메뉴 건너뛰기




Volumn 72, Issue , 2013, Pages 150-154

Application of Bio-Layer Interferometry for the analysis of protein/liposome interactions

Author keywords

Bio Layer interferometry; Biosensor; Erythropoietin; Liposomes; Protein membrane interactions

Indexed keywords

2 OLEOYL 1 PALMITOYLPHOSPHATIDYLCHOLINE; DIPALMITOYLPHOSPHATIDYLCHOLINE; IMMOBILIZED PROTEIN; LIPOSOME; PHOSPHATIDYLCHOLINE; RECOMBINANT ERYTHROPOIETIN; STREPTAVIDIN;

EID: 84869002011     PISSN: 07317085     EISSN: 1873264X     Source Type: Journal    
DOI: 10.1016/j.jpba.2012.10.008     Document Type: Article
Times cited : (68)

References (31)
  • 1
    • 70350049076 scopus 로고    scopus 로고
    • Biophysical interactions with model lipid membranes: applications in drug discovery and drug delivery
    • Peetla C., Stine A., Labhasetwar V. Biophysical interactions with model lipid membranes: applications in drug discovery and drug delivery. Mol. Pharm. 2009, 6:1264-1276.
    • (2009) Mol. Pharm. , vol.6 , pp. 1264-1276
    • Peetla, C.1    Stine, A.2    Labhasetwar, V.3
  • 2
    • 0035953319 scopus 로고    scopus 로고
    • Property-based design: optimization of drug absorption and pharmacokinetics
    • van De Waterbeemd H., Smith D.A., Beaumont K., Walker D.K. Property-based design: optimization of drug absorption and pharmacokinetics. J. Med. Chem. 2001, 44:1313-1333.
    • (2001) J. Med. Chem. , vol.44 , pp. 1313-1333
    • van De Waterbeemd, H.1    Smith, D.A.2    Beaumont, K.3    Walker, D.K.4
  • 3
    • 0037457824 scopus 로고    scopus 로고
    • Exploring peptide membrane interaction using surface plasmon resonance: differentiation between pore formation versus membrane disruption by lytic peptides
    • Papo N., Shai Y. Exploring peptide membrane interaction using surface plasmon resonance: differentiation between pore formation versus membrane disruption by lytic peptides. Biochemistry 2003, 42:458-466.
    • (2003) Biochemistry , vol.42 , pp. 458-466
    • Papo, N.1    Shai, Y.2
  • 4
    • 0035524138 scopus 로고    scopus 로고
    • Assessing the absorption of new pharmaceuticals
    • Hidalgo I.J. Assessing the absorption of new pharmaceuticals. Curr. Top. Med. Chem. 2001, 1:385-401.
    • (2001) Curr. Top. Med. Chem. , vol.1 , pp. 385-401
    • Hidalgo, I.J.1
  • 5
    • 0014500594 scopus 로고
    • Antibody binding and complement fixation by a liposomal model membrane
    • Alving C.R., Kinsky S.C., Haxby J.A., Kinsky C.B. Antibody binding and complement fixation by a liposomal model membrane. Biochemistry 1969, 8:1582-1587.
    • (1969) Biochemistry , vol.8 , pp. 1582-1587
    • Alving, C.R.1    Kinsky, S.C.2    Haxby, J.A.3    Kinsky, C.B.4
  • 6
    • 77951296711 scopus 로고    scopus 로고
    • Confocal microscopy of giant vesicles supports the absence of HIV-1 neutralizing 2F5 antibody reactivity to plasma membrane phospholipids
    • Apellaniz B., García-Sáez A.J., Huarte N., Kunert R., Vorauer-Uhl K., Katinger H., Schwille P., Nieva J.L. Confocal microscopy of giant vesicles supports the absence of HIV-1 neutralizing 2F5 antibody reactivity to plasma membrane phospholipids. FEBS Lett. 2010, 584:1591-1596.
    • (2010) FEBS Lett. , vol.584 , pp. 1591-1596
    • Apellaniz, B.1    García-Sáez, A.J.2    Huarte, N.3    Kunert, R.4    Vorauer-Uhl, K.5    Katinger, H.6    Schwille, P.7    Nieva, J.L.8
  • 7
    • 72149134206 scopus 로고    scopus 로고
    • Analysis of cationic liposomes by reversed-phase HPLC with evaporative light-scattering detection
    • Zhong Z., Ji Q., Zhang J.A. Analysis of cationic liposomes by reversed-phase HPLC with evaporative light-scattering detection. J. Pharm. Biomed. Anal. 2010, 51:947-951.
    • (2010) J. Pharm. Biomed. Anal. , vol.51 , pp. 947-951
    • Zhong, Z.1    Ji, Q.2    Zhang, J.A.3
  • 8
    • 2142767300 scopus 로고    scopus 로고
    • Probing the mechanism of drug/lipid membrane interactions using Biacore
    • Abdiche Y.N., Myszka D.G. Probing the mechanism of drug/lipid membrane interactions using Biacore. Anal. Biochem. 2004, 328:233-243.
    • (2004) Anal. Biochem. , vol.328 , pp. 233-243
    • Abdiche, Y.N.1    Myszka, D.G.2
  • 9
    • 84859153398 scopus 로고    scopus 로고
    • Combining label-free technologies: discovery in strength
    • Barbour R., Bova M.P. Combining label-free technologies: discovery in strength. Bioanalysis 2012, 4:619-622.
    • (2012) Bioanalysis , vol.4 , pp. 619-622
    • Barbour, R.1    Bova, M.P.2
  • 10
    • 0036853993 scopus 로고    scopus 로고
    • Surface plasmon resonance characterization of drug/liposome interactions
    • Baird C.L., Courtenay E.S., Myszka D.G. Surface plasmon resonance characterization of drug/liposome interactions. Anal. Biochem. 2002, 310:93-99.
    • (2002) Anal. Biochem. , vol.310 , pp. 93-99
    • Baird, C.L.1    Courtenay, E.S.2    Myszka, D.G.3
  • 11
    • 12244269069 scopus 로고    scopus 로고
    • Biosensor analysis of the interaction between drug compounds and liposomes of different properties; a two-dimensional characterization tool for estimation of membrane absorption
    • Frostell-Karlsson A., Widegren H., Green C.E., Hämäläinen M.D., Westerlund L., Karlsson R., Fenner K., van de Waterbeemd H. Biosensor analysis of the interaction between drug compounds and liposomes of different properties; a two-dimensional characterization tool for estimation of membrane absorption. J. Pharm. Sci. 2005, 94:25-37.
    • (2005) J. Pharm. Sci. , vol.94 , pp. 25-37
    • Frostell-Karlsson, A.1    Widegren, H.2    Green, C.E.3    Hämäläinen, M.D.4    Westerlund, L.5    Karlsson, R.6    Fenner, K.7    van de Waterbeemd, H.8
  • 12
    • 84869004610 scopus 로고    scopus 로고
    • Detection of deoxynivalenol using biolayer interferometry
    • Maragos C.M. Detection of deoxynivalenol using biolayer interferometry. Mycol. Res. 2011, 27:157-165.
    • (2011) Mycol. Res. , vol.27 , pp. 157-165
    • Maragos, C.M.1
  • 13
    • 43049120226 scopus 로고    scopus 로고
    • Determining kinetics and affinities of protein interactions using a parallel real-time label-free biosensor, the Octet
    • Abdiche Y., Malashock D., Pinkerton A., Pons J. Determining kinetics and affinities of protein interactions using a parallel real-time label-free biosensor, the Octet. Anal. Biochem. 2008, 377:209-217.
    • (2008) Anal. Biochem. , vol.377 , pp. 209-217
    • Abdiche, Y.1    Malashock, D.2    Pinkerton, A.3    Pons, J.4
  • 14
    • 0032535149 scopus 로고    scopus 로고
    • Equilibrium analysis of high affinity interactions using BIACORE
    • Myszka D.G., Jonsen M.D., Graves B.J. Equilibrium analysis of high affinity interactions using BIACORE. Anal. Biochem. 1998, 265:326-330.
    • (1998) Anal. Biochem. , vol.265 , pp. 326-330
    • Myszka, D.G.1    Jonsen, M.D.2    Graves, B.J.3
  • 16
    • 53549097076 scopus 로고    scopus 로고
    • Erythropoietin-mediated tissue protection: reducing collateral damage from the primary injury response
    • Brines M., Cerami A. Erythropoietin-mediated tissue protection: reducing collateral damage from the primary injury response. J. Intern. Med. 2008, 264:405-432.
    • (2008) J. Intern. Med. , vol.264 , pp. 405-432
    • Brines, M.1    Cerami, A.2
  • 17
    • 33846239262 scopus 로고    scopus 로고
    • A classical homodimeric erythropoietin receptor is essential for the antiapoptotic effects of erythropoietin on differentiated neuroblastoma SH-SY5Y and pheochromocytoma PC-12 cells
    • Um M., Gross A.W., Lodish H.F. A classical homodimeric erythropoietin receptor is essential for the antiapoptotic effects of erythropoietin on differentiated neuroblastoma SH-SY5Y and pheochromocytoma PC-12 cells. Cell. Signal. 2007, 19:634-645.
    • (2007) Cell. Signal. , vol.19 , pp. 634-645
    • Um, M.1    Gross, A.W.2    Lodish, H.F.3
  • 18
    • 45449104608 scopus 로고    scopus 로고
    • A rapid method for determining dynamic binding capacity of resins for the purification of proteins
    • Do T., Ho F., Heidecker B., Witte K., Chang L., Lerner L. A rapid method for determining dynamic binding capacity of resins for the purification of proteins. Protein Expr. Purif. 2008, 60:147-150.
    • (2008) Protein Expr. Purif. , vol.60 , pp. 147-150
    • Do, T.1    Ho, F.2    Heidecker, B.3    Witte, K.4    Chang, L.5    Lerner, L.6
  • 19
    • 85012373035 scopus 로고
    • Diffusion of univalent ions across the lamellae of swollen phospholipids
    • Bangham A.D., Standish M.M., Watkins J.C. Diffusion of univalent ions across the lamellae of swollen phospholipids. J. Mol. Biol. 1965, 13:238-252.
    • (1965) J. Mol. Biol. , vol.13 , pp. 238-252
    • Bangham, A.D.1    Standish, M.M.2    Watkins, J.C.3
  • 20
    • 0018719041 scopus 로고
    • Preparation of liposomes of defined size distribution by extrusion through polycarbonate membranes
    • Olson F., Hunt C.A., Szoka F.C., Vail W.J., Papahadjopoulos D. Preparation of liposomes of defined size distribution by extrusion through polycarbonate membranes. Biochim. Biophys. Acta 1979, 557:9-23.
    • (1979) Biochim. Biophys. Acta , vol.557 , pp. 9-23
    • Olson, F.1    Hunt, C.A.2    Szoka, F.C.3    Vail, W.J.4    Papahadjopoulos, D.5
  • 21
    • 0030589816 scopus 로고    scopus 로고
    • Preferential labeling of alpha-amino N-terminal groups in peptides by biotin: application to the detection of specific anti-peptide antibodies by enzyme immunoassays
    • Sélo I., Négroni L., Créminon C., Grassi J., Wal J.M. Preferential labeling of alpha-amino N-terminal groups in peptides by biotin: application to the detection of specific anti-peptide antibodies by enzyme immunoassays. J. Immunol. Methods 1996, 199:127-138.
    • (1996) J. Immunol. Methods , vol.199 , pp. 127-138
    • Sélo, I.1    Négroni, L.2    Créminon, C.3    Grassi, J.4    Wal, J.M.5
  • 23
    • 48249146140 scopus 로고    scopus 로고
    • Probing the binding mechanism and affinity of tanezumab, a recombinant humanized anti-NGF monoclonal antibody, using a repertoire of biosensors
    • Abdiche Y.N., Malashock D.S., Pons J. Probing the binding mechanism and affinity of tanezumab, a recombinant humanized anti-NGF monoclonal antibody, using a repertoire of biosensors. Protein Sci. 2008, 17:1326-1335.
    • (2008) Protein Sci. , vol.17 , pp. 1326-1335
    • Abdiche, Y.N.1    Malashock, D.S.2    Pons, J.3
  • 24
    • 14944364973 scopus 로고    scopus 로고
    • The biotin-streptavidin interaction can be reversibly broken using water at elevated temperatures
    • Holmberg A., Blomstergren A., Nord O., Lukacs M., Lundeberg J., Uhlen M. The biotin-streptavidin interaction can be reversibly broken using water at elevated temperatures. Electrophoresis 2005, 26:501-510.
    • (2005) Electrophoresis , vol.26 , pp. 501-510
    • Holmberg, A.1    Blomstergren, A.2    Nord, O.3    Lukacs, M.4    Lundeberg, J.5    Uhlen, M.6
  • 25
    • 0022181816 scopus 로고
    • Membrane lipid composition and cellular function
    • Spector A.A., Yorek M.A. Membrane lipid composition and cellular function. J. Lipid Res. 1985, 26:1015-1035.
    • (1985) J. Lipid Res. , vol.26 , pp. 1015-1035
    • Spector, A.A.1    Yorek, M.A.2
  • 28
    • 0033015372 scopus 로고    scopus 로고
    • Charge pairing of headgroups in phosphatidylcholine membranes: a molecular dynamics simulation study
    • Pasenkiewicz-Gierula M., Takaoka Y., Miyagawa H., Kitamura K., Kusumi A. Charge pairing of headgroups in phosphatidylcholine membranes: a molecular dynamics simulation study. Biophys. J. 1999, 76:1228-1240.
    • (1999) Biophys. J. , vol.76 , pp. 1228-1240
    • Pasenkiewicz-Gierula, M.1    Takaoka, Y.2    Miyagawa, H.3    Kitamura, K.4    Kusumi, A.5
  • 29
    • 0036169327 scopus 로고    scopus 로고
    • Binding of globular proteins to lipid membranes studied by isothermal titration calorimetry and fluorescence
    • Dimitrova M., Matsumura H., Terezova N., Neytchev V. Binding of globular proteins to lipid membranes studied by isothermal titration calorimetry and fluorescence. Colloids Surf. B 2002, 24:53-61.
    • (2002) Colloids Surf. B , vol.24 , pp. 53-61
    • Dimitrova, M.1    Matsumura, H.2    Terezova, N.3    Neytchev, V.4
  • 31
    • 36549031623 scopus 로고    scopus 로고
    • Is phospholipid-saturated alkyl column a convenient replacement for immobilized-artificial-membrane?
    • Luo H.B., Zheng C., Cheng Y.K. Is phospholipid-saturated alkyl column a convenient replacement for immobilized-artificial-membrane?. J. Chromatogr. A 2007, 1176:100-106.
    • (2007) J. Chromatogr. A , vol.1176 , pp. 100-106
    • Luo, H.B.1    Zheng, C.2    Cheng, Y.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.