J.A.1    Csonka, L.N.2
  • 23
    • 0031963911 scopus 로고    scopus 로고
    • Choline derivatives involved in osmotolerance of Penicillium fellutanum
    • Park Y.I., Gander J.E. Choline derivatives involved in osmotolerance of Penicillium fellutanum. Appl. Environ. Microbiol. 1998, 64:273-278.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 273-278
    • Park, Y.I.1    Gander, J.E.2
  • 24
    • 44649150510 scopus 로고    scopus 로고
    • Recent insights in islet amyloid polypeptide-induced membrane disruption and its role in β-cell death in type 2 diabetes mellitus
    • Khemtemourian L., Killian J.A., Hoppener J.W., Engel M.F. Recent insights in islet amyloid polypeptide-induced membrane disruption and its role in β-cell death in type 2 diabetes mellitus. Exp. Diabetes Res. 2008, 2008:421287.
    • (2008) Exp. Diabetes Res. , vol.2008 , pp. 421287
    • Khemtemourian, L.1    Killian, J.A.2    Hoppener, J.W.3    Engel, M.F.4
  • 25
    • 79954535899 scopus 로고    scopus 로고
    • Islet amyloid polypeptide, islet amyloid, and diabetes mellitus
    • Westermark P., Andersson A., Westermark G.T. Islet amyloid polypeptide, islet amyloid, and diabetes mellitus. Physiol. Rev. 2011, 91:795-826.
    • (2011) Physiol. Rev. , vol.91 , pp. 795-826
    • Westermark, P.1    Andersson, A.2    Westermark, G.T.3
  • 26
    • 0028797534 scopus 로고
    • Non-detergent sulphobetaines: a new class of mild solubilization agents for protein purification
    • Vuillard L., Braun-Breton C., Rabilloud T. Non-detergent sulphobetaines: a new class of mild solubilization agents for protein purification. Biochem. J 1995, 305(Pt 1):337-343.
    • (1995) Biochem. J , vol.305 , Issue.PART 1 , pp. 337-343
    • Vuillard, L.1    Braun-Breton, C.2    Rabilloud, T.3
  • 27
    • 0037438709 scopus 로고    scopus 로고
    • Physical-chemical features of non-detergent sulfobetaines active as protein-folding helpers
    • Expert-Bezançon N., Rabilloud T., Vuillard L., Goldberg M.E. Physical-chemical features of non-detergent sulfobetaines active as protein-folding helpers. Biophys. Chem. 2003, 100:469-479.
    • (2003) Biophys. Chem. , vol.100 , pp. 469-479
    • Expert-Bezançon, N.1    Rabilloud, T.2    Vuillard, L.3    Goldberg, M.E.4
  • 29
    • 0034677739 scopus 로고    scopus 로고
    • Preparation of synthetic human islet amyloid polypeptide (IAPP) in a stable conformation to enable study of conversion to amyloid-like fibrils
    • Higham C.E., Jaikaran E.T., Fraser P.E., Gross M., Clark A. Preparation of synthetic human islet amyloid polypeptide (IAPP) in a stable conformation to enable study of conversion to amyloid-like fibrils. FEBS Lett. 2000, 470:55-60.
    • (2000) FEBS Lett. , vol.470 , pp. 55-60
    • Higham, C.E.1    Jaikaran, E.T.2    Fraser, P.E.3    Gross, M.4    Clark, A.5
  • 30
    • 1842850631 scopus 로고    scopus 로고
    • Inhibition of insulin amyloid formation by small stress molecules
    • Arora A., Ha C., Park C.B. Inhibition of insulin amyloid formation by small stress molecules. FEBS Lett. 2004, 564:121-125.
    • (2004) FEBS Lett. , vol.564 , pp. 121-125
    • Arora, A.1    Ha, C.2    Park, C.B.3
  • 31
    • 0034672122 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis
    • Sreerama N., Venyaminov S.Y., Woody R.W. Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis. Anal. Biochem. 2000, 287:243-251.
    • (2000) Anal. Biochem. , vol.287 , pp. 243-251
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 32
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N., Woody R.W. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 2000, 287:252-260.
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 33
  • 36
    • 77952320068 scopus 로고    scopus 로고
    • Molecular mechanism of Thioflavin-T binding to amyloid fibrils
    • Biancalana M., Koide S. Molecular mechanism of Thioflavin-T binding to amyloid fibrils. Biochim. Biophys. Acta. 2010, 1804:1405-1412.
    • (2010) Biochim. Biophys. Acta. , vol.1804 , pp. 1405-1412
    • Biancalana, M.1    Koide, S.2
  • 38
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism
    • Nielsen L., Khurana R., Coats A., Frokjaer S., Brange J., Vyas S., Uversky V.N., Fink A.L. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry 2001, 40:6036-6046.
    • (2001) Biochemistry , vol.40 , pp. 6036-6046
    • Nielsen, L.1    Khurana, R.2    Coats, A.3    Frokjaer, S.4    Brange, J.5    Vyas, S.6    Uversky, V.N.7    Fink, A.L.8
  • 40
    • 8544272519 scopus 로고    scopus 로고
    • Inhibition of islet amyloid polypeptide fibril formation: a potential role for heteroaromatic interactions
    • Porat Y., Mazor Y., Efrat S., Gazit E. Inhibition of islet amyloid polypeptide fibril formation: a potential role for heteroaromatic interactions. Biochemistry 2004, 43:14454-14462.
    • (2004) Biochemistry , vol.43 , pp. 14454-14462
    • Porat, Y.1    Mazor, Y.2    Efrat, S.3    Gazit, E.4
  • 41
    • 0022032982 scopus 로고
    • The stabilization of proteins by osmolytes
    • Arakawa T., Timasheff S.N. The stabilization of proteins by osmolytes. Biophys. J. 1985, 47:411-414.
    • (1985) Biophys. J. , vol.47 , pp. 411-414
    • Arakawa, T.1    Timasheff, S.N.2
  • 42
    • 0037162456 scopus 로고    scopus 로고
    • Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components
    • Timasheff S.N. Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components. Proc. Natl. Acad. Sci. USA 2002, 99:9721-9726.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9721-9726
    • Timasheff, S.N.1
  • 43
    • 0842304735 scopus 로고    scopus 로고
    • Additive transfer free energies of the peptide backbone unit that are independent of the model compound and the choice of concentration scale
    • Auton M., Bolen D.W. Additive transfer free energies of the peptide backbone unit that are independent of the model compound and the choice of concentration scale. Biochemistry 2004, 43:1329-1342.
    • (2004) Biochemistry , vol.43 , pp. 1329-1342
    • Auton, M.1    Bolen, D.W.2
  • 44
    • 0028862864 scopus 로고
    • The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes
    • Liu Y., Bolen D.W. The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes. Biochemistry 1995, 34:12884-12891.
    • (1995) Biochemistry , vol.34 , pp. 12884-12891
    • Liu, Y.1    Bolen, D.W.2
  • 45
    • 0035958656 scopus 로고    scopus 로고
    • The osmophobic effect: natural selection of a thermodynamic force in protein folding
    • Bolen D.W., Baskakov I.V. The osmophobic effect: natural selection of a thermodynamic force in protein folding. J. Mol. Biol. 2001, 310:955-963.
    • (2001) J. Mol. Biol. , vol.310 , pp. 955-963
    • Bolen, D.W.1    Baskakov, I.V.2


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