Access the full text.
Sign up today, get DeepDyve free for 14 days.
Dafne Müller, Anette Karle, B. Meissburger, I. Höfig, R. Stork, R. Kontermann (2007)
Improved Pharmacokinetics of Recombinant Bispecific Antibody Molecules by Fusion to Human Serum Albumin*Journal of Biological Chemistry, 282
Claudia Bluemel, S. Hausmann, Petra Fluhr, Mirnalini Sriskandarajah, W. Stallcup, P. Baeuerle, P. Kufer (2010)
Epitope distance to the target cell membrane and antigen size determine the potency of T cell-mediated lysis by BiTE antibodies specific for a large melanoma surface antigenCancer Immunology, Immunotherapy, 59
J. Andersen, I. Sandlie (2009)
The versatile MHC class I-related FcRn protects IgG and albumin from degradation: implications for development of new diagnostics and therapeutics.Drug metabolism and pharmacokinetics, 24 4
D. Myszka, T. Morton (1998)
CLAMP: a biosensor kinetic data analysis program.Trends in biochemical sciences, 23 4
T. Morton, D. Myszka (1997)
Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors.Methods in enzymology, 295
Jan Andersen, Muluneh Daba, G. Berntzen, T. Michaelsen, I. Sandlie (2009)
Cross-species Binding Analyses of Mouse and Human Neonatal Fc Receptor Show Dramatic Differences in Immunoglobulin G and Albumin Binding*The Journal of Biological Chemistry, 285
A. Nguyen, A. Reyes, Min Zhang, Paul Mcdonald, W. Wong, L. Damico, M. Dennis (2006)
The pharmacokinetics of an albumin-binding Fab (AB.Fab) can be modulated as a function of affinity for albumin.Protein engineering, design & selection : PEDS, 19 7
R. Kontermann (2010)
Alternative antibody formats.Current opinion in molecular therapeutics, 12 2
A. Jonsson, Jakob Dogan, N. Herne, L. Abrahmsén, P. Nygren (2008)
Engineering of a femtomolar affinity binding protein to human serum albumin.Protein engineering, design & selection : PEDS, 21 8
Maneesh Jain, Neel Kamal, S. Batra (2007)
Engineering antibodies for clinical applications.Trends in biotechnology, 25 7
D. Powers, P. Amersdorfer, M. Poul, U. Nielsen, M. Shalaby, G. Adams, L. Weiner, J. Marks (2001)
Expression of single-chain Fv-Fc fusions in Pichia pastoris.Journal of immunological methods, 251 1-2
C. Chaudhury, Samina Mehnaz, J. Robinson, W. Hayton, D. Pearl, D. Roopenian, C. Anderson (2003)
The Major Histocompatibility Complex–related Fc Receptor for IgG (FcRn) Binds Albumin and Prolongs Its LifespanThe Journal of Experimental Medicine, 197
P. Hinton, Joanna Xiong, Mary Johlfs, M. Tang, Stephen Keller, N. Tsurushita (2006)
An Engineered Human IgG1 Antibody with Longer Serum Half-LifeThe Journal of Immunology, 176
Adam Walker, G. Dunlevy, Daniel Rycroft, P. Topley, Lucy Holt, Tom Herbert, Marie Davies, Fiona Cook, S. Holmes, L. Jespers, C. Herring (2010)
Anti-serum albumin domain antibodies in the development of highly potent, efficacious and long-acting interferon.Protein engineering, design & selection : PEDS, 23 4
C. Chaudhury, C. Brooks, D. Carter, J. Robinson, C. Anderson (2006)
Albumin binding to FcRn: distinct from the FcRn-IgG interaction.Biochemistry, 45 15
Sabrina Trüssel, Christoph Dumelin, Katharina Frey, A. Villa, F. Buller, D. Neri (2009)
New strategy for the extension of the serum half-life of antibody fragments.Bioconjugate chemistry, 20 12
W. Dall'acqua, P. Kiener, Herren Wu (2006)
Properties of Human IgG1s Engineered for Enhanced Binding to the Neonatal Fc Receptor (FcRn)*Journal of Biological Chemistry, 281
M. Johansson, I. Frick, H. Nilsson, P. Kraulis, S. Hober, P. Jonasson, M. Linhult, P. Nygren, M. Uhlén, L. Björck, T. Drakenberg, S. Forsén, M. Wikström (2002)
Structure, Specificity, and Mode of Interaction for Bacterial Albumin-binding Modules*The Journal of Biological Chemistry, 277
D. Colcher, G. Pavlínková, G. Beresford, B. Booth, A. Choudhury, S. Batra (1998)
Pharmacokinetics and biodistribution of genetically-engineered antibodies.The quarterly journal of nuclear medicine : official publication of the Italian Association of Nuclear Medicine (AIMN) [and] the International Association of Radiopharmacology, 42 4
J. Zalevsky, A. Chamberlain, H. Horton, S. Karki, Irene Leung, T. Sproule, G. Lazar, D. Roopenian, J. Desjarlais (2010)
Enhanced antibody half-life improves in vivo activityNature Biotechnology, 28
R. Kontermann (2012)
Strategies to Extend Plasma Half-Lives of Recombinant AntibodiesBioDrugs, 23
V. Kenanova, T. Olafsen, L. Williams, N. Ruel, J. Longmate, P. Yazaki, J. Shively, D. Colcher, A. Raubitschek, A. Wu (2007)
Radioiodinated versus radiometal-labeled anti-carcinoembryonic antigen single-chain Fv-Fc antibody fragments: optimal pharmacokinetics for therapy.Cancer research, 67 2
C. Enever, T. Batuwangala, C. Plummer, A. Sepp (2009)
Next generation immunotherapeutics--honing the magic bullet.Current opinion in biotechnology, 20 4
R. Stork, E. Campigna, B. Robert, Dafne Müller, R. Kontermann (2009)
Biodistribution of a Bispecific Single-chain Diabody and Its Half-life Extended Derivatives*The Journal of Biological Chemistry, 284
Dafne Müller, G. Trunk, A. Sichelstiel, K. Zettlitz, M. Quintanilla, R. Kontermann (2008)
Murine endoglin-specific single-chain Fv fragments for the analysis of vascular targeting strategies in mice.Journal of immunological methods, 339 1
Takuo Suzuki, A. Ishii-Watabe, M. Tada, Tetsu Kobayashi, T. Kanayasu‐Toyoda, T. Kawanishi, Teruhide Yamaguchi (2010)
Importance of Neonatal FcR in Regulating the Serum Half-Life of Therapeutic Proteins Containing the Fc Domain of Human IgG1: A Comparative Study of the Affinity of Monoclonal Antibodies and Fc-Fusion Proteins to Human Neonatal FcRThe Journal of Immunology, 184
Dafne Müller, R. Kontermann (2010)
Bispecific Antibodies for Cancer ImmunotherapyBioDrugs, 24
R. Stork, K. Zettlitz, Dafne Müller, Miriam Rether, F. Hanisch, R. Kontermann (2008)
N-Glycosylation as Novel Strategy to Improve Pharmacokinetic Properties of Bispecific Single-chain Diabodies*Journal of Biological Chemistry, 283
M. Linhult, H. Binz, M. Uhlén, S. Hober (2002)
Mutational analysis of the interaction between albumin‐binding domain from streptococcal protein G and human serum albuminProtein Science, 11
K. Chester, R. Begent, L. Robson, P. Keep, R. Pedley, J. LIBiol, G. Boxer, A. Green, G. Winter, O. Cochet, R. Hawkins (1994)
Phage libraries for generation of clinically useful antibodiesThe Lancet, 343
R. Stork, Dafne Müller, R. Kontermann (2007)
A novel tri-functional antibody fusion protein with improved pharmacokinetic properties generated by fusing a bispecific single-chain diabody with an albumin-binding domain from streptococcal protein G.Protein engineering, design & selection : PEDS, 20 11
C. Benedict, A. Mackrell, W. Anderson (1997)
Determination of the binding affinity of an anti-CD34 single-chain antibody using a novel, flow cytometry based assay.Journal of immunological methods, 201 2
Fusion of small recombinant antibody fragments to an albumin-binding domain (ABD) from streptococcal protein G strongly extends their plasma half-life. This ABD binds with nanomolar affinity to human (HSA) and mouse serum albumin (MSA). It was speculated that an increase in albumin-binding affinity should lead to a further increase in half-life. In the present study, we analyzed the effects of affinity and valency of the ABD on the pharmacokinetic properties of a bispecific single-chain diabody (scDb), applied previously to investigate various half-life extension strategies. The scDb is directed against carcinoembryonic antigen (CEA) and CD3 capable of mediating T cell retargeting to tumor cells. Two scDb derivatives with increased (scDb-ABD-H) and decreased (scDb-ABD-L) affinity as well as an scDb molecule fused to two ABD (scDb-ABD2) were generated and produced in mammalian cells. The altered binding of these constructs to HSA and MSA was confirmed by ELISA and quartz crystal microbalance measurements. All constructs bound efficiently to CEA and CD3-positive cells and were able to activate T cells in a target cell-dependent manner, although T cell activation was reduced in the presence of serum albumin. All three derivatives showed a strongly increased half-life in mice as compared with scDb. Compared with the wild-type scDb-ABD, the half-life of scDb-ABD-H exhibited a prolonged half-life and scDb-ABD-L a reduced half-life, while the half-life scDb-ABD2 was almost identical to that of scDb-ABD. However, these changes were only moderate, indicating that the half-life-extending property of the ABD in mice is only weakly influenced by affinity for serum albumin or valency of albumin binding.
Protein Engineering, Design and Selection – Oxford University Press
Published: Nov 3, 2010
Keywords: albumin-binding domain bispecific antibody carcinoembryonic antigen retargeting single-chain diabody
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.