메뉴 건너뛰기




Volumn 114, Issue 18, 2017, Pages 4673-4678

Inducing protein aggregation by extensional flow

Author keywords

Aggregation; Antibody; Bioprocessing; Extensional flow; Unfolding

Indexed keywords

BETA 2 MICROGLOBULIN; CYSTEINE; DISULFIDE; GRANULOCYTE COLONY STIMULATING FACTOR; MONOCLONAL ANTIBODY; MONOMER; PROTEIN; BOVINE SERUM ALBUMIN; PROTEIN AGGREGATE;

EID: 85018757082     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1702724114     Document Type: Article
Times cited : (79)

References (48)
  • 1
    • 28244437028 scopus 로고    scopus 로고
    • The Yin and Yang of protein folding
    • Jahn TR, Radford SE (2005) The Yin and Yang of protein folding. FEBS J 272: 5962-5970.
    • (2005) FEBS J , vol.272 , pp. 5962-5970
    • Jahn, T.R.1    Radford, S.E.2
  • 3
    • 33751244556 scopus 로고    scopus 로고
    • Do protein molecules unfold in a simple shear flow?
    • Jaspe J, Hagen SJ (2006) Do protein molecules unfold in a simple shear flow? Biophys J 91:3415-3424.
    • (2006) Biophys J , vol.91 , pp. 3415-3424
    • Jaspe, J.1    Hagen, S.J.2
  • 4
    • 15044359263 scopus 로고    scopus 로고
    • A tensor-based measure for estimating blood damage
    • Arora D, Behr M, Pasquali M (2004) A tensor-based measure for estimating blood damage. Artif Organs 28:1002-1015.
    • (2004) Artif Organs , vol.28 , pp. 1002-1015
    • Arora, D.1    Behr, M.2    Pasquali, M.3
  • 5
    • 33749057744 scopus 로고    scopus 로고
    • Protein aggregation and bioprocessing
    • Cromwell ME, Hilario E, Jacobson F (2006) Protein aggregation and bioprocessing. AAPS J 8:E572-E579.
    • (2006) AAPS J , vol.8 , pp. E572-E579
    • Cromwell, M.E.1    Hilario, E.2    Jacobson, F.3
  • 6
    • 77951498805 scopus 로고    scopus 로고
    • Protein aggregation-pathways and influencing factors
    • Wang W, Nema S, Teagarden D (2010) Protein aggregation-pathways and influencing factors. Int J Pharm 390:89-99.
    • (2010) Int J Pharm , vol.390 , pp. 89-99
    • Wang, W.1    Nema, S.2    Teagarden, D.3
  • 7
    • 79951768234 scopus 로고    scopus 로고
    • Effects of shear on proteins in solution
    • Thomas CR, Geer D (2011) Effects of shear on proteins in solution. Biotechnol Lett 33: 443-456.
    • (2011) Biotechnol Lett , vol.33 , pp. 443-456
    • Thomas, C.R.1    Geer, D.2
  • 8
    • 85018784113 scopus 로고
    • Perfusion culture
    • ed Miller AOA (Springer Netherlands, Dordrecht, The Netherlands)
    • Tolbert W, Prior C (1989) Perfusion culture. Advanced Research on Animal Cell Technology, ed Miller AOA (Springer Netherlands, Dordrecht, The Netherlands), pp 119-145.
    • (1989) Advanced Research On Animal Cell Technology , pp. 119-145
    • Tolbert, W.1    Prior, C.2
  • 9
    • 45149128290 scopus 로고    scopus 로고
    • Current perspectives on stability of protein drug products during formulation, fill and finish operations
    • Rathore N, Rajan RS (2008) Current perspectives on stability of protein drug products during formulation, fill and finish operations. Biotechnol Prog 24:504-514.
    • (2008) Biotechnol Prog , vol.24 , pp. 504-514
    • Rathore, N.1    Rajan, R.S.2
  • 11
    • 80054036751 scopus 로고    scopus 로고
    • Physical degradation of proteins in well-defined fluid flows studied within a four-roll apparatus
    • Simon S, Krause HJ, Weber C, Peukert W (2011) Physical degradation of proteins in well-defined fluid flows studied within a four-roll apparatus. Biotechnol Bioeng 108: 2914-2922.
    • (2011) Biotechnol Bioeng , vol.108 , pp. 2914-2922
    • Simon, S.1    Krause, H.J.2    Weber, C.3    Peukert, W.4
  • 12
  • 14
    • 0016632418 scopus 로고
    • Shear modification of enzyme-kinetics
    • Tirrell M, Middleman S (1975) Shear modification of enzyme-kinetics. Biotechnol Bioeng 17:299-303.
    • (1975) Biotechnol Bioeng , vol.17 , pp. 299-303
    • Tirrell, M.1    Middleman, S.2
  • 15
    • 0018599354 scopus 로고
    • Action of shear on enzymes: Studies with alcohol dehydrogenase
    • Thomas CR, Nienow AW, Dunnill P (1979) Action of shear on enzymes: Studies with alcohol dehydrogenase. Biotechnol Bioeng 21:2263-2278.
    • (1979) Biotechnol Bioeng , vol.21 , pp. 2263-2278
    • Thomas, C.R.1    Nienow, A.W.2    Dunnill, P.3
  • 16
    • 84970973791 scopus 로고    scopus 로고
    • The effect of shear on the structural conformation of rhGH and IgG1 in free solution
    • Brückl L, Schröder T, Scheler S, Hahn R, Sonderegger C (2016) The effect of shear on the structural conformation of rhGH and IgG1 in free solution. J Pharm Sci 105: 1810-1818.
    • (2016) J Pharm Sci , vol.105 , pp. 1810-1818
    • Brückl, L.1    Schröder, T.2    Scheler, S.3    Hahn, R.4    Sonderegger, C.5
  • 17
    • 0026909734 scopus 로고
    • Elongational flow studies on DNA in aqueous solution and stress-induced scission of the double helix
    • Atkins ED, Taylor MA (1992) Elongational flow studies on DNA in aqueous solution and stress-induced scission of the double helix. Biopolymers 32:911-923.
    • (1992) Biopolymers , vol.32 , pp. 911-923
    • Atkins, E.D.1    Taylor, M.A.2
  • 18
    • 33747892234 scopus 로고    scopus 로고
    • Single DNA molecule stretching in sudden mixed shear and elongational microflows
    • Larson JW, et al. (2006) Single DNA molecule stretching in sudden mixed shear and elongational microflows. Lab Chip 6:1187-1199.
    • (2006) Lab Chip , vol.6 , pp. 1187-1199
    • Larson, J.W.1
  • 19
    • 67650812831 scopus 로고    scopus 로고
    • Response of a concentrated monoclonal antibody formulation to high shear
    • Bee JS, et al. (2009) Response of a concentrated monoclonal antibody formulation to high shear. Biotechnol Bioeng 103:936-943.
    • (2009) Biotechnol Bioeng , vol.103 , pp. 936-943
    • Bee, J.S.1
  • 20
    • 34547855540 scopus 로고    scopus 로고
    • Prediction of shear damage of plasmid DNA in pump and centrifuge operations using an ultra scale-down device
    • Zhang H, et al. (2007) Prediction of shear damage of plasmid DNA in pump and centrifuge operations using an ultra scale-down device. Biotechnol Prog 23:858-865.
    • (2007) Biotechnol Prog , vol.23 , pp. 858-865
    • Zhang, H.1
  • 21
    • 84907369365 scopus 로고    scopus 로고
    • Von Willebrand factor, Jedi knight of the bloodstream
    • Springer TA (2014) von Willebrand factor, Jedi knight of the bloodstream. Blood 124: 1412-1425.
    • (2014) Blood , vol.124 , pp. 1412-1425
    • Springer, T.A.1
  • 23
    • 84950129983 scopus 로고    scopus 로고
    • Microfluidic assessment of mechanical cell damage by extensional stress
    • Bae YB, et al. (2016) Microfluidic assessment of mechanical cell damage by extensional stress. Lab Chip 16:96-103.
    • (2016) Lab Chip , vol.16 , pp. 96-103
    • Bae, Y.B.1
  • 24
    • 1842368477 scopus 로고    scopus 로고
    • Single polymer dynamics in an elongational flow
    • Perkins TT, Smith DE, Chu S (1997) Single polymer dynamics in an elongational flow. Science 276:2016-2021.
    • (1997) Science , vol.276 , pp. 2016-2021
    • Perkins, T.T.1    Smith, D.E.2    Chu, S.3
  • 25
    • 84866542720 scopus 로고    scopus 로고
    • Optimized cross-slot flow geometry for microfluidic extensional rheometry
    • Haward SJ, Oliveira MS, Alves MA, McKinley GH (2012) Optimized cross-slot flow geometry for microfluidic extensional rheometry. Phys Rev Lett 109:128301.
    • (2012) Phys Rev Lett , vol.109 , pp. 128301
    • Haward, S.J.1    Oliveira, M.S.2    Alves, M.A.3    McKinley, G.H.4
  • 26
  • 27
    • 34547577829 scopus 로고    scopus 로고
    • Degradation of supercoiled plasmid DNA within a capillary device
    • Meacle FJ, et al. (2007) Degradation of supercoiled plasmid DNA within a capillary device. Biotechnol Bioeng 97:1148-1157.
    • (2007) Biotechnol Bioeng , vol.97 , pp. 1148-1157
    • Meacle, F.J.1
  • 28
    • 84918816295 scopus 로고    scopus 로고
    • Concentrationdependent reversible self-oligomerization of serum albumins through intermolecular β-sheet formation
    • Bhattacharya A, Prajapati R, Chatterjee S, Mukherjee TK (2014) Concentrationdependent reversible self-oligomerization of serum albumins through intermolecular β-sheet formation. Langmuir 30:14894-14904.
    • (2014) Langmuir , vol.30 , pp. 14894-14904
    • Bhattacharya, A.1    Prajapati, R.2    Chatterjee, S.3    Mukherjee, T.K.4
  • 29
    • 79953777946 scopus 로고    scopus 로고
    • PH-Induced conformational isomerization of bovine serum albumin studied by extrinsic and intrinsic protein fluorescence
    • Bhattacharya M, Jain N, Bhasne K, Kumari V, Mukhopadhyay S (2011) pH-Induced conformational isomerization of bovine serum albumin studied by extrinsic and intrinsic protein fluorescence. J Fluoresc 21:1083-1090.
    • (2011) J Fluoresc , vol.21 , pp. 1083-1090
    • Bhattacharya, M.1    Jain, N.2    Bhasne, K.3    Kumari, V.4    Mukhopadhyay, S.5
  • 30
    • 79953805289 scopus 로고    scopus 로고
    • Insights into the mechanism of aggregation and fibril formation from bovine serum albumin
    • Bhattacharya M, Jain N, Mukhopadhyay S (2011) Insights into the mechanism of aggregation and fibril formation from bovine serum albumin. J Phys Chem B 115: 4195-4205.
    • (2011) J Phys Chem B , vol.115 , pp. 4195-4205
    • Bhattacharya, M.1    Jain, N.2    Mukhopadhyay, S.3
  • 31
    • 83455213242 scopus 로고    scopus 로고
    • Bovine serum albumin unfolds in Couette flow
    • Bekard IB, et al. (2012) Bovine serum albumin unfolds in Couette flow. Soft Matter 8: 385-389.
    • (2012) Soft Matter , vol.8 , pp. 385-389
    • Bekard, I.B.1
  • 32
    • 77953291167 scopus 로고    scopus 로고
    • Critical evaluation of Nanoparticle Tracking Analysis (NTA) by NanoSight for the measurement of nanoparticles and protein aggregates
    • Filipe V, Hawe A, Jiskoot W (2010) Critical evaluation of Nanoparticle Tracking Analysis (NTA) by NanoSight for the measurement of nanoparticles and protein aggregates. Pharm Res 27:796-810.
    • (2010) Pharm Res , vol.27 , pp. 796-810
    • Filipe, V.1    Hawe, A.2    Jiskoot, W.3
  • 33
    • 77049124756 scopus 로고    scopus 로고
    • Free-solution, label-free protein-protein interactions characterized by dynamic light scattering
    • Hanlon AD, Larkin MI, Reddick RM (2010) Free-solution, label-free protein-protein interactions characterized by dynamic light scattering. Biophys J 98:297-304.
    • (2010) Biophys J , vol.98 , pp. 297-304
    • Hanlon, A.D.1    Larkin, M.I.2    Reddick, R.M.3
  • 34
    • 84921306354 scopus 로고    scopus 로고
    • Making sense of Brownian motion: Colloid characterization by dynamic light scattering
    • Hassan PA, Rana S, Verma G (2015) Making sense of Brownian motion: Colloid characterization by dynamic light scattering. Langmuir 31:3-12.
    • (2015) Langmuir , vol.31 , pp. 3-12
    • Hassan, P.A.1    Rana, S.2    Verma, G.3
  • 35
    • 84959461812 scopus 로고    scopus 로고
    • A new robust estimator of polydispersity from dynamic light scattering data
    • Roger V, Cottet H, Cipelletti L (2016) A new robust estimator of polydispersity from dynamic light scattering data. Anal Chem 88:2630-2636.
    • (2016) Anal Chem , vol.88 , pp. 2630-2636
    • Roger, V.1    Cottet, H.2    Cipelletti, L.3
  • 36
    • 84886655678 scopus 로고    scopus 로고
    • Structure, folding dynamics, and amyloidogenesis of D76N β2-microglobulin: Roles of shear flow, hydrophobic surfaces, and α-crystallin
    • Mangione PP, et al. (2013) Structure, folding dynamics, and amyloidogenesis of D76N β2-microglobulin: Roles of shear flow, hydrophobic surfaces, and α-crystallin. J Biol Chem 288:30917-30930.
    • (2013) J Biol Chem , vol.288 , pp. 30917-30930
    • Mangione, P.P.1
  • 37
    • 84866984392 scopus 로고    scopus 로고
    • Improved drug-like properties of therapeutic proteins by directed evolution
    • Buchanan A, et al. (2012) Improved drug-like properties of therapeutic proteins by directed evolution. Protein Eng Des Sel 25:631-638.
    • (2012) Protein Eng des Sel , vol.25 , pp. 631-638
    • Buchanan, A.1
  • 38
    • 85007000932 scopus 로고    scopus 로고
    • Engineering the surface properties of a human monoclonal antibody prevents self-association and rapid clearance in vivo
    • Dobson CL, et al. (2016) Engineering the surface properties of a human monoclonal antibody prevents self-association and rapid clearance in vivo. Sci Rep 6:38644.
    • (2016) Sci Rep , vol.6 , pp. 38644
    • Dobson, C.L.1
  • 40
    • 0034702685 scopus 로고    scopus 로고
    • Effect of initial conformation, flow strength, and hydrodynamic interaction on polymer molecules in extensional flows
    • Agarwal US (2000) Effect of initial conformation, flow strength, and hydrodynamic interaction on polymer molecules in extensional flows. J Chem Phys 113:3397-3403.
    • (2000) J Chem Phys , vol.113 , pp. 3397-3403
    • Agarwal, U.S.1
  • 41
    • 0000420940 scopus 로고    scopus 로고
    • Brownian dynamics simulation of a polymer molecule in solution under elongational flow
    • Agarwal US, Bhargava R, Mashelkar RA (1998) Brownian dynamics simulation of a polymer molecule in solution under elongational flow. J Chem Phys 108:1610-1617.
    • (1998) J Chem Phys , vol.108 , pp. 1610-1617
    • Agarwal, U.S.1    Bhargava, R.2    Mashelkar, R.A.3
  • 42
    • 36749109216 scopus 로고
    • Coilstretch transition of dilute flexible polymers under ultrahigh velocity gradients
    • De Gennes PG (1974) Coilstretch transition of dilute flexible polymers under ultrahigh velocity gradients. J Chem Phys 60:5030-5042.
    • (1974) J Chem Phys , vol.60 , pp. 5030-5042
    • De Gennes, P.G.1
  • 43
    • 33750453758 scopus 로고    scopus 로고
    • Stretching of proteins in a uniform flow
    • Szymczak P, Cieplak M (2006) Stretching of proteins in a uniform flow. J Chem Phys 125:164903-164908.
    • (2006) J Chem Phys , vol.125 , pp. 164903-164908
    • Szymczak, P.1    Cieplak, M.2
  • 44
    • 38449119615 scopus 로고    scopus 로고
    • Proteins in a shear flow
    • Szymczak P, Cieplak M (2007) Proteins in a shear flow. J Chem Phys 127: 155106-155107.
    • (2007) J Chem Phys , vol.127 , pp. 155106-155107
    • Szymczak, P.1    Cieplak, M.2
  • 45
    • 84923084610 scopus 로고    scopus 로고
    • Force-induced remodelling of proteins and their complexes
    • Chen Y, Radford SE, Brockwell DJ (2015) Force-induced remodelling of proteins and their complexes. Curr Opin Struct Biol 30:89-99.
    • (2015) Curr Opin Struct Biol , vol.30 , pp. 89-99
    • Chen, Y.1    Radford, S.E.2    Brockwell, D.J.3
  • 46
    • 77952255844 scopus 로고    scopus 로고
    • Elongational flow induces the unfolding of von Willebrand factor at physiological flow rates
    • Sing CE, Alexander-Katz A (2010) Elongational flow induces the unfolding of von Willebrand factor at physiological flow rates. Biophys J 98:L35-L37.
    • (2010) Biophys J , vol.98 , pp. L35-L37
    • Sing, C.E.1    Alexander-Katz, A.2
  • 47
    • 77955983405 scopus 로고    scopus 로고
    • Unravelling the design principles for single protein mechanical strength
    • Crampton N, Brockwell DJ (2010) Unravelling the design principles for single protein mechanical strength. Curr Opin Struct Biol 20:508-517.
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 508-517
    • Crampton, N.1    Brockwell, D.J.2
  • 48
    • 84928963185 scopus 로고    scopus 로고
    • PH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers
    • Tipping KW, et al. (2015) pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers. Proc Natl Acad Sci USA 112:5691-5696.
    • (2015) Proc Natl Acad Sci USA , vol.112 , pp. 5691-5696
    • Tipping, K.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.