메뉴 건너뛰기




Volumn 161, Issue 2, 2012, Pages 121-125

Mirror image phage display - Generating stable therapeutically and diagnostically active peptides with biotechnological means

Author keywords

D enantiomeric peptide; Drug discovery; Mirror image phage display; Pharmaceutical biotechnology

Indexed keywords

ACTIVE PEPTIDES; BIOTECHNOLOGICAL APPROACHES; DRUG DEVELOPMENT; DRUG DISCOVERY; EARLY DIAGNOSIS; IN-VIVO; MIRROR IMAGES; PHAGE DISPLAY; PHARMACEUTICAL BIOTECHNOLOGY;

EID: 84864609470     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2012.05.019     Document Type: Article
Times cited : (24)

References (52)
  • 2
    • 0031695197 scopus 로고    scopus 로고
    • Projections of Alzheimer's disease in the United States and the public health impact of delaying disease onset
    • Brookmeyer R., Gray S., Kawas C. Projections of Alzheimer's disease in the United States and the public health impact of delaying disease onset. American Journal of Public Health 1998, 88:1337-1342.
    • (1998) American Journal of Public Health , vol.88 , pp. 1337-1342
    • Brookmeyer, R.1    Gray, S.2    Kawas, C.3
  • 5
    • 0033791223 scopus 로고    scopus 로고
    • Synthesis of native proteins by chemical ligation
    • Dawson P.E., Kent S.B. Synthesis of native proteins by chemical ligation. Annual Review of Biochemistry 2000, 69:923-960.
    • (2000) Annual Review of Biochemistry , vol.69 , pp. 923-960
    • Dawson, P.E.1    Kent, S.B.2
  • 6
    • 0027944205 scopus 로고
    • Synthesis of proteins by native chemical ligation
    • Dawson P.E., Muir T.W., Clark-Lewis I., Kent S.B. Synthesis of proteins by native chemical ligation. Science 1994, 266:776-779.
    • (1994) Science , vol.266 , pp. 776-779
    • Dawson, P.E.1    Muir, T.W.2    Clark-Lewis, I.3    Kent, S.B.4
  • 7
    • 0028100458 scopus 로고
    • Kunitz domain inhibitors of tissue factor-factor VIIa. II. Potent and specific inhibitors by competitive phage selection
    • Dennis M.S., Lazarus R.A. Kunitz domain inhibitors of tissue factor-factor VIIa. II. Potent and specific inhibitors by competitive phage selection. Journal of Biological Chemistry 1994, 269:22137-22144.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 22137-22144
    • Dennis, M.S.1    Lazarus, R.A.2
  • 8
    • 0025004285 scopus 로고
    • Random peptide libraries: a source of specific protein binding molecules
    • Devlin J.J., Panganiban L.C., Devlin P.E. Random peptide libraries: a source of specific protein binding molecules. Science 1990, 249:404-406.
    • (1990) Science , vol.249 , pp. 404-406
    • Devlin, J.J.1    Panganiban, L.C.2    Devlin, P.E.3
  • 9
    • 0027167443 scopus 로고
    • A comparison of the immunogenicity of a pair of enantiomeric proteins
    • Dintzis H.M., Symer D.E., Dintzis R.Z., Zawadzke L.E., Berg J.M. A comparison of the immunogenicity of a pair of enantiomeric proteins. Proteins 1993, 16:306-308.
    • (1993) Proteins , vol.16 , pp. 306-308
    • Dintzis, H.M.1    Symer, D.E.2    Dintzis, R.Z.3    Zawadzke, L.E.4    Berg, J.M.5
  • 10
    • 0027946232 scopus 로고
    • Isolation of a peptide antagonist to the thrombin receptor using phage display
    • Doorbar J., Winter G. Isolation of a peptide antagonist to the thrombin receptor using phage display. Journal of Molecular Biology 1994, 244:361-369.
    • (1994) Journal of Molecular Biology , vol.244 , pp. 361-369
    • Doorbar, J.1    Winter, G.2
  • 12
    • 0033214895 scopus 로고    scopus 로고
    • Inhibiting HIV-1 entry: discovery of d-peptide inhibitors that target the gp41 coiled-coil pocket
    • Eckert D.M., Malashkevich V.N., Hong L.H., Carr P.A., Kim P.S. Inhibiting HIV-1 entry: discovery of d-peptide inhibitors that target the gp41 coiled-coil pocket. Cell 1999, 99:103-115.
    • (1999) Cell , vol.99 , pp. 103-115
    • Eckert, D.M.1    Malashkevich, V.N.2    Hong, L.H.3    Carr, P.A.4    Kim, P.S.5
  • 14
    • 84856450292 scopus 로고    scopus 로고
    • Peptides for therapy and diagnosis of Alzheimer's disease
    • Funke S.A., Willbold D. Peptides for therapy and diagnosis of Alzheimer's disease. Current Pharmaceutical Design 2012, 18:755-767.
    • (2012) Current Pharmaceutical Design , vol.18 , pp. 755-767
    • Funke, S.A.1    Willbold, D.2
  • 15
    • 0028243847 scopus 로고
    • Applications of combinatorial technologies to drug discovery. 1. Background and peptide combinatorial libraries
    • Gallop M.A., Barrett R.W., Dower W.J., Fodor S.P., Gordon E.M. Applications of combinatorial technologies to drug discovery. 1. Background and peptide combinatorial libraries. Journal of Medicinal Chemistry 1994, 37:1233-1251.
    • (1994) Journal of Medicinal Chemistry , vol.37 , pp. 1233-1251
    • Gallop, M.A.1    Barrett, R.W.2    Dower, W.J.3    Fodor, S.P.4    Gordon, E.M.5
  • 16
    • 84855217314 scopus 로고    scopus 로고
    • Distribution and binding of (18)F-labeled and (125)I-labeled analogues of ACI-80, a prospective molecular imaging biomarker of disease: a whole hemisphere post mortem autoradiography study in human brains obtained from Alzheimer's disease patients
    • Gulyas B., Spenger C., Beliczai Z., Gulya K., Kasa P., Jahan M., Jia Z., Weber U., Pfeifer A., Muhs A., Willbold D., Halldin C. Distribution and binding of (18)F-labeled and (125)I-labeled analogues of ACI-80, a prospective molecular imaging biomarker of disease: a whole hemisphere post mortem autoradiography study in human brains obtained from Alzheimer's disease patients. Neurochemistry international 2012, 60:153-162.
    • (2012) Neurochemistry international , vol.60 , pp. 153-162
    • Gulyas, B.1    Spenger, C.2    Beliczai, Z.3    Gulya, K.4    Kasa, P.5    Jahan, M.6    Jia, Z.7    Weber, U.8    Pfeifer, A.9    Muhs, A.10    Willbold, D.11    Halldin, C.12
  • 17
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy J., Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002, 297:353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 19
    • 84858159538 scopus 로고    scopus 로고
    • Fluorine-18 labeling of three novel d-peptides by conjugation with N-succinimidyl-4-[(18)F]fluorobenzoate and preliminary examination by postmortem whole-hemisphere human brain autoradiography
    • Jahan M., Nag S., Krasikova R., Weber U., Muhs A., Pfeifer A., Spenger C., Willbold D., Gulyas B., Halldin C. Fluorine-18 labeling of three novel d-peptides by conjugation with N-succinimidyl-4-[(18)F]fluorobenzoate and preliminary examination by postmortem whole-hemisphere human brain autoradiography. Nuclear Medicine and Biology 2012, 39:315-323.
    • (2012) Nuclear Medicine and Biology , vol.39 , pp. 315-323
    • Jahan, M.1    Nag, S.2    Krasikova, R.3    Weber, U.4    Muhs, A.5    Pfeifer, A.6    Spenger, C.7    Willbold, D.8    Gulyas, B.9    Halldin, C.10
  • 20
    • 62449282062 scopus 로고    scopus 로고
    • Total chemical synthesis of proteins
    • Kent S.B. Total chemical synthesis of proteins. Chemical Society Reviews 2009, 38:338-351.
    • (2009) Chemical Society Reviews , vol.38 , pp. 338-351
    • Kent, S.B.1
  • 22
    • 0027267959 scopus 로고
    • Selection of peptides binding to the alpha 5 beta 1 integrin from phage display library
    • Koivunen E., Gay D.A., Ruoslahti E. Selection of peptides binding to the alpha 5 beta 1 integrin from phage display library. Journal of Biological Chemistry 1993, 268:20205-20210.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 20205-20210
    • Koivunen, E.1    Gay, D.A.2    Ruoslahti, E.3
  • 23
    • 18544362088 scopus 로고    scopus 로고
    • Synthesis of solid-supported mirror-image sugars: a novel method for selecting receptors for cellular-surface carbohydrates
    • Kozlov I.A., Mao S., Xu Y., Huang X., Lee L., Sears P.S., Gao C., Coyle A.R., Janda K.D., Wong C.H. Synthesis of solid-supported mirror-image sugars: a novel method for selecting receptors for cellular-surface carbohydrates. Chembiochem 2001, 2:741-746.
    • (2001) Chembiochem , vol.2 , pp. 741-746
    • Kozlov, I.A.1    Mao, S.2    Xu, Y.3    Huang, X.4    Lee, L.5    Sears, P.S.6    Gao, C.7    Coyle, A.R.8    Janda, K.D.9    Wong, C.H.10
  • 24
    • 77952413110 scopus 로고    scopus 로고
    • Transport of Alzheimer disease amyloid-beta-binding d-amino acid peptides across an in vitro blood-brain barrier model
    • Liu H., Funke S.A., Willbold D. Transport of Alzheimer disease amyloid-beta-binding d-amino acid peptides across an in vitro blood-brain barrier model. Rejuvenation Research 2010, 13:210-213.
    • (2010) Rejuvenation Research , vol.13 , pp. 210-213
    • Liu, H.1    Funke, S.A.2    Willbold, D.3
  • 27
    • 74949094904 scopus 로고    scopus 로고
    • Aptamers: from bench side research towards patented molecules with therapeutic applications
    • Majumder P., Gomes K.N., Ulrich H. Aptamers: from bench side research towards patented molecules with therapeutic applications. Expert Opinion on Therapeutic Patents 2009, 19:1603-1613.
    • (2009) Expert Opinion on Therapeutic Patents , vol.19 , pp. 1603-1613
    • Majumder, P.1    Gomes, K.N.2    Ulrich, H.3
  • 29
    • 33845611951 scopus 로고    scopus 로고
    • Modeling the therapeutic efficacy of p53 restoration in tumors
    • Martins C.P., Brown-Swigart L., Evan G.I. Modeling the therapeutic efficacy of p53 restoration in tumors. Cell 2006, 127:1323-1334.
    • (2006) Cell , vol.127 , pp. 1323-1334
    • Martins, C.P.1    Brown-Swigart, L.2    Evan, G.I.3
  • 31
    • 0026686436 scopus 로고
    • Total chemical synthesis of a d-enzyme: the enantiomers of HIV-1 protease show reciprocal chiral substrate specificity
    • Milton R.C., Milton S.C., Kent S.B. Total chemical synthesis of a d-enzyme: the enantiomers of HIV-1 protease show reciprocal chiral substrate specificity. Science 1992, 256:1445-1448.
    • (1992) Science , vol.256 , pp. 1445-1448
    • Milton, R.C.1    Milton, S.C.2    Kent, S.B.3
  • 40
    • 0025112794 scopus 로고
    • Searching for peptide ligands with an epitope library
    • Scott J.K., Smith G.P. Searching for peptide ligands with an epitope library. Science 1990, 249:386-390.
    • (1990) Science , vol.249 , pp. 386-390
    • Scott, J.K.1    Smith, G.P.2
  • 41
    • 0032839878 scopus 로고    scopus 로고
    • Plaque busters: strategies to inhibit amyloid formation in Alzheimer's disease
    • Soto C. Plaque busters: strategies to inhibit amyloid formation in Alzheimer's disease. Molecular Medicine Today 1999, 5:343-350.
    • (1999) Molecular Medicine Today , vol.5 , pp. 343-350
    • Soto, C.1
  • 42
    • 33645800972 scopus 로고    scopus 로고
    • RNA aptamers: from basic science towards therapy
    • Ulrich H. RNA aptamers: from basic science towards therapy. Handbook of Experimental Pharmacology 2006, 305-326.
    • (2006) Handbook of Experimental Pharmacology , pp. 305-326
    • Ulrich, H.1
  • 43
    • 60849108336 scopus 로고    scopus 로고
    • In vitro and in vivo staining characteristics of small, fluorescent, Abeta42-binding d-enantiomeric peptides in transgenic AD mouse models
    • van Groen T., Kadish I., Wiesehan K., Funke S.A., Willbold D. In vitro and in vivo staining characteristics of small, fluorescent, Abeta42-binding d-enantiomeric peptides in transgenic AD mouse models. ChemMedChem 2009, 4:276-282.
    • (2009) ChemMedChem , vol.4 , pp. 276-282
    • van Groen, T.1    Kadish, I.2    Wiesehan, K.3    Funke, S.A.4    Willbold, D.5
  • 44
    • 57549085740 scopus 로고    scopus 로고
    • Reduction of Alzheimer's disease amyloid plaque load in transgenic mice by D3, A d-enantiomeric peptide identified by mirror image phage display
    • van Groen T., Wiesehan K., Funke S.A., Kadish I., Nagel-Steger L., Willbold D. Reduction of Alzheimer's disease amyloid plaque load in transgenic mice by D3, A d-enantiomeric peptide identified by mirror image phage display. ChemMedChem 2008, 3:1848-1852.
    • (2008) ChemMedChem , vol.3 , pp. 1848-1852
    • van Groen, T.1    Wiesehan, K.2    Funke, S.A.3    Kadish, I.4    Nagel-Steger, L.5    Willbold, D.6
  • 49
    • 0041467577 scopus 로고    scopus 로고
    • Selection of d-amino-acid peptides that bind to Alzheimer's disease amyloid peptide abeta1-42 by mirror image phage display
    • Wiesehan K., Buder K., Linke R.P., Patt S., Stoldt M., Unger E., Schmitt B., Bucci E., Willbold D. Selection of d-amino-acid peptides that bind to Alzheimer's disease amyloid peptide abeta1-42 by mirror image phage display. Chembiochem 2003, 4:748-753.
    • (2003) Chembiochem , vol.4 , pp. 748-753
    • Wiesehan, K.1    Buder, K.2    Linke, R.P.3    Patt, S.4    Stoldt, M.5    Unger, E.6    Schmitt, B.7    Bucci, E.8    Willbold, D.9
  • 50
    • 41149162218 scopus 로고    scopus 로고
    • Inhibition of cytotoxicity and amyloid fibril formation by a d-amino acid peptide that specifically binds to Alzheimer's disease amyloid peptide
    • Wiesehan K., Stohr J., Nagel-Steger L., van Groen T., Riesner D., Willbold D. Inhibition of cytotoxicity and amyloid fibril formation by a d-amino acid peptide that specifically binds to Alzheimer's disease amyloid peptide. Protein Engineering Design & Selection 2008, 21:241-246.
    • (2008) Protein Engineering Design & Selection , vol.21 , pp. 241-246
    • Wiesehan, K.1    Stohr, J.2    Nagel-Steger, L.3    van Groen, T.4    Riesner, D.5    Willbold, D.6
  • 51
    • 0141683549 scopus 로고    scopus 로고
    • Mirror-image phage display: aiming at the mirror
    • Wiesehan K., Willbold D. Mirror-image phage display: aiming at the mirror. Chembiochem 2003, 811-815.
    • (2003) Chembiochem , pp. 811-815
    • Wiesehan, K.1    Willbold, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.