메뉴 건너뛰기




Volumn 1794, Issue 6, 2009, Pages 913-920

Suppression of lysozyme aggregation at alkaline pH by tri-N-acetylchitotriose

Author keywords

Amyloid fibril; Atomic force microscopy; Enzyme activity; Inhibitor; Protein stabilization; SDS PAGE; Thioflavin T

Indexed keywords

ASPARAGINE; ASPARTIC ACID; EGG WHITE; LYSOZYME; N,N',N''' TRIACETYLCHITOTRIOSE; TRI N ACETYLCHITOTRIOSE; TRIOSE; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 67349219351     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.01.009     Document Type: Article
Times cited : (37)

References (44)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid and human disease
    • Chiti F., and Dobson C.M. Protein misfolding, functional amyloid and human disease. Annu. Rev. Biochem. 75 (2006) 333-366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 10644225416 scopus 로고    scopus 로고
    • Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world
    • Stefani M. Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world. Biochim. Biophys. Acta. 1739 (2004) 5-25
    • (2004) Biochim. Biophys. Acta. , vol.1739 , pp. 5-25
    • Stefani, M.1
  • 3
    • 34547126694 scopus 로고    scopus 로고
    • Novel therapeutic strategies for the treatment of protein-misfolding diseases
    • Rochet J.C. Novel therapeutic strategies for the treatment of protein-misfolding diseases. Exp. Rev. Mol. Med. 9 (2007) 1-34
    • (2007) Exp. Rev. Mol. Med. , vol.9 , pp. 1-34
    • Rochet, J.C.1
  • 4
    • 33644868088 scopus 로고    scopus 로고
    • Developing therapeutics for diseases of protein misfolding
    • May B.C., Govaerts C., and Cohen F.E. Developing therapeutics for diseases of protein misfolding. Neurology 66 Suppl 1 (2006) S118-S122
    • (2006) Neurology , vol.66 , Issue.SUPPL. 1
    • May, B.C.1    Govaerts, C.2    Cohen, F.E.3
  • 5
    • 28244502156 scopus 로고    scopus 로고
    • Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: a focus on the transthyretin amyloidoses
    • Johnson S.M., Wiseman R.L., Sekijima Y., Green N.S., Adamski-Werner S.L., and Kelly J.W. Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: a focus on the transthyretin amyloidoses. Acc. Chem. Res. 38 (2005) 911-921
    • (2005) Acc. Chem. Res. , vol.38 , pp. 911-921
    • Johnson, S.M.1    Wiseman, R.L.2    Sekijima, Y.3    Green, N.S.4    Adamski-Werner, S.L.5    Kelly, J.W.6
  • 6
    • 0037473750 scopus 로고    scopus 로고
    • Prevention of transthyretin amyloid disease by changing protein misfolding energetics
    • Hammarstrom P., Wiseman R.L., Powers E.T., and Kelly J.W. Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science 299 (2003) 713-716
    • (2003) Science , vol.299 , pp. 713-716
    • Hammarstrom, P.1    Wiseman, R.L.2    Powers, E.T.3    Kelly, J.W.4
  • 7
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross C.A., and Poirier M.A. Protein aggregation and neurodegenerative disease. Nature Med. 10 (2004) S10-S17
    • (2004) Nature Med. , vol.10
    • Ross, C.A.1    Poirier, M.A.2
  • 8
    • 3042540232 scopus 로고    scopus 로고
    • Pharmacological chaperones: potential treatment for conformational diseases
    • Bernier V., Lagace M., Bichet D.G., and Bouvier M. Pharmacological chaperones: potential treatment for conformational diseases. Trends Endocrinol. Metab. 15 (2004) 222-228
    • (2004) Trends Endocrinol. Metab. , vol.15 , pp. 222-228
    • Bernier, V.1    Lagace, M.2    Bichet, D.G.3    Bouvier, M.4
  • 9
    • 54049088134 scopus 로고    scopus 로고
    • How do surfactants and DTT affect the size, dynamics, activity and growth of soluble lysozyme aggregates?
    • Kumar S., Ravi V.K., and Swaminathan R. How do surfactants and DTT affect the size, dynamics, activity and growth of soluble lysozyme aggregates?. Biochem. J. 415 (2008) 275-288
    • (2008) Biochem. J. , vol.415 , pp. 275-288
    • Kumar, S.1    Ravi, V.K.2    Swaminathan, R.3
  • 10
    • 34547105186 scopus 로고    scopus 로고
    • Chemical and pharmacological chaperones as new therapeutic agents
    • Loo T.W., and Clarke D.M. Chemical and pharmacological chaperones as new therapeutic agents. Exp. Rev. Mol. Med. 9 (2007) 1-18
    • (2007) Exp. Rev. Mol. Med. , vol.9 , pp. 1-18
    • Loo, T.W.1    Clarke, D.M.2
  • 11
    • 33646008876 scopus 로고    scopus 로고
    • Chemical chaperones: mechanisms of action and potential use
    • Papp E., and Csermely P. Chemical chaperones: mechanisms of action and potential use. Handb Exp. Pharmacol. 172 (2006) 405-416
    • (2006) Handb Exp. Pharmacol. , vol.172 , pp. 405-416
    • Papp, E.1    Csermely, P.2
  • 12
    • 14844361966 scopus 로고    scopus 로고
    • Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation
    • Ray S.S., Nowak R.J., Brown Jr. R.H., and Lansbury Jr. P.T. Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 3639-3644
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 3639-3644
    • Ray, S.S.1    Nowak, R.J.2    Brown Jr., R.H.3    Lansbury Jr., P.T.4
  • 14
    • 33749243722 scopus 로고    scopus 로고
    • Stabilization of a native protein mediated by ligand binding inhibits amyloid formation independently of the aggregation pathway
    • Soldi G., Plakoutsi G., Taddei N., and Chiti F. Stabilization of a native protein mediated by ligand binding inhibits amyloid formation independently of the aggregation pathway. J. Med. Chem. 49 (2006) 6057-6064
    • (2006) J. Med. Chem. , vol.49 , pp. 6057-6064
    • Soldi, G.1    Plakoutsi, G.2    Taddei, N.3    Chiti, F.4
  • 15
    • 23044445857 scopus 로고    scopus 로고
    • A novel therapeutic strategy for polyglutamine diseases by stabilizing aggregation-prone proteins with small molecules
    • Tanaka M., Machida Y., and Nukina N. A novel therapeutic strategy for polyglutamine diseases by stabilizing aggregation-prone proteins with small molecules. J. Mol. Med. 83 (2005) 343-352
    • (2005) J. Mol. Med. , vol.83 , pp. 343-352
    • Tanaka, M.1    Machida, Y.2    Nukina, N.3
  • 17
    • 39349102682 scopus 로고    scopus 로고
    • The formation of amyloid fibrils from proteins in the lysozyme family
    • Trexler A.J., and Nilsson M.R. The formation of amyloid fibrils from proteins in the lysozyme family. Curr. Protein Pept Sci. 8 (2007) 537-557
    • (2007) Curr. Protein Pept Sci. , vol.8 , pp. 537-557
    • Trexler, A.J.1    Nilsson, M.R.2
  • 18
    • 33645211553 scopus 로고    scopus 로고
    • Slow aggregation of lysozyme in alkaline pH monitored in real time employing the fluorescence anisotropy of covalently labeled dansyl probe
    • Homchaudhuri L., Kumar S., and Swaminathan R. Slow aggregation of lysozyme in alkaline pH monitored in real time employing the fluorescence anisotropy of covalently labeled dansyl probe. FEBS Lett. 580 (2006) 2097-2101
    • (2006) FEBS Lett. , vol.580 , pp. 2097-2101
    • Homchaudhuri, L.1    Kumar, S.2    Swaminathan, R.3
  • 19
    • 0032830122 scopus 로고    scopus 로고
    • In vitro immunoglobulin light chain fibrillogenesis
    • Wall J., Murphy C.L., and Solomon A. In vitro immunoglobulin light chain fibrillogenesis. Methods Enzymol. 309 (1999) 204-217
    • (1999) Methods Enzymol. , vol.309 , pp. 204-217
    • Wall, J.1    Murphy, C.L.2    Solomon, A.3
  • 20
    • 0014687514 scopus 로고
    • The dependence of lysozyme activity on pH and ionic strength
    • Davies R.C., Neuberger A., and Wilson B.M. The dependence of lysozyme activity on pH and ionic strength. Biochim. Biophys. Acta 178 (1969) 294-305
    • (1969) Biochim. Biophys. Acta , vol.178 , pp. 294-305
    • Davies, R.C.1    Neuberger, A.2    Wilson, B.M.3
  • 24
    • 0015935370 scopus 로고
    • Temperature and pH dependence of the binding of oligosaccharides to lysozyme
    • Banerjee S.K., and Rupley J.A. Temperature and pH dependence of the binding of oligosaccharides to lysozyme. J. Biol. Chem. 248 (1973) 2117-2124
    • (1973) J. Biol. Chem. , vol.248 , pp. 2117-2124
    • Banerjee, S.K.1    Rupley, J.A.2
  • 25
    • 0026756368 scopus 로고
    • Redesign of the substrate-binding site of hen egg white lysozyme based on the molecular evolution of C-type lysozymes
    • Kumagai I., Sunada F., Takeda S., and Miura K. Redesign of the substrate-binding site of hen egg white lysozyme based on the molecular evolution of C-type lysozymes. J. Biol. Chem. 267 (1992) 4608-4612
    • (1992) J. Biol. Chem. , vol.267 , pp. 4608-4612
    • Kumagai, I.1    Sunada, F.2    Takeda, S.3    Miura, K.4
  • 26
    • 0014354873 scopus 로고
    • Fluorescence spectroscopy of proteins
    • Stryer L. Fluorescence spectroscopy of proteins. Science 162 (1968) 526-533
    • (1968) Science , vol.162 , pp. 526-533
    • Stryer, L.1
  • 27
    • 0027502784 scopus 로고
    • Thioflavin T interaction with synthetic Alzheimer's disease β amyloid peptides: detection of amyloid aggregation in solution
    • LeVine III H. Thioflavin T interaction with synthetic Alzheimer's disease β amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2 (1993) 404-410
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • LeVine III, H.1
  • 28
    • 0014690594 scopus 로고
    • Association sites of lysozyme in solution. The active site
    • Sophianopoulos A.J. Association sites of lysozyme in solution. The active site. J. Biol. Chem. 244 (1969) 3188-3193
    • (1969) J. Biol. Chem. , vol.244 , pp. 3188-3193
    • Sophianopoulos, A.J.1
  • 29
    • 0014791972 scopus 로고
    • Thermochemistry of lysozyme-inhibitor binding
    • Bjurulf C., Laynez J., and Wadso I. Thermochemistry of lysozyme-inhibitor binding. Eur. J. Biochem. 14 (1970) 47-52
    • (1970) Eur. J. Biochem. , vol.14 , pp. 47-52
    • Bjurulf, C.1    Laynez, J.2    Wadso, I.3
  • 30
    • 38449094348 scopus 로고    scopus 로고
    • Different molten globule-like folding intermediates of hen egg white lysozyme induced by high pH and tertiary butanol
    • Hameed M., Ahmad B., Fazili K.M., Andrabi K., and Khan R.H. Different molten globule-like folding intermediates of hen egg white lysozyme induced by high pH and tertiary butanol. J. Biochem. (Tokyo) 141 (2007) 573-583
    • (2007) J. Biochem. (Tokyo) , vol.141 , pp. 573-583
    • Hameed, M.1    Ahmad, B.2    Fazili, K.M.3    Andrabi, K.4    Khan, R.H.5
  • 32
    • 0343003602 scopus 로고
    • Evidence for dimerization of lysozyme in alkaline solution
    • Sophianopoulos A.J., and van Holde K.E. Evidence for dimerization of lysozyme in alkaline solution. J. Biol. Chem. 236 (1961) PC82-PC83
    • (1961) J. Biol. Chem. , vol.236
    • Sophianopoulos, A.J.1    van Holde, K.E.2
  • 35
    • 34548389339 scopus 로고    scopus 로고
    • Heat-induced conversion of β2-microglobulin and hen egg-white lysozyme into amyloid fibrils
    • Sasahara K., Yagi H., Naiki H., and Goto Y. Heat-induced conversion of β2-microglobulin and hen egg-white lysozyme into amyloid fibrils. J. Mol. Biol. 372 (2007) 981-991
    • (2007) J. Mol. Biol. , vol.372 , pp. 981-991
    • Sasahara, K.1    Yagi, H.2    Naiki, H.3    Goto, Y.4
  • 38
    • 0033572725 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on protein folding and aggregation
    • van den Berg B., Ellis R.J., and Dobson C.M. Effects of macromolecular crowding on protein folding and aggregation. EMBO J. 18 (1999) 6927-6933
    • (1999) EMBO J. , vol.18 , pp. 6927-6933
    • van den Berg, B.1    Ellis, R.J.2    Dobson, C.M.3
  • 40
    • 43049096368 scopus 로고    scopus 로고
    • Mixed macromolecular crowding inhibits amyloid formation of hen egg white lysozyme
    • Zhou B.R., Zhou Z., Hu Q.L., Chen J., and Liang Y. Mixed macromolecular crowding inhibits amyloid formation of hen egg white lysozyme. Biochim. Biophys. Acta. 1784 (2008) 472-480
    • (2008) Biochim. Biophys. Acta. , vol.1784 , pp. 472-480
    • Zhou, B.R.1    Zhou, Z.2    Hu, Q.L.3    Chen, J.4    Liang, Y.5
  • 41
    • 36749011905 scopus 로고    scopus 로고
    • Inhibition of amyloid fibrillation of lysozyme by indole derivatives-possible mechanism of action
    • Morshedi D., Rezaei-Ghaleh N., Ebrahim-Habibi A., Ahmadian S., and Nemat-Gorgani M. Inhibition of amyloid fibrillation of lysozyme by indole derivatives-possible mechanism of action. FEBS J. 274 (2007) 6415-6425
    • (2007) FEBS J. , vol.274 , pp. 6415-6425
    • Morshedi, D.1    Rezaei-Ghaleh, N.2    Ebrahim-Habibi, A.3    Ahmadian, S.4    Nemat-Gorgani, M.5
  • 42
    • 33750616210 scopus 로고    scopus 로고
    • Effects of p-benzoquinone and melatonin on amyloid fibrillogenesis of hen egg-white lysozyme
    • Wang S.S.S., Chen P.H., and Hung Y.Tz. Effects of p-benzoquinone and melatonin on amyloid fibrillogenesis of hen egg-white lysozyme. J. Mol. Catal. B: Enzym. 43 (2006) 49-57
    • (2006) J. Mol. Catal. B: Enzym. , vol.43 , pp. 49-57
    • Wang, S.S.S.1    Chen, P.H.2    Hung, Y.Tz.3
  • 43
    • 34250373347 scopus 로고    scopus 로고
    • Inhibition of amyloid fibrillization of hen egg-white lysozymes by rifampicin and p-benzoquinone
    • Lieu V.H., Wu J.W., Wang S.S., and Wu C.H. Inhibition of amyloid fibrillization of hen egg-white lysozymes by rifampicin and p-benzoquinone. Biotechnol. Prog. 23 (2007) 698-706
    • (2007) Biotechnol. Prog. , vol.23 , pp. 698-706
    • Lieu, V.H.1    Wu, J.W.2    Wang, S.S.3    Wu, C.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.