References
- Carter PJ, Lazar GA. Next generation antibody drugs: pursuit of the ‘high-hanging fruit’. Nat Rev Drug Discov. 2017;17:197–11.
- Lagassé HAD, Alexaki A, Simhadri VL, Katagiri NH, Jankowski W, Sauna ZE, Kimchi-Sarfaty C. Recent advances in (therapeutic protein) drug development. F1000Res. 2017;6:113. doi:https://doi.org/10.12688/f1000research.9970.1.
- Ward ES, Gussow D, Griffiths AD, Jones PT, Winter G. Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli. Nature. 1989;341:544–46. doi:https://doi.org/10.1038/341544a0.
- Jespers L, Schon O, Famm K, Winter G. Aggregation-resistant domain antibodies selected on phage by heat denaturation. Nat Biotechnol. 2004;22:1161–65. doi:https://doi.org/10.1038/nbt1000.
- Sheridan C. Ablynx’s nanobody fragments go places antibodies cannot. Nat Biotechnol. 2017;35:1115. doi:https://doi.org/10.1038/nbt1217-1115.
- Ellerman D. Bispecific T-cell engagers: towards understanding variables influencing the in vitro potency and tumor selectivity and their modulation to enhance their efficacy and safety. Methods. 2019;154:102–17. doi:https://doi.org/10.1016/j.ymeth.2018.10.026.
- Wensel D, Sun Y, Li Z, Zhang S, Picarillo C, McDonagh T, Fabrizio D, Cockett M, Krystal M, Davis J, et al. Discovery and characterization of a novel CD4-binding adnectin with potent anti-HIV activity. Antimicrob Agents Chemother. 2017;61:e00508–17. doi:https://doi.org/10.1128/AAC.00508-17.
- Plückthun A. Designed Ankyrin Repeat Proteins (DARPins): binding proteins for research, diagnostics, and therapy. Annu Rev Pharmacol Toxicol. 2015;55:489–511. doi:https://doi.org/10.1146/annurev-pharmtox-010611-134654.
- Rothe C, Skerra A. Anticalin(®) proteins as therapeutic agents in human diseases. BioDrugs. 2018;32:233–43. doi:https://doi.org/10.1007/s40259-018-0278-1.
- Boudousquie C, Bossi G, Hurst JM, Rygiel KA, Jakobsen BK, Hassan NJ. Polyfunctional response by ImmTAC (IMCgp100) redirected CD8(+) and CD4(+) T cells. Immunology. 2017;152:425–38. doi:https://doi.org/10.1111/imm.12779.
- Morgan P, Van Der Graaf PH, Arrowsmith J, Feltner DE, Drummond KS, Wegner CD, Street SDA. Can the flow of medicines be improved? Fundamental pharmacokinetic and pharmacological principles toward improving phase II survival. Drug Discov Today. 2012;17:419–24.
- Rippe B, Haraldsson B. Transport of macromolecules across microvascular walls: the two-pore theory. Physiol Rev. 1994;74:163–219. doi:https://doi.org/10.1152/physrev.1994.74.1.163.
- Sepp A, Berges A, Sanderson A, Meno-Tetang G. Development of a physiologically based pharmacokinetic model for a domain antibody in mice using the two-pore theory. J Pharmacokinet Pharmacodyn. 2015;42:97–109. doi:https://doi.org/10.1007/s10928-014-9402-0.
- Sepp A, Meno-Tetang G, Weber A, Sanderson A, Schon O, Berges A. Computer-assembled cross-species/cross-modalities two-pore physiologically based pharmacokinetic model for biologics in mice and rats. J Pharmacokinet Pharmacodyn. 2019;46:339–59. doi:https://doi.org/10.1007/s10928-019-09640-9.
- Thorneloe KS, Sepp A, Zhang S, Galinanes-Garcia L, Galette P, Al-Azzam W, Vugts DJ, van Dongen G, Elsinga P, Wiegers J, et al. The biodistribution and clearance of AlbudAb, a novel biopharmaceutical medicine platform, assessed via PET imaging in humans. EJNMMI Res. 2019;9:45. doi:https://doi.org/10.1186/s13550-019-0514-9.
- Kim J, Hayton WL, Robinson JM, Anderson CL. Kinetics of FcRn-mediated recycling of IgG and albumin in human: pathophysiology and therapeutic implications using a simplified mechanism-based model. Clin Immunol. 2007;122:146–55. doi:https://doi.org/10.1016/j.clim.2006.09.001.
- Waldmann TA, Strober W. Metabolism of immunoglobulins. Prog Allergy. 1969;13:1–110.
- Waldmann TA, Terry WD. Familial hypercatabolic hypoproteinemia. A disorder of endogenous catabolism of albumin and immunoglobulin. J Clin Invest. 1990;86:2093–98. doi:https://doi.org/10.1172/JCI114947.
- Wani MA, Haynes LD, Kim J, Bronson CL, Chaudhury C, Mohanty S, Waldmann TA, Robinson JM, Anderson CL. Familial hypercatabolic hypoproteinemia caused by deficiency of the neonatal Fc receptor, FcRn, due to a mutant β2-microglobulin gene. Proc Natl Acad Sci USA. 2006;103:5084–89. doi:https://doi.org/10.1073/pnas.0600548103.
- Lobo ED, Hansen RJ, Balthasar JP. Antibody pharmacokinetics and pharmacodynamics. J Pharm Sci. 2004;93:2645–68. doi:https://doi.org/10.1002/jps.20178.
- Fan -Y-Y, Avery LB, Wang M, O’Hara DM, Leung S, Neubert H. Tissue expression profile of human neonatal Fc receptor (FcRn) in Tg32 transgenic mice. mAbs. 2016;8:848–53. doi:https://doi.org/10.1080/19420862.2016.1178436.
- Cameron J, Sleep D, Sandlie I, Andersen JT Pharmacokinetic animal model. WO 2014/125082, Google Patents; 2014.
- Beeken WL, Volwiler W, Goldsworthy PD, Garby LE, Reynolds WE, Stogsdill R, Stemler RS. Studies of I-131-albumin catabolism and distribution in normal young male adults. J Clin Invest. 1962;41:1312–33. doi:https://doi.org/10.1172/JCI104594.
- Anderson CL, Chaudhury C, Kim J, Bronson CL, Wani MA, Mohanty S. Perspective – fcRn transports albumin: relevance to immunology and medicine. Trends Immunol. 2006;27:343–48. doi:https://doi.org/10.1016/j.it.2006.05.004.
- Levitt DG, Levitt MD. Human serum albumin homeostasis: a new look at the roles of synthesis, catabolism, renal and gastrointestinal excretion, and the clinical value of serum albumin measurements. Int J Gen Med. 2016;9:229–55. doi:https://doi.org/10.2147/IJGM.S102819.
- Vincent J-L, Russell JA, Jacob M, Martin G, Guidet B, Wernerman J, Roca R, McCluskey SA, Gattinoni L. Albumin administration in the acutely ill: what is new and where next? Crit Care. 2014;18:231. doi:https://doi.org/10.1186/cc13991.
- Tojo A, Kinugasa S. Mechanisms of glomerular albumin filtration and tubular reabsorption. Int J Nephrol. 2012;2012:9. doi:https://doi.org/10.1155/2012/481520.
- Norden AGW, Lapsley M, Lee PJ, Pusey CD, Scheinman SJ, Tam FWK, Thakker RV, Unwin RJ, Wrong O. Glomerular protein sieving and implications for renal failure in Fanconi syndrome. Kidney Int. 2001;60:1885–92. doi:https://doi.org/10.1046/j.1523-1755.2001.00016.x.
- Rutili G, Arfors K-E. Protein concentration in interstitial and lymphatic fluids from the subcutaneous tissue. Acta Physiol Scand. 1977;99:1–8. doi:https://doi.org/10.1111/j.1748-1716.1977.tb10345.x.
- Morgan P, Brown DG, Lennard S, Anderton MJ, Barrett JC, Eriksson U, Fidock M, Hamrén B, Johnson A, March RE, et al. Impact of a five-dimensional framework on R&D productivity at AstraZeneca. Nat Rev Drug Discov. 2018;17:167–181.
- Bayliss MK, Butler J, Feldman PL, Green DVS, Leeson PD, Palovich MR, Taylor AJ. Quality guidelines for oral drug candidates: dose, solubility and lipophilicity. Drug Discov Today. 2016;21:1719–27. doi:https://doi.org/10.1016/j.drudis.2016.07.007.
- Petitcollin A, Bensalem A, Verdier M-C, Tron C, Lemaitre F, Paintaud G, Bellissant E, Ternant D. Modelling of the time-varying pharmacokinetics of therapeutic monoclonal antibodies: a literature review. Clin Pharmacokinet. 2020;59:37–49. doi:https://doi.org/10.1007/s40262-019-00816-7.
- Shah DK, Betts AM. Towards a platform PBPK model to characterize the plasma and tissue disposition of monoclonal antibodies in preclinical species and human. J Pharmacokinet Pharmacodyn. 2012;39:67–86. doi:https://doi.org/10.1007/s10928-011-9232-2.
- Nguyen A, Reyes AE, Zhang M, McDonald P, Wong WLT, Damico LA, Dennis MS. The pharmacokinetics of an albumin-binding Fab (AB.Fab) can be modulated as a function of affinity for albumin. Protein Eng Des Sel. 2006;19:291–97. doi:https://doi.org/10.1093/protein/gzl011.
- Hoefman S, Ottevaere I, Baumeister J, Sargentini-Maier ML. Pre-clinical intravenous serum pharmacokinetics of albumin binding and non-half-life extended nanobodies®. Antibodies. 2015;4:141–56. doi:https://doi.org/10.3390/antib4030141.
- Holt LJ, Basran A, Jones K, Chorlton J, Jespers LS, Brewis ND, Tomlinson IM. Anti-serum albumin domain antibodies for extending the half-lives of short lived drugs. Protein Eng Des Sel. 2008;21:283–88. doi:https://doi.org/10.1093/protein/gzm067.
- Herring C, Schon O. AlbudAb™ technology platform–versatile albumin binding domains for the development of therapeutics with tunable half-lives. Therapeutic Proteins: Wiley-VCH Verlag GmbH & Co. KGaA; 2012. p. 249–68.
- Rothschild MA, Bauman A, Yalow RS, Berson SA. Tissue distribution of I131 labeled human serum albumin following intravenous administration. J Clin Invest. 1955;34:1354–58. doi:https://doi.org/10.1172/JCI103183.
- Ellmerer M, Schaupp L, Brunner GA, Sendlhofer G, Wutte A, Wach P, Pieber TR. Measurement of interstitial albumin in human skeletal muscle and adipose tissue by open-flow microperfusion. Am J Physiol Endocrinol Metab. 2000;278:E352–E6. doi:https://doi.org/10.1152/ajpendo.2000.278.2.E352.
- Hladky SB, Barrand MA. Mechanisms of fluid movement into, through and out of the brain: evaluation of the evidence. Fluids Barriers CNS. 2014;11:26. doi:https://doi.org/10.1186/2045-8118-11-26.
- Andersen JT, Daba MB, Berntzen G, Michaelsen TE, Sandlie I. Cross-species binding analyses of mouse and human neonatal fc receptor show dramatic differences in immunoglobulin G and albumin binding. J Biol Chem. 2010;285:4826–36. doi:https://doi.org/10.1074/jbc.M109.081828.
- Andersen JT, Cameron J, Plumridge A, Evans L, Sleep D, Sandlie I. Single-chain variable fragment albumin fusions bind the neonatal Fc receptor (FcRn) in a species dependent manner: implications for in vivo half-life evaluation of albumin-fusion therapeutics. J Biol Chem. 2013;288:24277–85. doi:https://doi.org/10.1074/jbc.M113.463000.
- Andersen JT, Dalhus B, Viuff D, Thue Ravn B, Gunnarsen KS, Plumridge A, Bunting K, Antunes F, Williamson R, Athwal S, et al. Extending serum half-life of albumin by engineering FcRn binding. J Biol Chem. 2014;289:13492–502. doi:https://doi.org/10.1074/jbc.M114.549832.
- Viuff D, Antunes F, Evans L, Cameron J, Dyrnesli H, Thue Ravn B, Stougaard M, Thiam K, Andersen B, Kjærulff S, et al. Generation of a double transgenic humanized neonatal Fc receptor (FcRn)/albumin mouse to study the pharmacokinetics of albumin-linked drugs. J Controlled Release. 2016;223:22–30. doi:https://doi.org/10.1016/j.jconrel.2015.12.019.
- Nilsen J, Bern M, Sand KMK, Grevys A, Dalhus B, Sandlie I, Andersen JT. Human and mouse albumin bind their respective neonatal Fc receptors differently. Sci Rep. 2018;8:14648. doi:https://doi.org/10.1038/s41598-018-32817-0.
- Gambhir SS. Molecular imaging of cancer with positron emission tomography. Nat Rev Cancer. 2002;2:683. doi:https://doi.org/10.1038/nrc882.
- Lamberts LE, Williams SP, Terwisscha van Scheltinga AGT, Lub-de Hooge MN, Schröder CP, Gietema JA, Brouwers AH, de Vries EGE. Antibody positron emission tomography imaging in anticancer drug development. J Clin Oncol. 2015;33:1491–504. doi:https://doi.org/10.1200/JCO.2014.57.8278.
- van Dongen GAMS, Vosjan MJWD. Immuno-positron emission tomography: shedding light on clinical antibody therapy. Cancer Biother Radiopharm. 2010;25:375–85. doi:https://doi.org/10.1089/cbr.2010.0812.
- Deri MA, Zeglis BM, Francesconi LC, Lewis JS. PET imaging with ⁸⁹Zr: from radiochemistry to the clinic. Nucl Med Biol. 2013;40:3–14. doi:https://doi.org/10.1016/j.nucmedbio.2012.08.004.
- Vosjan MJWD, Perk LR, Visser GWM, Budde M, Jurek P, Kiefer GE, van Dongen GAMS. Conjugation and radiolabeling of monoclonal antibodies with zirconium-89 for PET imaging using the bifunctional chelate p-isothiocyanatobenzyl-desferrioxamine. Nat Protoc. 2010;5:739. doi:https://doi.org/10.1038/nprot.2010.13.
- Holland JP, Divilov V, Bander NH, Smith-Jones PM, Larson SM, Lewis JS. 89Zr-DFO-J591 for immunopet of prostate-specific membrane antigen expression in vivo. J Nucl Med. 2010;51:1293–300. doi:https://doi.org/10.2967/jnumed.110.076174.
- Haraldsson B, Nystrom J, Deen WM. Properties of the glomerular barrier and mechanisms of proteinuria. Physiol Rev. 2008;88:451–87. doi:https://doi.org/10.1152/physrev.00055.2006.
- Haraldsson B, Jeansson M. Glomerular filtration barrier. Curr Opin Nephrol Hypertens. 2009;18:331–35. doi:https://doi.org/10.1097/MNH.0b013e32832c9dba.
- Comper WD, Deen WM, Haraldsson B. Resolved: normal glomeruli filter nephrotic levels of albumin. J Am Soc Nephrol. 2008;19:427–32. doi:https://doi.org/10.1681/ASN.2007090997.
- Raavé R, Sandker G, Adumeau P, Jacobsen CB, Mangin F, Meyer M, Moreau M, Bernhard C, Da Costa L, Dubois A, et al. Direct comparison of the in vitro and in vivo stability of DFO, DFO* and DFOcyclo* for 89Zr-immunoPET. Eur J Nucl Med Mol Imaging. 2019;46:1966–77. doi:https://doi.org/10.1007/s00259-019-04343-2.
- Meijs WE, Herscheid JDM, Haisma HJ, Pinedo HM. Evaluation of desferal as a bifunctional chelating agent for labeling antibodies with Zr-89. Int J Rad Appl Instrum A. 1992;43:1443–47. doi:https://doi.org/10.1016/0883-2889(92)90170-J.
- Bensch F, Smeenk MM, van Es SC, de Jong JR, Schröder CP, Oosting SF, Lub-de Hooge MN, Menke-van der Houven van Oordt CW, Brouwers AH, Boellaard R, et al. Comparative biodistribution analysis across four different 89Zr-monoclonal antibody tracers-the first step towards an imaging warehouse. Theranostics. 2018;8:4295–304. doi:https://doi.org/10.7150/thno.26370.
- Nakada T, Kwee IL. Fluid dynamics inside the brain barrier: current concept of interstitial flow, glymphatic flow, and cerebrospinal fluid circulation in the brain. Neuroscientist. 2018;25:155–66. doi:https://doi.org/10.1177/1073858418775027.
- Chang H-Y, Wu S, Meno-Tetang G, Shah DK. A translational platform PBPK model for antibody disposition in the brain. J Pharmacokinet Pharmacodyn. 2019;46:319–38. doi:https://doi.org/10.1007/s10928-019-09641-8.
- Iacob SA, Iacob DG. Ibalizumab targeting CD4 receptors, an emerging molecule in HIV therapy. Front Microbiol. 2017;8:2323. doi:https://doi.org/10.3389/fmicb.2017.02323.
- Song R, Franco D, Kao C-Y, Yu F, Huang Y, Ho DD. Epitope mapping of ibalizumab, a humanized anti-CD4 monoclonal antibody with anti-HIV-1 activity in infected patients. J Virol. 2010;84:6935–42. doi:https://doi.org/10.1128/JVI.00453-10.
- Jacobson JM, Kuritzkes DR, Godofsky E, DeJesus E, Larson JA, Weinheimer SP, Lewis ST. Safety, pharmacokinetics, and antiretroviral activity of multiple doses of ibalizumab (formerly TNX-355), an anti-CD4 monoclonal antibody, in human immunodeficiency virus type 1-infected adults. Antimicrob Agents Chemother. 2009;53:450–57. doi:https://doi.org/10.1128/AAC.00942-08.
- Wong JK, Yukl SA. Tissue reservoirs of HIV. Curr Opin HIV AIDS. 2016;11:362–70. doi:https://doi.org/10.1097/COH.0000000000000293.
- Ganusov VV. Strong inference in mathematical modeling: a method for robust science in the twenty-first century. Front Microbiol. 2016;7. doi:https://doi.org/10.3389/fmicb.2016.01131.
- Graf JF, Scholz BJ, Zavodszky MI. BioDMET: a physiologically based pharmacokinetic simulation tool for assessing proposed solutions to complex biological problems. J Pharmacokinet Pharmacodyn. 2012;39:37–54. doi:https://doi.org/10.1007/s10928-011-9229-x.
- Wiig H, Gyenge C, Iversen PO, Gullberg D, Tenstad O. The role of the extracellular matrix in tissue distribution of macromolecules in normal and pathological tissues: potential therapeutic consequences. Microcirculation. 2008;15:283–96. doi:https://doi.org/10.1080/10739680701671105.
- Garg A, Balthasar J. Physiologically-based pharmacokinetic (PBPK) model to predict IgG tissue kinetics in wild-type and FcRn-knockout mice. J Pharmacokinet Pharmacodyn. 2007;34:687–709. doi:https://doi.org/10.1007/s10928-007-9065-1.
- Hansen RJ, Balthasar JP. Pharmacokinetic/pharmacodynamic modeling of the effects of intravenous immunoglobulin on the disposition of antiplatelet antibodies in a rat model of immune thrombocytopenia. J Pharm Sci. 2003;92:1206–15. doi:https://doi.org/10.1002/jps.10364.