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Volumn 39, Issue 5, 2006, Pages 1159-1165

Chemo-enzymatic synthesis of precursor tetrapeptide Bz-RGDS-NH2 of cellular adhesion motif in low-water organic media

Author keywords

Organic solvents; pH memory; RGDS; Tetrapeptide synthesis; Trypsin

Indexed keywords

ACETYLATION; ENZYMES; ETHANOL; HYDROLYSIS; ORGANIC SOLVENTS; PH EFFECTS; SYNTHESIS (CHEMICAL);

EID: 33745940579     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2006.02.027     Document Type: Article
Times cited : (3)

References (32)
  • 1
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signailing
    • Giancotti F.G., and Ruoslahti E. Integrin signailing. Science 285 (1999) 1028-1032
    • (1999) Science , vol.285 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 3
    • 0027652426 scopus 로고
    • Adhesion molecules and their role in cancer metastasis
    • Lafrenie R.M., Buchanan M.R., and Orr F.W. Adhesion molecules and their role in cancer metastasis. Cell Biophys 23 1-3 (1993) 83-89
    • (1993) Cell Biophys , vol.23 , Issue.1-3 , pp. 83-89
    • Lafrenie, R.M.1    Buchanan, M.R.2    Orr, F.W.3
  • 5
    • 0023637601 scopus 로고
    • New perspectives in cells adhesion RGD and integrins
    • Ruoslahti E., and Pierschbacher M.D. New perspectives in cells adhesion RGD and integrins. Science 238 4826 (1987) 491-497
    • (1987) Science , vol.238 , Issue.4826 , pp. 491-497
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 6
    • 0033985483 scopus 로고    scopus 로고
    • Inhibitory effect of hexapeptide (RGRHGD) on platelet aggregation
    • Wu T.M., Li M.L., and Chou T.C. Inhibitory effect of hexapeptide (RGRHGD) on platelet aggregation. Thromb Res 97 4 (2000) 191-199
    • (2000) Thromb Res , vol.97 , Issue.4 , pp. 191-199
    • Wu, T.M.1    Li, M.L.2    Chou, T.C.3
  • 7
    • 0023609864 scopus 로고
    • Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binging specificity in cell adhesion
    • Pierschbacher M.D., and Ruoslahti E. Influence of stereochemistry of the sequence Arg-Gly-Asp-Xaa on binging specificity in cell adhesion. J Biol Chem 262 (1987) 17294-17298
    • (1987) J Biol Chem , vol.262 , pp. 17294-17298
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 9
    • 2542440603 scopus 로고    scopus 로고
    • RGDS peptide induces caspase 8 and caspase 9 activation in human endothelial cells
    • Aguzzi M.S., Giampietri C., De Marchis F., Padula F., Gaeta R., Ragone G., et al. RGDS peptide induces caspase 8 and caspase 9 activation in human endothelial cells. Blood 103 (2004) 4180-4187
    • (2004) Blood , vol.103 , pp. 4180-4187
    • Aguzzi, M.S.1    Giampietri, C.2    De Marchis, F.3    Padula, F.4    Gaeta, R.5    Ragone, G.6
  • 10
    • 0031589974 scopus 로고    scopus 로고
    • RGD containing peptide trigger apoptosis in glomerular mesangial cells of adult human kidneys
    • Chen X.M., Wang J.Z., Fu B., and Yu L.F. RGD containing peptide trigger apoptosis in glomerular mesangial cells of adult human kidneys. Biochem Biophys Res Co 234 (1997) 594-599
    • (1997) Biochem Biophys Res Co , vol.234 , pp. 594-599
    • Chen, X.M.1    Wang, J.Z.2    Fu, B.3    Yu, L.F.4
  • 11
    • 0034091791 scopus 로고    scopus 로고
    • Glycoprotein IIb/IIIa antagonists induce apoptosis in rat cardiomyocytes by caspase-3 activation
    • Adderley S.R., and Fitzgerard D.J. Glycoprotein IIb/IIIa antagonists induce apoptosis in rat cardiomyocytes by caspase-3 activation. J Biol Chem 275 (2000) 5760-5766
    • (2000) J Biol Chem , vol.275 , pp. 5760-5766
    • Adderley, S.R.1    Fitzgerard, D.J.2
  • 12
    • 0037409617 scopus 로고    scopus 로고
    • Apoptosis by RGD-containing peptides observed in hemocytes of the Pacific oyster, Crassostrea gigas
    • Terahara K., Takahashi K.G., and Mori K. Apoptosis by RGD-containing peptides observed in hemocytes of the Pacific oyster, Crassostrea gigas. Dev Comp Immunol 27 (2003) 521-528
    • (2003) Dev Comp Immunol , vol.27 , pp. 521-528
    • Terahara, K.1    Takahashi, K.G.2    Mori, K.3
  • 13
    • 0033990930 scopus 로고    scopus 로고
    • Application of membrance phase seperation for enzymatic synthesis of aspartame precursor in biphasic reaction system
    • Isono Y., and Nakajima M. Application of membrance phase seperation for enzymatic synthesis of aspartame precursor in biphasic reaction system. Biochem Eng J 4 (2000) 143-147
    • (2000) Biochem Eng J , vol.4 , pp. 143-147
    • Isono, Y.1    Nakajima, M.2
  • 15
    • 0031239642 scopus 로고    scopus 로고
    • Protease-catalyzed synthesis of new hydrophobic dipeptides containing nonproteinogenic amino acids
    • Krix G., Eichhorn U.H., Jakubke H.D., and Kula M.R. Protease-catalyzed synthesis of new hydrophobic dipeptides containing nonproteinogenic amino acids. Enzyme Microb Technol 21 (1997) 252-257
    • (1997) Enzyme Microb Technol , vol.21 , pp. 252-257
    • Krix, G.1    Eichhorn, U.H.2    Jakubke, H.D.3    Kula, M.R.4
  • 16
    • 0028842995 scopus 로고
    • Enzymatic oligopeptide synthesis using a minimal protection strategy: sequential assembly of a growing oligopeptide chain
    • Gill I., López-Fandiño R., Jorba X., and Vulfson E.N. Enzymatic oligopeptide synthesis using a minimal protection strategy: sequential assembly of a growing oligopeptide chain. J Am Chem Soc 117 (1995) 6175-6181
    • (1995) J Am Chem Soc , vol.117 , pp. 6175-6181
    • Gill, I.1    López-Fandiño, R.2    Jorba, X.3    Vulfson, E.N.4
  • 17
    • 0001647456 scopus 로고
    • Efeeects of solvents and additives on the reaction of N-Benzyloxycarbonyl-l-aspartic anhydride with l-Phenylananine methyl ester (synthesis of Aspartame)
    • Yang C.P., and Su C.S. Efeeects of solvents and additives on the reaction of N-Benzyloxycarbonyl-l-aspartic anhydride with l-Phenylananine methyl ester (synthesis of Aspartame). J Org Chem 51 (1986) 5186-5191
    • (1986) J Org Chem , vol.51 , pp. 5186-5191
    • Yang, C.P.1    Su, C.S.2
  • 19
    • 33646682070 scopus 로고
    • The synthesis of peptide in aqueous medium
    • Veber D., Hirschmann R., and Denkewalter R.G. The synthesis of peptide in aqueous medium. J Org Chem 34 3 (1969) 753-754
    • (1969) J Org Chem , vol.34 , Issue.3 , pp. 753-754
    • Veber, D.1    Hirschmann, R.2    Denkewalter, R.G.3
  • 20
    • 0035822751 scopus 로고    scopus 로고
    • Lipase-catalyzed synthesis of RGD amide in aqueous water-miscible organic solvents
    • Zhang L.Q., Zhang Y.D., Xu L., Li X.L., Yang X.C., Xu G., et al. Lipase-catalyzed synthesis of RGD amide in aqueous water-miscible organic solvents. Enzyme Microb Technol 29 (2001) 129-135
    • (2001) Enzyme Microb Technol , vol.29 , pp. 129-135
    • Zhang, L.Q.1    Zhang, Y.D.2    Xu, L.3    Li, X.L.4    Yang, X.C.5    Xu, G.6
  • 22
    • 0034135723 scopus 로고    scopus 로고
    • Protease-catalyzed tripeptide (RGD) synthesis
    • So J.E., Shik J.S., and Kim B.G. Protease-catalyzed tripeptide (RGD) synthesis. Enzyme Microb Technol 26 (2000) 108-114
    • (2000) Enzyme Microb Technol , vol.26 , pp. 108-114
    • So, J.E.1    Shik, J.S.2    Kim, B.G.3
  • 23
  • 24
    • 0035843166 scopus 로고    scopus 로고
    • Improving enzymes by using them in organic solvents
    • Klibanov A.M. Improving enzymes by using them in organic solvents. Nature 409 (2001) 241-246
    • (2001) Nature , vol.409 , pp. 241-246
    • Klibanov, A.M.1
  • 25
    • 0024278258 scopus 로고
    • Enzymatic catalysis in nonaqueous solvents
    • Zaks A., and Klibanov A.M. Enzymatic catalysis in nonaqueous solvents. J Biol Chem 263 (1988) 3194-3201
    • (1988) J Biol Chem , vol.263 , pp. 3194-3201
    • Zaks, A.1    Klibanov, A.M.2
  • 26
    • 0029858946 scopus 로고    scopus 로고
    • pH control of the catalytic activity of cross-linked enzyme crystals in organic solvents
    • Xu K., and Klibanov A.M. pH control of the catalytic activity of cross-linked enzyme crystals in organic solvents. J Am Chem Soc 118 (1996) 9815-9819
    • (1996) J Am Chem Soc , vol.118 , pp. 9815-9819
    • Xu, K.1    Klibanov, A.M.2
  • 27
    • 0023385987 scopus 로고
    • Rule of optimization of biocatalysis in organic solvents
    • Laane C., Boeren S., Vos K., and Veeger C. Rule of optimization of biocatalysis in organic solvents. Biotechnol Bioeng 30 (1987) 81-87
    • (1987) Biotechnol Bioeng , vol.30 , pp. 81-87
    • Laane, C.1    Boeren, S.2    Vos, K.3    Veeger, C.4
  • 28
    • 0000914483 scopus 로고
    • Enzyme reaction in organic solvent
    • Hirata H. Enzyme reaction in organic solvent. Yukagaku 39 (1990) 1003-1013
    • (1990) Yukagaku , vol.39 , pp. 1003-1013
    • Hirata, H.1
  • 29
    • 0024287893 scopus 로고
    • The effect of water on enzyme action in organic media
    • Zaks A., and Klibanov M.A. The effect of water on enzyme action in organic media. J Biol Chem 263 (1988) 8017-8021
    • (1988) J Biol Chem , vol.263 , pp. 8017-8021
    • Zaks, A.1    Klibanov, M.A.2
  • 30
    • 0033819378 scopus 로고    scopus 로고
    • Enzymic peptide synthesis using s microaqueous highly concentrated amino acid mixture
    • Isono Y., and Nakajima M. Enzymic peptide synthesis using s microaqueous highly concentrated amino acid mixture. Process Biochem 26 (2000) 275-278
    • (2000) Process Biochem , vol.26 , pp. 275-278
    • Isono, Y.1    Nakajima, M.2
  • 31
    • 0036669618 scopus 로고    scopus 로고
    • Enzyme activation for nonaqueous media
    • Lee M.Y., and Dordick J.S. Enzyme activation for nonaqueous media. Curr Opin Biotechnol 13 4 (2002) 376-384
    • (2002) Curr Opin Biotechnol , vol.13 , Issue.4 , pp. 376-384
    • Lee, M.Y.1    Dordick, J.S.2
  • 32
    • 0032126858 scopus 로고    scopus 로고
    • Enzymatic synthesis with mainly undissoved substrates at very high concentrations
    • Erbeldinger M., Ni X., and Halling P.J. Enzymatic synthesis with mainly undissoved substrates at very high concentrations. Enzyme Microb Technol 23 (2000) 141-148
    • (2000) Enzyme Microb Technol , vol.23 , pp. 141-148
    • Erbeldinger, M.1    Ni, X.2    Halling, P.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.