References
- Peters T Jr., Stewart AJ. Albumin research in the 21st century. Biochim Biophys Acta. 2013;1830(12):5351–17. doi:https://doi.org/10.1016/j.bbagen.2013.05.012.
- Fanali G, Di Masi A, Trezza V, Marino M, Fasano M, Ascenzi P. Human serum albumin: from bench to bedside. Mol Aspects Med. 2012;33(3):209–90. doi:https://doi.org/10.1016/j.mam.2011.12.002.
- Merlot AM, Kalinowski DS, Richardson DR. Unraveling the mysteries of serum albumin-more than just a serum protein. Front Physiol. 2014;5:299. doi:https://doi.org/10.3389/fphys.2014.00299.
- Liu H, Moynihan KD, Zheng Y, Szeto GL, Li AV, Huang B, Van Egeren DS, Park C, Irvine DJ. Structure-based programming of lymph-node targeting in molecular vaccines. Nature. 2014;507(7493):519–22. doi:https://doi.org/10.1038/nature12978.
- Chen N, Brachmann C, Liu X, Pierce DW, Dey J, Kerwin WS, Li Y, Zhou S, Hou S, Carleton M, et al. Albumin-bound nanoparticle (nab) paclitaxel exhibits enhanced paclitaxel tissue distribution and tumor penetration. Cancer Chemother Pharmacol. 2015;76(4):699–712. doi:https://doi.org/10.1007/s00280-015-2833-5.
- Chaudhury C, Mehnaz S, Robinson JM, Hayton WL, Pearl DK, Roopenian DC, Anderson CL. The major histocompatibility complex–related Fc receptor for IgG (FcRn) binds Albumin and prolongs its lifespan. J Exp Med. 2003;197(3):315–22. doi:https://doi.org/10.1084/jem.20021829.
- Wang Y, Lang L, Huang P, Wang Z, Jacobson O, Kiesewetter DO, Ali IU, Teng G, Niu G, Chen X, et al. In vivo albumin labeling and lymphatic imaging. Proc Natl Acad Sci U S A. 2015;112(1):208–13. doi:https://doi.org/10.1073/pnas.1414821112.
- Peek MC, Charalampoudis P, Anninga B, Baker R, Douek M. Blue dye for identification of sentinel nodes in breast cancer and malignant melanoma: a systematic review and meta-analysis. Future Oncology. 2017;13(5):455–67. doi:https://doi.org/10.2217/fon-2016-0255.
- Ma WW, Hidalgo M. The winning formulation: the development of paclitaxel in pancreatic cancer. Clin Cancer Res. 2013;19(20):5572–79. doi:https://doi.org/10.1158/1078-0432.CCR-13-1356.
- Maeda H, Matsumura Y. EPR effect based drug design and clinical outlook for enhanced cancer chemotherapy. Adv Drug Deliv Rev. 2011;63(3):129–30. doi:https://doi.org/10.1016/j.addr.2010.05.001.
- Porporato PE. Understanding cachexia as a cancer metabolism syndrome. Oncogenesis. 2016;5:e200. doi:https://doi.org/10.1038/oncsis.2016.3.
- Stehle G, Sinn H, Wunder A, Schrenk HH, Stewart JCM, Hartung G, Maier-Borst W, Heene DL. Plasma protein (albumin) catabolism by the tumor itself–implications for tumor metabolism and the genesis of cachexia. Crit Rev Oncol Hematol. 1997;26(2):77–100. doi:https://doi.org/10.1016/S1040-8428(97)00015-2.
- Hanahan D, Weinberg RA. Hallmarks of cancer: the next generation. Cell. 2011;144(5):646–74. doi:https://doi.org/10.1016/j.cell.2011.02.013.
- Commisso C, Davidson SM, Soydaner-Azeloglu RG, Parker SJ, Kamphorst JJ, Hackett S, Grabocka E, Nofal M, Drebin JA, Thompson CB, et al. Macropinocytosis of protein is an amino acid supply route in Ras-transformed cells. Nature. 2013;497(7451):633–37. doi:https://doi.org/10.1038/nature12138.
- Davidson SM, Jonas O, Keibler MA, Hou HW, Luengo A, Mayers JR, Wyckoff J, Del Rosario AM, Whitman M, Chin CR, et al. Direct evidence for cancer-cell-autonomous extracellular protein catabolism in pancreatic tumors. Nat Med. 2017;23(2):235–41. doi:https://doi.org/10.1038/nm.4256.
- Swiercz R, Mo M, Khare P, Schneider Z, Ober RJ, Ward ES. Loss of expression of the recycling receptor, FcRn, promotes tumor cell growth by increasing albumin consumption. Oncotarget. 2017;8(2):3528–41. doi:https://doi.org/10.18632/oncotarget.13869.
- Chlenski A, Cohn SL. Modulation of matrix remodeling by SPARC in neoplastic progression. Semin Cell Dev Biol. 2010;21(1):55–65. doi:https://doi.org/10.1016/j.semcdb.2009.11.018.
- Yu IS, Cheung WY. A contemporary review of the treatment landscape and the role of predictive and prognostic biomarkers in pancreatic adenocarcinoma. Can J Gastroenterol Hepatol. 2018;2018:1863535. doi:https://doi.org/10.1155/2018/1863535.
- Chatterjee M, Ben-Josef E, Robb R, Vedaie M, Seum S, Thirumoorthy K, Palanichamy K, Harbrecht M, Chakravarti A, Williams TM, et al. Caveolae-mediated endocytosis is critical for albumin cellular uptake and response to albumin-bound chemotherapy. Cancer Res. 2017;77(21):5925–37. doi:https://doi.org/10.1158/0008-5472.CAN-17-0604.
- Lu RM, Hwang YC, Liu IJ, Lee CC, Tsai HZ, Li HJ, Wu HC. Development of therapeutic antibodies for the treatment of diseases. J Biomed Sci. 2020;27(1):1. doi:https://doi.org/10.1186/s12929-019-0592-z.
- Jain RK. Barriers to drug delivery in solid tumors. Sci Am. 1994;271(1):58–65. doi:https://doi.org/10.1038/scientificamerican0794-58.
- Beckman RA, Weiner LM, Davis HM. Antibody constructs in cancer therapy: protein engineering strategies to improve exposure in solid tumors. Cancer. 2007;109(2):170–79. doi:https://doi.org/10.1002/cncr.22402.
- Thurber GM, Schmidt MM, Wittrup KD. Factors determining antibody distribution in tumors. Trends Pharmacol Sci. 2008;29(2):57–61. doi:https://doi.org/10.1016/j.tips.2007.11.004.
- Choi IK, Strauss R, Richter M, Yun C-O, Lieber A. Strategies to increase drug penetration in solid tumors. Front Oncol. 2013;3:193. doi:https://doi.org/10.3389/fonc.2013.00193.
- Kintzing JR, Filsinger Interrante MV, Cochran JR. Emerging strategies for developing next-generation protein therapeutics for cancer treatment. Trends Pharmacol Sci. 2016;37(12):993–1008. doi:https://doi.org/10.1016/j.tips.2016.10.005.
- Sand KM, Bern M, Nilsen J, Noordzij HT, Sandlie I, Andersen JT. Unraveling the Interaction between FcRn and Albumin: opportunities for design of Albumin-based therapeutics. Front Immunol. 2014;5:682.
- Dennis MS, Jin H, Dugger D, Yang R, McFarland L, Ogasawara A, Williams S, Cole MJ, Ross S, Schwall R, et al. Imaging tumors with an albumin-binding Fab, a novel tumor-targeting agent. Cancer Res. 2007;67(1):254–61. doi:https://doi.org/10.1158/0008-5472.CAN-06-2531.
- Escobar-Cabrera E, Lario P, Baardsnes J, Schrag J, Durocher Y, Dixit S. Asymmetric Fc engineering for bispecific antibodies with reduced effector function. Antibodies. 2017;6(2):7. doi:https://doi.org/10.3390/antib6020007.
- Tam SH, McCarthy SG, Armstrong AA, Somani S, Wu SJ, Liu X, Gervais A, Ernst R, Saro D, Decker R, et al. Functional, biophysical, and structural characterization of human IgG1 and IgG4 Fc variants with ablated immune functionality. Antibodies. 2017;6(3):12.
- Almagro JC, Daniels-Wells TR, Perez-Tapia SM, Penichet ML. Progress and challenges in the design and clinical development of antibodies for cancer therapy. Front Immunol. 2018;8:1751.
- Brinkmann U, Kontermann RE. The making of bispecific antibodies. MAbs. 2017;9(2):182–212. doi:https://doi.org/10.1080/19420862.2016.1268307.
- Spangler JB, Manzari MT, Rosalia EK, Chen TF, Wittrup KD. Triepitopic antibody fusions inhibit cetuximab-resistant BRAF and KRAS mutant tumors via EGFR signal repression. J Mol Biol. 2012;422(4):532–44. doi:https://doi.org/10.1016/j.jmb.2012.06.014.
- Li JY, Perry SR, Muniz-Medina V, Wang X, Wetzel LK, Rebelatto MC, Hinrichs MJM, Bezabeh BZ, Fleming RL, Dimasi N, et al. A biparatopic HER2-targeting antibody-drug conjugate induces tumor regression in primary models refractory to or ineligible for HER2-targeted therapy. Cancer Cell. 2016;29(1):117–29. doi:https://doi.org/10.1016/j.ccell.2015.12.008.
- Jost C, Schilling J, Tamaskovic R, Schwill M, Honegger A, Plückthun A. Structural basis for eliciting a cytotoxic effect in HER2-overexpressing cancer cells via binding to the extracellular domain of HER2. Structure. 2013;21(11):1979–91. doi:https://doi.org/10.1016/j.str.2013.08.020.
- Tamaskovic R, Schwill M, Nagy-Davidescu G, Jost C, Schaefer DC, Verdurmen WPR, Schaefer JV, Honegger A, Plückthun A. Intermolecular biparatopic trapping of ErbB2 prevents compensatory activation of PI3K/AKT via RAS–p110 crosstalk. Nat Commun. 2016;7(1):11672. doi:https://doi.org/10.1038/ncomms11672.
- Weisser N, Wickman G, Davies R, Rowse G. Abstract 31: preclinical development of a novel biparatopic HER2 antibody with activity in low to high HER2 expressing cancers. Cancer Res. 2017;77(13 Supplement):31–31. doi:https://doi.org/10.1158/1538-7445.AM2017-31
- de Miguel D, Lemke J, Anel A, Walczak H, Martinez-Lostao L. Onto better trails for cancer treatment. Cell Death Differ. 2016;23(5):733–47. doi:https://doi.org/10.1038/cdd.2015.174.
- McDonagh CF, Huhalov A, Harms BD, Adams S, Paragas V, Oyama S, Zhang B, Luus L, Overland R, Nguyen S, et al. Antitumor activity of a novel bispecific antibody that targets the ErbB2/ErbB3 oncogenic unit and inhibits heregulin-induced activation of ErbB3. Mol Cancer Ther. 2012;11(3):582–93. doi:https://doi.org/10.1158/1535-7163.MCT-11-0820.
- Nelson DR, Benhamou Y, Chuang WL, Lawitz EJ, Rodriguez–Torres M, Flisiak R, Rasenack JWF, Kryczka W, Lee C, Bain VG, et al. Albinterferon Alfa-2b was not inferior to pegylated interferon-alpha in a randomized trial of patients with chronic hepatitis C virus genotype 2 or 3. Gastroenterology. 2010;139(4):1267–76. doi:https://doi.org/10.1053/j.gastro.2010.06.062.
- Zeuzem S, Sulkowski MS, Lawitz EJ, Rustgi VK, Rodriguez–Torres M, Bacon BR, Grigorescu M, Tice AD, Lurie Y, Cianciara J, et al. Albinterferon Alfa-2b was not inferior to pegylated interferon-alpha in a randomized trial of patients with chronic hepatitis C virus genotype 1. Gastroenterol. 2010;139(4):1257–66. doi:https://doi.org/10.1053/j.gastro.2010.06.066.
- Matthews JE, Stewart MW, De Boever EH, Dobbins RL, Hodge RJ, Walker SE, Holland MC, Bush MA. Pharmacodynamics, pharmacokinetics, safety, and tolerability of Albiglutide, a long-acting glucagon-like peptide-1 mimetic, in patients with Type 2 diabetes. J Clin Endocrinol Metab. 2008;93(12):4810–17. doi:https://doi.org/10.1210/jc.2008-1518.
- Oganesyan V, Damschroder MM, Cook KE, Li Q, Gao C, Wu H, Dall’Acqua WF. Structural insights into neonatal Fc receptor-based recycling mechanisms. J Biol Chem. 2014;289(11):7812–24. doi:https://doi.org/10.1074/jbc.M113.537563.
- Andersen JT, Dalhus B, Viuff D, Ravn BT, Gunnarsen KS, Plumridge A, Bunting K, Antunes F, Williamson R, Athwal S, et al. Extending serum half-life of albumin by engineering neonatal Fc receptor (FcRn) binding. J Biol Chem. 2014;289(19):13492–502. doi:https://doi.org/10.1074/jbc.M114.549832.
- Hein KL, Kragh-Hansen U, Morth JP, Jeppesen MD, Otzen D, Møller JV, Nissen P. Crystallographic analysis reveals a unique lidocaine binding site on human serum albumin. J Struct Biol. 2010;171(3):353–60. doi:https://doi.org/10.1016/j.jsb.2010.03.014.
- Kollman PA, Massova I, Reyes C, Kuhn B, Huo S, Chong L, Lee M, Lee T, Duan Y, Wang W, et al. Calculating structures and free energies of complex molecules: combining molecular mechanics and continuum models. Acc Chem Res. 2000;33(12):889–97. doi:https://doi.org/10.1021/ar000033j.
- Schmidt MM, Townson SA, Andreucci AJ, King B, Schirmer E, Murillo A, Dombrowski C, Tisdale A, Lowden P, Masci A, et al. Crystal structure of an HSA/FcRn complex reveals recycling by competitive mimicry of HSA ligands at a pH-dependent hydrophobic interface. Structure. 2013;21(11):1966–78. doi:https://doi.org/10.1016/j.str.2013.08.022.
- Shi C, Shin YO, Hanson J, Cass B, Loewen MC, Durocher Y. Purification and characterization of a recombinant G-protein-coupled receptor, Saccharomyces cerevisiae Ste2p, transiently expressed in HEK293 EBNA1 cells. Biochemistry. 2005;44(48):15705–14. doi:https://doi.org/10.1021/bi051292p.
- Delafosse L, Xu P, Durocher Y. Comparative study of polyethylenimines for transient gene expression in mammalian HEK293 and CHO cells. J Biotechnol. 2016;227:103–11. doi:https://doi.org/10.1016/j.jbiotec.2016.04.028.
- Raymond C, Robotham A, Spearman M, Butler M, Kelly J, Durocher Y. Production of alpha2,6-sialylated IgG1 in CHO cells. MAbs. 2015;7(3):571–83. doi:https://doi.org/10.1080/19420862.2015.1029215.
- 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 Control Release. 2016;223:22–30. doi:https://doi.org/10.1016/j.jconrel.2015.12.019.
- Schmidt MM, Thurber GM, Wittrup KD. Kinetics of anti-carcinoembryonic antigen antibody internalization: effects of affinity, bivalency, and stability. Cancer Immunol Immunother. 2008;57(12):1879–90. doi:https://doi.org/10.1007/s00262-008-0518-1.
- Lang BE, Cole KD. Unfolding properties of recombinant human serum albumin products are due to bioprocessing steps. Biotechnol Prog. 2015;31(1):62–69. doi:https://doi.org/10.1002/btpr.1996.
- Michnik A. Thermal stability of bovine serum albumin DSC study. J Therm Anal Calorim. 2003;71:509–19. doi:https://doi.org/10.1023/A:1022851809481.
- Schier R, McCall A, Adams GP, Marshall KW, Merritt H, Yim M, Crawford RS, Weiner LM, Marks C, Marks JD, et al. Isolation of picomolar affinity anti-c-erbB-2 single-chain Fv by molecular evolution of the complementarity determining regions in the center of the antibody binding site. J Mol Biol. 1996;263(4):551–67. doi:https://doi.org/10.1006/jmbi.1996.0598.
- Schier R, Bye J, Apell G, McCall A, Adams GP, Malmqvist M, Weiner LM, Marks JD. Isolation of high-affinity monomeric human anti-c-erbB-2 single chain Fv using affinity-driven selection. J Mol Biol. 1996;255(1):28–43. doi:https://doi.org/10.1006/jmbi.1996.0004.
- Franklin MC, Carey KD, Vajdos FF, Leahy DJ, de Vos AM, Sliwkowski MX. Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex. Cancer Cell. 2004;5(4):317–28. doi:https://doi.org/10.1016/S1535-6108(04)00083-2.
- Cho HS, Mason K, Ramyar KX, Stanley AM, Gabelli SB, Denney DW, Leahy DJ. Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab. Nature. 2003;421(6924):756–60. doi:https://doi.org/10.1038/nature01392.
- Von Kreudenstein TS, Escobar-Carbrera E, Lario PI, D’Angelo I, Brault K, Kelly JF, Durocher Y, Baardsnes J, Woods RJ, Xie MH, et al. Improving biophysical properties of a bispecific antibody scaffold to aid developability: quality by molecular design. MAbs. 2013;5(5):646–54. doi:https://doi.org/10.4161/mabs.25632.
- Roopenian DC, Low BE, Christianson GJ, Proetzel G, Sproule TJ, Wiles MV. Albumin-deficient mouse models for studying metabolism of human albumin and pharmacokinetics of albumin-based drugs. MAbs. 2015;7(2):344–51. doi:https://doi.org/10.1080/19420862.2015.1008345.
- Lambert JM, Chari RV, Emtansine A-T. (T-DM1): an antibody-drug conjugate (ADC) for HER2-positive breast cancer. J Med Chem. 2014;57(16):6949–64. doi:https://doi.org/10.1021/jm500766w.
- Bahadur RP, Zacharias M. The interface of protein-protein complexes: analysis of contacts and prediction of interactions. Cell Mol Life Sci. 2008;65(7–8):1059–72. doi:https://doi.org/10.1007/s00018-007-7451-x.
- Heaney-Kieras J, King TP. Limited pepsin digestion of human plasma albumin. J Biol Chem. 1977;252:4326–29.
- Ben-Kasus T, Schechter B, Lavi S, Yarden Y, Sela M. Persistent elimination of ErbB-2/HER2-overexpressing tumors using combinations of monoclonal antibodies: relevance of receptor endocytosis. Proc Natl Acad Sci U S A. 2009;106(9):3294–99. doi:https://doi.org/10.1073/pnas.0812059106.
- Friedman LM, Rinon A, Schechter B, Lyass L, Lavi S, Bacus SS, Sela M, Yarden Y. Synergistic down-regulation of receptor tyrosine kinases by combinations of mAbs: implications for cancer immunotherapy. Proc Natl Acad Sci U S A. 2005;102(6):1915–20. doi:https://doi.org/10.1073/pnas.0409610102.
- Kelton C, Wesolowski JS, Soloviev M, Schweickhardt R, Fischer D, Kurosawa E, McKenna SD, Gross AW. Anti-EGFR biparatopic-SEED antibody has enhanced combination-activity in a single molecule. Arch Biochem Biophys. 2012;526(2):219–25. doi:https://doi.org/10.1016/j.abb.2012.03.005.
- Bhattacharya AA, Grune T, Curry S. Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin. J Mol Biol. 2000;303(5):721–32. doi:https://doi.org/10.1006/jmbi.2000.4158.
- Zhang H, Wang Y, Wu Y, Jiang X, Tao Y, Yao Y, Peng Y, Chen X, Fu Y, Yu L, et al. Therapeutic potential of an anti-HER2 single chain antibody-DM1 conjugates for the treatment of HER2-positive cancer. Signal Transduct Target Ther. 2017;2:17015. doi:https://doi.org/10.1038/sigtrans.2017.15.