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Volumn 35, Issue 8, 2017, Pages 691-712

Affibody Molecules in Biotechnological and Medical Applications

Author keywords

affibody; affinity protein; alternative scaffolds; biologicals; molecular imaging; next generation biotherapeutics; targeted therapy

Indexed keywords

BIOTECHNOLOGY; COVALENT BONDS; DIAGNOSIS; MEDICAL APPLICATIONS; MOLECULAR IMAGING; NEURODEGENERATIVE DISEASES; PATHOLOGY; PATIENT TREATMENT; PROTEINS; SCAFFOLDS (BIOLOGY); SULFUR COMPOUNDS;

EID: 85019227020     PISSN: 01677799     EISSN: 18793096     Source Type: Journal    
DOI: 10.1016/j.tibtech.2017.04.007     Document Type: Review
Times cited : (266)

References (152)
  • 1
    • 67649872364 scopus 로고    scopus 로고
    • Engineered protein scaffolds as next-generation antibody therapeutics
    • Gebauer, M., Skerra, A., Engineered protein scaffolds as next-generation antibody therapeutics. Curr. Opin. Chem. Biol. 13 (2009), 245–255.
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 245-255
    • Gebauer, M.1    Skerra, A.2
  • 2
    • 80053438315 scopus 로고    scopus 로고
    • Non-immunoglobulin based protein scaffolds
    • Löfblom, J., et al. Non-immunoglobulin based protein scaffolds. Curr. Opin. Biotechnol. 22 (2011), 843–848.
    • (2011) Curr. Opin. Biotechnol. , vol.22 , pp. 843-848
    • Löfblom, J.1
  • 3
    • 0028982245 scopus 로고
    • A combinatorial library of an alpha-helical bacterial receptor domain
    • Nord, K., et al. A combinatorial library of an alpha-helical bacterial receptor domain. Protein Eng. 8 (1995), 601–608.
    • (1995) Protein Eng. , vol.8 , pp. 601-608
    • Nord, K.1
  • 4
    • 0030835822 scopus 로고    scopus 로고
    • Binding proteins selected from combinatorial libraries of an alpha-helical bacterial receptor domain
    • Nord, K., et al. Binding proteins selected from combinatorial libraries of an alpha-helical bacterial receptor domain. Nat. Biotechnol. 15 (1997), 772–777.
    • (1997) Nat. Biotechnol. , vol.15 , pp. 772-777
    • Nord, K.1
  • 5
    • 79960947751 scopus 로고    scopus 로고
    • The development of peptide-based tools for the analysis of angiogenesis
    • Fedorova, A., et al. The development of peptide-based tools for the analysis of angiogenesis. Chem. Biol. 18 (2011), 839–845.
    • (2011) Chem. Biol. , vol.18 , pp. 839-845
    • Fedorova, A.1
  • 6
    • 84995745245 scopus 로고    scopus 로고
    • Generation of affibody molecules specific for HPV16 E7 recognition
    • Xue, X., et al. Generation of affibody molecules specific for HPV16 E7 recognition. Oncotarget 7 (2016), 73995–74005.
    • (2016) Oncotarget , vol.7 , pp. 73995-74005
    • Xue, X.1
  • 7
    • 84978767559 scopus 로고    scopus 로고
    • LOVTRAP: an optogenetic system for photoinduced protein dissociation
    • Wang, H., et al. LOVTRAP: an optogenetic system for photoinduced protein dissociation. Nat. Methods 13 (2016), 755–758.
    • (2016) Nat. Methods , vol.13 , pp. 755-758
    • Wang, H.1
  • 8
    • 80052628399 scopus 로고    scopus 로고
    • Bacterial display in combinatorial protein engineering
    • Löfblom, J., Bacterial display in combinatorial protein engineering. Biotechnol. J. 6 (2011), 1115–1129.
    • (2011) Biotechnol. J. , vol.6 , pp. 1115-1129
    • Löfblom, J.1
  • 9
    • 41149172339 scopus 로고    scopus 로고
    • A novel affinity protein selection system based on staphylococcal cell surface display and flow cytometry
    • Kronqvist, N., et al. A novel affinity protein selection system based on staphylococcal cell surface display and flow cytometry. Protein Eng. Des. Sel. 21 (2008), 247–255.
    • (2008) Protein Eng. Des. Sel. , vol.21 , pp. 247-255
    • Kronqvist, N.1
  • 10
    • 84859894200 scopus 로고    scopus 로고
    • Selection of TNF-alpha binding affibody molecules using a beta-lactamase protein fragment complementation assay
    • Lofdahl, P.A., et al. Selection of TNF-alpha binding affibody molecules using a beta-lactamase protein fragment complementation assay. Nat. Biotechnol. 26 (2009), 251–259.
    • (2009) Nat. Biotechnol. , vol.26 , pp. 251-259
    • Lofdahl, P.A.1
  • 11
    • 80054079725 scopus 로고    scopus 로고
    • Ribosome display selection of a murine IgG(1) Fab binding affibody molecule allowing species selective recovery of monoclonal antibodies
    • Grimm, S., et al. Ribosome display selection of a murine IgG(1) Fab binding affibody molecule allowing species selective recovery of monoclonal antibodies. Mol. Biotechnol. 48 (2011), 263–276.
    • (2011) Mol. Biotechnol. , vol.48 , pp. 263-276
    • Grimm, S.1
  • 12
    • 85006293410 scopus 로고    scopus 로고
    • Flow-cytometric screening of aggregation-inhibitors using a fluorescence-assisted intracellular method
    • Published online December 1 2016.
    • Lindberg, H., et al. Flow-cytometric screening of aggregation-inhibitors using a fluorescence-assisted intracellular method. Biotechnol. J., 2016, 10.1002/biot.201600364 Published online December 1, 2016.
    • (2016) Biotechnol. J.
    • Lindberg, H.1
  • 13
    • 78650001663 scopus 로고    scopus 로고
    • Staphylococcal surface display in combinatorial protein engineering and epitope mapping of antibodies
    • Kronqvist, N., et al. Staphylococcal surface display in combinatorial protein engineering and epitope mapping of antibodies. Recent Pat. Biotechnol. 4 (2010), 171–182.
    • (2010) Recent Pat. Biotechnol. , vol.4 , pp. 171-182
    • Kronqvist, N.1
  • 14
    • 33646261864 scopus 로고    scopus 로고
    • Tumor imaging using a picomolar affinity HER2 binding affibody molecule
    • Orlova, A., et al. Tumor imaging using a picomolar affinity HER2 binding affibody molecule. Cancer Res. 66 (2006), 4339–4348.
    • (2006) Cancer Res. , vol.66 , pp. 4339-4348
    • Orlova, A.1
  • 15
    • 84877609907 scopus 로고    scopus 로고
    • Inhibiting HER3-mediated tumor cell growth with affibody molecules engineered to low picomolar affinity by position-directed error-prone PCR-like diversification
    • Malm, M., et al. Inhibiting HER3-mediated tumor cell growth with affibody molecules engineered to low picomolar affinity by position-directed error-prone PCR-like diversification. PLoS One, 8, 2013, e62791.
    • (2013) PLoS One , vol.8 , pp. e62791
    • Malm, M.1
  • 16
    • 84947041962 scopus 로고    scopus 로고
    • A truncated and dimeric format of an affibody library on bacteria enables FACS-mediated isolation of amyloid-beta aggregation inhibitors with subnanomolar affinity
    • Lindberg, H., et al. A truncated and dimeric format of an affibody library on bacteria enables FACS-mediated isolation of amyloid-beta aggregation inhibitors with subnanomolar affinity. Biotechnol. J. 10 (2015), 1707–1718.
    • (2015) Biotechnol. J. , vol.10 , pp. 1707-1718
    • Lindberg, H.1
  • 17
    • 84922784130 scopus 로고    scopus 로고
    • Simultaneous targeting of two ligand-binding sites on VEGFR2 using biparatopic affibody molecules results in dramatically improved affinity
    • Fleetwood, F., et al. Simultaneous targeting of two ligand-binding sites on VEGFR2 using biparatopic affibody molecules results in dramatically improved affinity. Sci. Rep., 4, 2014, 7518.
    • (2014) Sci. Rep. , vol.4 , pp. 7518
    • Fleetwood, F.1
  • 18
    • 84862296121 scopus 로고    scopus 로고
    • Mixed oligonucleotides for random mutagenesis: best way of making them
    • Arunachalam, T.S., Mixed oligonucleotides for random mutagenesis: best way of making them. Org. Biomol. Chem. 10 (2012), 4641–4650.
    • (2012) Org. Biomol. Chem. , vol.10 , pp. 4641-4650
    • Arunachalam, T.S.1
  • 19
    • 77951768789 scopus 로고    scopus 로고
    • Design of an optimized scaffold for affibody molecules
    • Feldwisch, J., et al. Design of an optimized scaffold for affibody molecules. J. Mol. Biol. 398 (2010), 232–247.
    • (2010) J. Mol. Biol. , vol.398 , pp. 232-247
    • Feldwisch, J.1
  • 20
    • 84860251745 scopus 로고    scopus 로고
    • A native chemical ligation approach for combinatorial assembly of affibody molecules
    • Lindgren, J., et al. A native chemical ligation approach for combinatorial assembly of affibody molecules. Chembiochem 13 (2012), 1024–1031.
    • (2012) Chembiochem , vol.13 , pp. 1024-1031
    • Lindgren, J.1
  • 21
    • 84865145661 scopus 로고    scopus 로고
    • Influence of DOTA chelator position on biodistribution and targeting properties of (111)In-labeled synthetic anti-HER2 affibody molecules
    • Perols, A., et al. Influence of DOTA chelator position on biodistribution and targeting properties of (111)In-labeled synthetic anti-HER2 affibody molecules. Bioconjug. Chem. 23 (2012), 1661–1770.
    • (2012) Bioconjug. Chem. , vol.23 , pp. 1661-1770
    • Perols, A.1
  • 22
    • 43549101411 scopus 로고    scopus 로고
    • Alternative binding proteins: affibody binding proteins developed from a small three-helix bundle scaffold
    • Nygren, P.Å., Alternative binding proteins: affibody binding proteins developed from a small three-helix bundle scaffold. FEBS J. 275 (2008), 2668–2676.
    • (2008) FEBS J. , vol.275 , pp. 2668-2676
    • Nygren, P.Å.1
  • 23
    • 77953130101 scopus 로고    scopus 로고
    • Affibody molecules: engineered proteins for therapeutic, diagnostic and biotechnological applications
    • Löfblom, J., et al. Affibody molecules: engineered proteins for therapeutic, diagnostic and biotechnological applications. FEBS Lett. 584 (2010), 2670–2680.
    • (2010) FEBS Lett. , vol.584 , pp. 2670-2680
    • Löfblom, J.1
  • 24
    • 77957374838 scopus 로고    scopus 로고
    • Radiolabelled receptor-tyrosine-kinase targeting drugs for patient stratification and monitoring of therapy response: prospects and pitfalls
    • Tolmachev, V., et al. Radiolabelled receptor-tyrosine-kinase targeting drugs for patient stratification and monitoring of therapy response: prospects and pitfalls. Lancet Oncol. 11 (2010), 992–1000.
    • (2010) Lancet Oncol. , vol.11 , pp. 992-1000
    • Tolmachev, V.1
  • 25
    • 84883201671 scopus 로고    scopus 로고
    • Design and evaluation of radiolabeled tracers for tumor imaging
    • Wallberg, H., Stahl, S., Design and evaluation of radiolabeled tracers for tumor imaging. Biotechnol. Appl. Biochem. 60 (2013), 365–383.
    • (2013) Biotechnol. Appl. Biochem. , vol.60 , pp. 365-383
    • Wallberg, H.1    Stahl, S.2
  • 26
    • 84996565692 scopus 로고    scopus 로고
    • Feasibility of imaging of epidermal growth factor receptor expression with ZEGFR:2377 affibody molecule labeled with 99mTc using a peptide-based cysteine-containing chelator
    • Andersson, K.G., et al. Feasibility of imaging of epidermal growth factor receptor expression with ZEGFR:2377 affibody molecule labeled with 99mTc using a peptide-based cysteine-containing chelator. Int. J. Oncol. 49 (2016), 2285–2293.
    • (2016) Int. J. Oncol. , vol.49 , pp. 2285-2293
    • Andersson, K.G.1
  • 27
    • 79952798198 scopus 로고    scopus 로고
    • Molecular design and optimization of 99mTc-labeled recombinant affibody molecules improves their biodistribution and imaging properties
    • Wallberg, H., et al. Molecular design and optimization of 99mTc-labeled recombinant affibody molecules improves their biodistribution and imaging properties. J. Nucl. Med. 52 (2011), 461–469.
    • (2011) J. Nucl. Med. , vol.52 , pp. 461-469
    • Wallberg, H.1
  • 28
    • 84968547778 scopus 로고    scopus 로고
    • Increasing the net negative charge by replacement of DOTA chelator with DOTAGA improves the biodistribution of radiolabeled second-generation synthetic affibody molecules
    • Westerlund, K., et al. Increasing the net negative charge by replacement of DOTA chelator with DOTAGA improves the biodistribution of radiolabeled second-generation synthetic affibody molecules. Mol. Pharm. 13 (2016), 1668–1678.
    • (2016) Mol. Pharm. , vol.13 , pp. 1668-1678
    • Westerlund, K.1
  • 29
    • 84901325574 scopus 로고    scopus 로고
    • First-in-human molecular imaging of HER2 expression in breast cancer metastases using the 111In-ABY-025 affibody molecule
    • Sorensen, J., et al. First-in-human molecular imaging of HER2 expression in breast cancer metastases using the 111In-ABY-025 affibody molecule. J. Nucl. Med. 55 (2014), 730–735.
    • (2014) J. Nucl. Med. , vol.55 , pp. 730-735
    • Sorensen, J.1
  • 30
    • 84989872106 scopus 로고    scopus 로고
    • Two-photon tracer for human epidermal growth factor receptor-2: detection of breast cancer in a live tissue
    • Choi, J.W., et al. Two-photon tracer for human epidermal growth factor receptor-2: detection of breast cancer in a live tissue. Anal. Chem. 88 (2016), 9412–9418.
    • (2016) Anal. Chem. , vol.88 , pp. 9412-9418
    • Choi, J.W.1
  • 31
    • 84978062632 scopus 로고    scopus 로고
    • Preclinical PET imaging of EGFR levels: pairing a targeting with a non-targeting Sel-tagged affibody-based tracer to estimate the specific uptake
    • Cheng, Q., et al. Preclinical PET imaging of EGFR levels: pairing a targeting with a non-targeting Sel-tagged affibody-based tracer to estimate the specific uptake. EJNMMI Res., 6, 2016, 58.
    • (2016) EJNMMI Res. , vol.6 , pp. 58
    • Cheng, Q.1
  • 32
    • 84959020465 scopus 로고    scopus 로고
    • PET imaging of epidermal growth factor receptor expression in tumours using 89Zr-labelled ZEGFR:2377 affibody molecules
    • Garousi, J., et al. PET imaging of epidermal growth factor receptor expression in tumours using 89Zr-labelled ZEGFR:2377 affibody molecules. Int. J. Oncol. 48 (2016), 1325–1332.
    • (2016) Int. J. Oncol. , vol.48 , pp. 1325-1332
    • Garousi, J.1
  • 33
    • 84945176046 scopus 로고    scopus 로고
    • Affibody-mediated PET imaging of HER3 expression in malignant tumours
    • Rosestedt, M., et al. Affibody-mediated PET imaging of HER3 expression in malignant tumours. Sci. Rep., 5, 2015, 15226.
    • (2015) Sci. Rep. , vol.5 , pp. 15226
    • Rosestedt, M.1
  • 34
    • 84927630924 scopus 로고    scopus 로고
    • Gallium-68-labeled affibody molecule for PET imaging of PDGFRbeta expression in vivo
    • Strand, J., et al. Gallium-68-labeled affibody molecule for PET imaging of PDGFRbeta expression in vivo. Mol. Pharm. 11 (2014), 3957–3964.
    • (2014) Mol. Pharm. , vol.11 , pp. 3957-3964
    • Strand, J.1
  • 35
    • 84922105067 scopus 로고    scopus 로고
    • Evaluation of 99mTc-Z IGF1R:4551-GGGC affibody molecule, a new probe for imaging of insulin-like growth factor type 1 receptor expression
    • Mitran, B., et al. Evaluation of 99mTc-Z IGF1R:4551-GGGC affibody molecule, a new probe for imaging of insulin-like growth factor type 1 receptor expression. Amino Acids 47 (2015), 303–315.
    • (2015) Amino Acids , vol.47 , pp. 303-315
    • Mitran, B.1
  • 36
    • 84994536143 scopus 로고    scopus 로고
    • Comparative evaluation of affibody molecules for radionuclide imaging of in vivo expression of carbonic anhydrase IX
    • Garousi, J., et al. Comparative evaluation of affibody molecules for radionuclide imaging of in vivo expression of carbonic anhydrase IX. Mol. Pharm. 13 (2016), 3676–3687.
    • (2016) Mol. Pharm. , vol.13 , pp. 3676-3687
    • Garousi, J.1
  • 37
    • 84954520777 scopus 로고    scopus 로고
    • Measuring HER2-receptor expression in metastatic breast cancer using [(68)Ga]ABY-025 affibody PET/CT
    • Sorensen, J., et al. Measuring HER2-receptor expression in metastatic breast cancer using [(68)Ga]ABY-025 affibody PET/CT. Theranostics 6 (2016), 262–271.
    • (2016) Theranostics , vol.6 , pp. 262-271
    • Sorensen, J.1
  • 38
    • 84973595060 scopus 로고    scopus 로고
    • Biodistribution and radiation dosimetry of the anti-HER2 affibody molecule 68Ga-ABY-025 in breast cancer patients
    • Sandstrom, M., et al. Biodistribution and radiation dosimetry of the anti-HER2 affibody molecule 68Ga-ABY-025 in breast cancer patients. J. Nucl. Med. 57 (2016), 867–871.
    • (2016) J. Nucl. Med. , vol.57 , pp. 867-871
    • Sandstrom, M.1
  • 39
    • 77953927395 scopus 로고    scopus 로고
    • Molecular imaging of HER2-expressing malignant tumors in breast cancer patients using synthetic 111In- or 68Ga-labeled affibody molecules
    • Baum, R.P., et al. Molecular imaging of HER2-expressing malignant tumors in breast cancer patients using synthetic 111In- or 68Ga-labeled affibody molecules. J. Nucl. Med. 51 (2010), 892–897.
    • (2010) J. Nucl. Med. , vol.51 , pp. 892-897
    • Baum, R.P.1
  • 40
    • 85020572468 scopus 로고    scopus 로고
    • Good manufacturing practice production of [(68)Ga]Ga-ABY-025 for HER2 specific breast cancer imaging
    • Velikyan, I., et al. Good manufacturing practice production of [(68)Ga]Ga-ABY-025 for HER2 specific breast cancer imaging. Am. J. Nucl. Med. Mol. Imaging 6 (2016), 135–153.
    • (2016) Am. J. Nucl. Med. Mol. Imaging , vol.6 , pp. 135-153
    • Velikyan, I.1
  • 41
    • 84903718234 scopus 로고    scopus 로고
    • ImmunoPET and biodistribution with human epidermal growth factor receptor 3 targeting antibody (8)(9)Zr-RG7116
    • Terwisscha van Scheltinga, A.G., et al. ImmunoPET and biodistribution with human epidermal growth factor receptor 3 targeting antibody (8)(9)Zr-RG7116. MAbs 6 (2014), 1051–1058.
    • (2014) MAbs , vol.6 , pp. 1051-1058
    • Terwisscha van Scheltinga, A.G.1
  • 42
    • 84870330734 scopus 로고    scopus 로고
    • Small-animal SPECT/CT of HER2 and HER3 expression in tumor xenografts in athymic mice using trastuzumab Fab-heregulin bispecific radioimmunoconjugates
    • Razumienko, E.J., et al. Small-animal SPECT/CT of HER2 and HER3 expression in tumor xenografts in athymic mice using trastuzumab Fab-heregulin bispecific radioimmunoconjugates. J. Nucl. Med. 53 (2012), 1943–1950.
    • (2012) J. Nucl. Med. , vol.53 , pp. 1943-1950
    • Razumienko, E.J.1
  • 43
    • 84983437097 scopus 로고    scopus 로고
    • Efficient [(18)F]AlF radiolabeling of ZHER3:8698 affibody molecule for imaging of HER3 positive tumors
    • Da Pieve, C., et al. Efficient [(18)F]AlF radiolabeling of ZHER3:8698 affibody molecule for imaging of HER3 positive tumors. Bioconjug. Chem. 27 (2016), 1839–1849.
    • (2016) Bioconjug. Chem. , vol.27 , pp. 1839-1849
    • Da Pieve, C.1
  • 44
    • 84994908259 scopus 로고    scopus 로고
    • Evaluation of the first 44Sc-labeled affibody molecule for imaging of HER2-expressing tumors
    • Honarvar, H., et al. Evaluation of the first 44Sc-labeled affibody molecule for imaging of HER2-expressing tumors. Nucl. Med. Biol. 45 (2017), 15–21.
    • (2017) Nucl. Med. Biol. , vol.45 , pp. 15-21
    • Honarvar, H.1
  • 45
    • 84879575076 scopus 로고    scopus 로고
    • HAHAHA, HEHEHE, HIHIHI, or HKHKHK: influence of position and composition of histidine containing tags on biodistribution of [(99m)Tc(CO)3](+)-labeled affibody molecules
    • Hofstrom, C., et al. HAHAHA, HEHEHE, HIHIHI, or HKHKHK: influence of position and composition of histidine containing tags on biodistribution of [(99m)Tc(CO)3](+)-labeled affibody molecules. J. Med. Chem. 56 (2013), 4966–4974.
    • (2013) J. Med. Chem. , vol.56 , pp. 4966-4974
    • Hofstrom, C.1
  • 46
    • 84866162512 scopus 로고    scopus 로고
    • HER2-positive tumors imaged within 1 hour using a site-specifically 11C-labeled Sel-tagged affibody molecule
    • Wallberg, H., et al. HER2-positive tumors imaged within 1 hour using a site-specifically 11C-labeled Sel-tagged affibody molecule. J. Nucl. Med. 53 (2012), 1446–1453.
    • (2012) J. Nucl. Med. , vol.53 , pp. 1446-1453
    • Wallberg, H.1
  • 47
    • 84977123736 scopus 로고    scopus 로고
    • Small-protein-stabilized semiconductor nanoprobe for targeted imaging of cancer cells
    • Zhao, N., et al. Small-protein-stabilized semiconductor nanoprobe for targeted imaging of cancer cells. Chembiochem 17 (2016), 1202–1206.
    • (2016) Chembiochem , vol.17 , pp. 1202-1206
    • Zhao, N.1
  • 48
    • 84955746433 scopus 로고    scopus 로고
    • A small-molecule dye for NIR-II imaging
    • Antaris, A.L., et al. A small-molecule dye for NIR-II imaging. Nat. Mater. 15 (2016), 235–242.
    • (2016) Nat. Mater. , vol.15 , pp. 235-242
    • Antaris, A.L.1
  • 49
    • 84955420437 scopus 로고    scopus 로고
    • Optical imaging of ovarian cancer using HER-2 affibody conjugated nanoparticles
    • Satpathy, M., et al. Optical imaging of ovarian cancer using HER-2 affibody conjugated nanoparticles. Methods Mol. Biol. 1219 (2015), 171–185.
    • (2015) Methods Mol. Biol. , vol.1219 , pp. 171-185
    • Satpathy, M.1
  • 50
    • 84925059084 scopus 로고    scopus 로고
    • Superparamagnetic iron oxide nanoparticle micelles stabilized by recombinant oleosin for targeted magnetic resonance imaging
    • Vargo, K.B., et al. Superparamagnetic iron oxide nanoparticle micelles stabilized by recombinant oleosin for targeted magnetic resonance imaging. Small 11 (2015), 1409–1413.
    • (2015) Small , vol.11 , pp. 1409-1413
    • Vargo, K.B.1
  • 51
    • 84907654664 scopus 로고    scopus 로고
    • A novel affibody bioconjugate for dual-modality imaging of ovarian cancer
    • Wang, Y., et al. A novel affibody bioconjugate for dual-modality imaging of ovarian cancer. Chem. Commun. (Camb) 50 (2014), 12832–12835.
    • (2014) Chem. Commun. (Camb) , vol.50 , pp. 12832-12835
    • Wang, Y.1
  • 52
    • 84873076558 scopus 로고    scopus 로고
    • Affibody modified and radiolabeled gold-iron oxide hetero-nanostructures for tumor PET, optical and MR imaging
    • Yang, M., et al. Affibody modified and radiolabeled gold-iron oxide hetero-nanostructures for tumor PET, optical and MR imaging. Biomaterials 34 (2013), 2796–2806.
    • (2013) Biomaterials , vol.34 , pp. 2796-2806
    • Yang, M.1
  • 53
    • 84973579913 scopus 로고    scopus 로고
    • Vision 20/20: Molecular-guided surgical oncology based upon tumor metabolism or immunologic phenotype: technological pathways for point of care imaging and intervention
    • Pogue, B.W., et al. Vision 20/20: Molecular-guided surgical oncology based upon tumor metabolism or immunologic phenotype: technological pathways for point of care imaging and intervention. Med. Phys., 43, 2016, 3143.
    • (2016) Med. Phys. , vol.43 , pp. 3143
    • Pogue, B.W.1
  • 54
    • 84977124877 scopus 로고    scopus 로고
    • Fluorescent affibody molecule administered In vivo at a microdose level labels egfr expressing glioma tumor regions
    • de Souza, A.L., et al. Fluorescent affibody molecule administered In vivo at a microdose level labels egfr expressing glioma tumor regions. Mol. Imaging Biol. 19 (2017), 41–48.
    • (2017) Mol. Imaging Biol. , vol.19 , pp. 41-48
    • de Souza, A.L.1
  • 55
    • 85000956557 scopus 로고    scopus 로고
    • Toxicity and pharmacokinetic profile for single-dose injection of ABY-029: a fluorescent anti-EGFR synthetic affibody molecule for human use
    • Published online December 1 2016.
    • Samkoe, K.S., et al. Toxicity and pharmacokinetic profile for single-dose injection of ABY-029: a fluorescent anti-EGFR synthetic affibody molecule for human use. Mol. Imaging Biol., 2016, 10.1007/s11307-016-1033-y Published online December 1, 2016.
    • (2016) Mol. Imaging Biol.
    • Samkoe, K.S.1
  • 56
    • 85018414613 scopus 로고    scopus 로고
    • Simultaneous in vivo fluorescent markers for perfusion, protoporphyrin metabolism and EGFR expression for optically guided identification of orthotopic glioma
    • Elliott, J.T., et al. Simultaneous in vivo fluorescent markers for perfusion, protoporphyrin metabolism and EGFR expression for optically guided identification of orthotopic glioma. Clin. Cancer Res. 23 (2017), 2203–2212.
    • (2017) Clin. Cancer Res. , vol.23 , pp. 2203-2212
    • Elliott, J.T.1
  • 57
    • 84876071085 scopus 로고    scopus 로고
    • Fluorescent affibody peptide penetration in glioma margin is superior to full antibody
    • Sexton, K., et al. Fluorescent affibody peptide penetration in glioma margin is superior to full antibody. PLoS One, 8, 2013, e60390.
    • (2013) PLoS One , vol.8 , pp. e60390
    • Sexton, K.1
  • 58
    • 84989339198 scopus 로고    scopus 로고
    • Targeting HER3 using mono- and bispecific antibodies or alternative scaffolds
    • Malm, M., et al. Targeting HER3 using mono- and bispecific antibodies or alternative scaffolds. MAbs 8 (2016), 1195–1209.
    • (2016) MAbs , vol.8 , pp. 1195-1209
    • Malm, M.1
  • 59
    • 79952686672 scopus 로고    scopus 로고
    • Combining phage and staphylococcal surface display for generation of ErbB3-specific affibody molecules
    • Kronqvist, N., et al. Combining phage and staphylococcal surface display for generation of ErbB3-specific affibody molecules. Protein Eng. Des. Sel. 24 (2011), 385–396.
    • (2011) Protein Eng. Des. Sel. , vol.24 , pp. 385-396
    • Kronqvist, N.1
  • 60
    • 84906948848 scopus 로고    scopus 로고
    • Engineering of a bispecific affibody molecule towards HER2 and HER3 by addition of an albumin-binding domain allows for affinity purification and in vivo half-life extension
    • Malm, M., et al. Engineering of a bispecific affibody molecule towards HER2 and HER3 by addition of an albumin-binding domain allows for affinity purification and in vivo half-life extension. Biotechnol. J. 9 (2014), 1215–1222.
    • (2014) Biotechnol. J. , vol.9 , pp. 1215-1222
    • Malm, M.1
  • 61
    • 85019022799 scopus 로고    scopus 로고
    • Engineered multivalency enhances affibody-based HER3 inhibition and downregulation in cancer cells
    • Schardt, J.S., et al. Engineered multivalency enhances affibody-based HER3 inhibition and downregulation in cancer cells. Mol. Pharm. 14 (2017), 1047–1056.
    • (2017) Mol. Pharm. , vol.14 , pp. 1047-1056
    • Schardt, J.S.1
  • 62
    • 84877609907 scopus 로고    scopus 로고
    • Inhibiting HER3-mediated tumor cell growth with affibody molecules engineered to low picomolar affinity by position-directed error-prone PCR-like diversification
    • Malm, M., et al. Inhibiting HER3-mediated tumor cell growth with affibody molecules engineered to low picomolar affinity by position-directed error-prone PCR-like diversification. PLoS One, 8, 2013, e62791.
    • (2013) PLoS One , vol.8 , pp. e62791
    • Malm, M.1
  • 63
    • 85013769093 scopus 로고    scopus 로고
    • In vivo evaluation of a novel format of a bivalent HER3-targeting and albumin-binding therapeutic affibody construct
    • Bass, T.Z., et al. In vivo evaluation of a novel format of a bivalent HER3-targeting and albumin-binding therapeutic affibody construct. Sci. Rep., 7, 2017, 43118.
    • (2017) Sci. Rep. , vol.7 , pp. 43118
    • Bass, T.Z.1
  • 64
    • 84876336136 scopus 로고    scopus 로고
    • Monoclonal antibody therapeutics with up to five specificities: functional enhancement through fusion of target-specific peptides
    • LaFleur, D., et al. Monoclonal antibody therapeutics with up to five specificities: functional enhancement through fusion of target-specific peptides. MAbs 6 (2013), 208–218.
    • (2013) MAbs , vol.6 , pp. 208-218
    • LaFleur, D.1
  • 65
    • 84962247651 scopus 로고    scopus 로고
    • Novel affinity binders for neutralization of vascular endothelial growth factor (VEGF) signaling
    • Fleetwood, F., et al. Novel affinity binders for neutralization of vascular endothelial growth factor (VEGF) signaling. Cell. Mol. Life Sci. 73 (2016), 1671–1683.
    • (2016) Cell. Mol. Life Sci. , vol.73 , pp. 1671-1683
    • Fleetwood, F.1
  • 66
    • 79952313111 scopus 로고    scopus 로고
    • Engineered high-affinity affibody molecules targeting platelet-derived growth factor receptor beta in vivo
    • Lindborg, M., et al. Engineered high-affinity affibody molecules targeting platelet-derived growth factor receptor beta in vivo. J. Mol. Biol. 407 (2011), 298–315.
    • (2011) J. Mol. Biol. , vol.407 , pp. 298-315
    • Lindborg, M.1
  • 67
    • 77954828431 scopus 로고    scopus 로고
    • Selection of affibody molecules to the ligand-binding site of the insulin-like growth factor-1 receptor
    • Li, J., et al. Selection of affibody molecules to the ligand-binding site of the insulin-like growth factor-1 receptor. Biotechnol. Appl. Biochem. 55 (2010), 99–109.
    • (2010) Biotechnol. Appl. Biochem. , vol.55 , pp. 99-109
    • Li, J.1
  • 68
    • 84920827599 scopus 로고    scopus 로고
    • An affibody-adalimumab hybrid blocks combined IL-6 and TNF-triggered serum amyloid A secretion in vivo
    • Yu, F., et al. An affibody-adalimumab hybrid blocks combined IL-6 and TNF-triggered serum amyloid A secretion in vivo. MAbs 6 (2014), 1598–1607.
    • (2014) MAbs , vol.6 , pp. 1598-1607
    • Yu, F.1
  • 69
    • 70350521639 scopus 로고    scopus 로고
    • Generation of tumour-necrosis-factor-alpha-specific affibody molecules capable of blocking receptor binding in vitro
    • Jonsson, A., et al. Generation of tumour-necrosis-factor-alpha-specific affibody molecules capable of blocking receptor binding in vitro. Biotechnol. Appl. Biochem. 54 (2009), 93–103.
    • (2009) Biotechnol. Appl. Biochem. , vol.54 , pp. 93-103
    • Jonsson, A.1
  • 70
    • 85007471058 scopus 로고    scopus 로고
    • Dextran sulphate sodium colitis in C57BL/6J mice is alleviated by Lactococcus lactis and worsened by the neutralization of tumor necrosis factor alpha
    • Berlec, A., et al. Dextran sulphate sodium colitis in C57BL/6J mice is alleviated by Lactococcus lactis and worsened by the neutralization of tumor necrosis factor alpha. Int. Immunopharmacol. 43 (2017), 219–226.
    • (2017) Int. Immunopharmacol. , vol.43 , pp. 219-226
    • Berlec, A.1
  • 71
    • 84977071601 scopus 로고    scopus 로고
    • Phase 3 trials of Ixekizumab in moderate-to-severe plaque psoriasis
    • Gordon, K.B., et al. Phase 3 trials of Ixekizumab in moderate-to-severe plaque psoriasis. N. Engl. J. Med. 375 (2016), 345–356.
    • (2016) N. Engl. J. Med. , vol.375 , pp. 345-356
    • Gordon, K.B.1
  • 72
    • 85021308251 scopus 로고    scopus 로고
    • Secukinumab self-administration by prefilled syringe maintains reduction of plaque psoriasis severity over 52 weeks: results of the FEATURE trial
    • Gottlieb, A.B., et al. Secukinumab self-administration by prefilled syringe maintains reduction of plaque psoriasis severity over 52 weeks: results of the FEATURE trial. J. Drugs Dermatol. 15 (2016), 1226–1234.
    • (2016) J. Drugs Dermatol. , vol.15 , pp. 1226-1234
    • Gottlieb, A.B.1
  • 73
    • 84960379919 scopus 로고    scopus 로고
    • The clinical potential of affibody-based inhibitors of C5 for therapeutic complement disruption
    • Berglund, M.M., Stromberg, P., The clinical potential of affibody-based inhibitors of C5 for therapeutic complement disruption. Expert Rev. Proteom. 13 (2016), 241–243.
    • (2016) Expert Rev. Proteom. , vol.13 , pp. 241-243
    • Berglund, M.M.1    Stromberg, P.2
  • 74
    • 78649713667 scopus 로고    scopus 로고
    • Selection and characterisation of affibody molecules inhibiting the interaction between Ras and Raf in vitro
    • Grimm, S., et al. Selection and characterisation of affibody molecules inhibiting the interaction between Ras and Raf in vitro. N. Biotechnol. 27 (2010), 766–773.
    • (2010) N. Biotechnol. , vol.27 , pp. 766-773
    • Grimm, S.1
  • 75
    • 84862008140 scopus 로고    scopus 로고
    • Monitored whole gene in vitro evolution of an anti-hRaf-1 affibody molecule towards increased binding affinity
    • Grimm, S., et al. Monitored whole gene in vitro evolution of an anti-hRaf-1 affibody molecule towards increased binding affinity. N. Biotechnol. 29 (2012), 534–542.
    • (2012) N. Biotechnol. , vol.29 , pp. 534-542
    • Grimm, S.1
  • 76
    • 84957590363 scopus 로고    scopus 로고
    • Inhibitory effects of H-Ras/Raf-1-binding affibody molecules on synovial cell function
    • Shibasaki, S., et al. Inhibitory effects of H-Ras/Raf-1-binding affibody molecules on synovial cell function. AMB Express, 4, 2014, 82.
    • (2014) AMB Express , vol.4 , pp. 82
    • Shibasaki, S.1
  • 77
    • 84919339948 scopus 로고    scopus 로고
    • Delivery of antibody mimics into mammalian cells via anthrax toxin protective antigen
    • Liao, X., et al. Delivery of antibody mimics into mammalian cells via anthrax toxin protective antigen. Chembiochem 15 (2014), 2458–2466.
    • (2014) Chembiochem , vol.15 , pp. 2458-2466
    • Liao, X.1
  • 78
    • 33845665382 scopus 로고    scopus 로고
    • Selection and characterization of affibody ligands binding to Alzheimer amyloid beta peptides
    • Gronwall, C., et al. Selection and characterization of affibody ligands binding to Alzheimer amyloid beta peptides. J. Biotechnol. 128 (2007), 162–183.
    • (2007) J. Biotechnol. , vol.128 , pp. 162-183
    • Gronwall, C.1
  • 79
    • 42449111198 scopus 로고    scopus 로고
    • Stabilization of a beta-hairpin in monomeric Alzheimer's amyloid-beta peptide inhibits amyloid formation
    • Hoyer, W., et al. Stabilization of a beta-hairpin in monomeric Alzheimer's amyloid-beta peptide inhibits amyloid formation. Proc. Natl. Acad. Sci. U. S. A. 105 (2008), 5099–5104.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 5099-5104
    • Hoyer, W.1
  • 80
    • 77950579610 scopus 로고    scopus 로고
    • Sequestration of the Abeta peptide prevents toxicity and promotes degradation in vivo
    • Luheshi, L.M., et al. Sequestration of the Abeta peptide prevents toxicity and promotes degradation in vivo. PLoS Biol., 8, 2010, e1000334.
    • (2010) PLoS Biol. , vol.8 , pp. e1000334
    • Luheshi, L.M.1
  • 81
    • 84947031613 scopus 로고    scopus 로고
    • Development of a high affinity affibody-derived protein against amyloid beta-peptide for future Alzheimer's disease therapy
    • De Genst, E., Muyldermans, S., Development of a high affinity affibody-derived protein against amyloid beta-peptide for future Alzheimer's disease therapy. Biotechnol. J. 10 (2015), 1668–1669.
    • (2015) Biotechnol. J. , vol.10 , pp. 1668-1669
    • De Genst, E.1    Muyldermans, S.2
  • 82
    • 85032703620 scopus 로고    scopus 로고
    • An affibody to monomeric abeta as a novel therapeutic approach for Alzheimer's disease pathology
    • Boutajangout, A., et al. An affibody to monomeric abeta as a novel therapeutic approach for Alzheimer's disease pathology. Alzheimers Dement. J. Alzheimers Assoc. 12 (2016), P835–P836.
    • (2016) Alzheimers Dement. J. Alzheimers Assoc. , vol.12 , pp. P835-P836
    • Boutajangout, A.1
  • 83
    • 84905976762 scopus 로고    scopus 로고
    • Alternative conformations of the Tau repeat domain in complex with an engineered binding protein
    • Gruning, C.S., et al. Alternative conformations of the Tau repeat domain in complex with an engineered binding protein. J. Biol. Chem. 289 (2014), 23209–23218.
    • (2014) J. Biol. Chem. , vol.289 , pp. 23209-23218
    • Gruning, C.S.1
  • 84
    • 84898650496 scopus 로고    scopus 로고
    • Sequestration of a beta-hairpin for control of alpha-synuclein aggregation
    • Mirecka, E.A., et al. Sequestration of a beta-hairpin for control of alpha-synuclein aggregation. Angew. Chem. Int. Ed. Engl. 53 (2014), 4227–4230.
    • (2014) Angew. Chem. Int. Ed. Engl. , vol.53 , pp. 4227-4230
    • Mirecka, E.A.1
  • 85
    • 84937394006 scopus 로고    scopus 로고
    • Impact of subunit linkages in an engineered homodimeric binding protein to alpha-synuclein
    • Gauhar, A., et al. Impact of subunit linkages in an engineered homodimeric binding protein to alpha-synuclein. Protein Eng. Des. Sel. 27 (2014), 473–479.
    • (2014) Protein Eng. Des. Sel. , vol.27 , pp. 473-479
    • Gauhar, A.1
  • 86
    • 84911937264 scopus 로고    scopus 로고
    • Engineered aggregation inhibitor fusion for production of highly amyloidogenic human islet amyloid polypeptide
    • Mirecka, E.A., et al. Engineered aggregation inhibitor fusion for production of highly amyloidogenic human islet amyloid polypeptide. J. Biotechnol. 191 (2014), 221–227.
    • (2014) J. Biotechnol. , vol.191 , pp. 221-227
    • Mirecka, E.A.1
  • 87
    • 84988346218 scopus 로고    scopus 로고
    • Beta-hairpin of islet amyloid polypeptide bound to an aggregation inhibitor
    • Mirecka, E.A., et al. Beta-hairpin of islet amyloid polypeptide bound to an aggregation inhibitor. Sci. Rep., 6, 2016, 33474.
    • (2016) Sci. Rep. , vol.6 , pp. 33474
    • Mirecka, E.A.1
  • 88
    • 70349696649 scopus 로고    scopus 로고
    • Affitoxin – a novel recombinant, HER2-specific, anticancer agent for targeted therapy of HER2-positive tumors
    • Zielinski, R., et al. Affitoxin – a novel recombinant, HER2-specific, anticancer agent for targeted therapy of HER2-positive tumors. J. Immunother. 32 (2009), 817–825.
    • (2009) J. Immunother. , vol.32 , pp. 817-825
    • Zielinski, R.1
  • 89
    • 79961003260 scopus 로고    scopus 로고
    • HER2-affitoxin: a potent therapeutic agent for the treatment of HER2-overexpressing tumors
    • Zielinski, R., et al. HER2-affitoxin: a potent therapeutic agent for the treatment of HER2-overexpressing tumors. Clin. Cancer Res. 17 (2011), 5071–5081.
    • (2011) Clin. Cancer Res. , vol.17 , pp. 5071-5081
    • Zielinski, R.1
  • 90
    • 84932646862 scopus 로고    scopus 로고
    • Target-specific cytotoxic effects on HER2-expressing cells by the tripartite fusion toxin ZHER2:2891-ABD-PE38X8, including a targeting affibody molecule and a half-life extension domain
    • Liu, H., et al. Target-specific cytotoxic effects on HER2-expressing cells by the tripartite fusion toxin ZHER2:2891-ABD-PE38X8, including a targeting affibody molecule and a half-life extension domain. Int. J. Oncol. 47 (2015), 601–609.
    • (2015) Int. J. Oncol. , vol.47 , pp. 601-609
    • Liu, H.1
  • 91
    • 84979587919 scopus 로고    scopus 로고
    • Fusion of an albumin-binding domain extends the half-life of immunotoxins
    • Guo, R., et al. Fusion of an albumin-binding domain extends the half-life of immunotoxins. Int. J. Pharm. 511 (2016), 538–549.
    • (2016) Int. J. Pharm. , vol.511 , pp. 538-549
    • Guo, R.1
  • 92
    • 84978531659 scopus 로고    scopus 로고
    • Influence of molecular design on biodistribution and targeting properties of an affibody-fused HER2-recognising anticancer toxin
    • Altai, M., et al. Influence of molecular design on biodistribution and targeting properties of an affibody-fused HER2-recognising anticancer toxin. Int. J. Oncol. 49 (2016), 1185–1194.
    • (2016) Int. J. Oncol. , vol.49 , pp. 1185-1194
    • Altai, M.1
  • 93
    • 84957703228 scopus 로고    scopus 로고
    • Immunogenicity of therapeutic recombinant immunotoxins
    • Mazor, R., et al. Immunogenicity of therapeutic recombinant immunotoxins. Immunol. Rev. 270 (2016), 152–164.
    • (2016) Immunol. Rev. , vol.270 , pp. 152-164
    • Mazor, R.1
  • 94
    • 84934897412 scopus 로고    scopus 로고
    • Designing the furin-cleavable linker in recombinant immunotoxins based on Pseudomonas exotoxin A
    • Weldon, J.E., et al. Designing the furin-cleavable linker in recombinant immunotoxins based on Pseudomonas exotoxin A. Bioconjug. Chem. 26 (2015), 1120–1128.
    • (2015) Bioconjug. Chem. , vol.26 , pp. 1120-1128
    • Weldon, J.E.1
  • 95
    • 84971207188 scopus 로고    scopus 로고
    • HER2-targeted immunotoxins with low nonspecific toxicity and immunogenicity
    • Guo, R., et al. HER2-targeted immunotoxins with low nonspecific toxicity and immunogenicity. Biochem. Biophys. Res. Commun. 475 (2016), 93–99.
    • (2016) Biochem. Biophys. Res. Commun. , vol.475 , pp. 93-99
    • Guo, R.1
  • 96
    • 84922691680 scopus 로고    scopus 로고
    • Advances in anticancer immunotoxin therapy
    • Alewine, C., et al. Advances in anticancer immunotoxin therapy. Oncologist 20 (2015), 176–185.
    • (2015) Oncologist , vol.20 , pp. 176-185
    • Alewine, C.1
  • 97
    • 84885661550 scopus 로고    scopus 로고
    • Receptor-directed chimeric toxins created by sortase-mediated protein fusion
    • McCluskey, A.J., Collier, R.J., Receptor-directed chimeric toxins created by sortase-mediated protein fusion. Mol. Cancer Ther. 12 (2013), 2273–2281.
    • (2013) Mol. Cancer Ther. , vol.12 , pp. 2273-2281
    • McCluskey, A.J.1    Collier, R.J.2
  • 98
    • 84878116059 scopus 로고    scopus 로고
    • Targeting HER2-positive cancer cells with receptor-redirected anthrax protective antigen
    • McCluskey, A.J., et al. Targeting HER2-positive cancer cells with receptor-redirected anthrax protective antigen. Mol. Oncol. 7 (2013), 440–451.
    • (2013) Mol. Oncol. , vol.7 , pp. 440-451
    • McCluskey, A.J.1
  • 99
    • 85010955862 scopus 로고    scopus 로고
    • Targeted delivery of an ADP-ribosylating bacterial toxin into cancer cells
    • Zahaf, N.I., et al. Targeted delivery of an ADP-ribosylating bacterial toxin into cancer cells. Sci. Rep., 7, 2017, 41252.
    • (2017) Sci. Rep. , vol.7 , pp. 41252
    • Zahaf, N.I.1
  • 100
    • 84970007003 scopus 로고    scopus 로고
    • A novel affibody-auristatin e conjugate with a potent and selective activity against HER2+ cell lines
    • Sochaj-Gregorczyk, A.M., A novel affibody-auristatin e conjugate with a potent and selective activity against HER2+ cell lines. J. Immunother. 39 (2016), 223–232.
    • (2016) J. Immunother. , vol.39 , pp. 223-232
    • Sochaj-Gregorczyk, A.M.1
  • 101
    • 85013004924 scopus 로고    scopus 로고
    • A conjugate based on anti-HER2 diaffibody and Auristatin E targets HER 2-positive cancer cells
    • Serwotka-Suszczak, A.M., et al. A conjugate based on anti-HER2 diaffibody and Auristatin E targets HER 2-positive cancer cells. Int. J. Mol. Sci., 2017, 18.
    • (2017) Int. J. Mol. Sci. , pp. 18
    • Serwotka-Suszczak, A.M.1
  • 102
    • 77949268342 scopus 로고    scopus 로고
    • (186)Re-maSGS-Z (HER2:342), a potential affibody conjugate for systemic therapy of HER2-expressing tumours
    • Orlova, A., et al. (186)Re-maSGS-Z (HER2:342), a potential affibody conjugate for systemic therapy of HER2-expressing tumours. Eur. J. Nucl. Med. Mol. Imaging 37 (2010), 260–269.
    • (2010) Eur. J. Nucl. Med. Mol. Imaging , vol.37 , pp. 260-269
    • Orlova, A.1
  • 103
    • 84907818093 scopus 로고    scopus 로고
    • Selection of an optimal cysteine-containing peptide-based chelator for labeling of affibody molecules with (188)Re
    • Altai, M., et al. Selection of an optimal cysteine-containing peptide-based chelator for labeling of affibody molecules with (188)Re. Eur. J. Med. Chem. 87 (2014), 519–528.
    • (2014) Eur. J. Med. Chem. , vol.87 , pp. 519-528
    • Altai, M.1
  • 104
    • 62149127839 scopus 로고    scopus 로고
    • Influence of valency and labelling chemistry on in vivo targeting using radioiodinated HER2-binding affibody molecules
    • Tolmachev, V., et al. Influence of valency and labelling chemistry on in vivo targeting using radioiodinated HER2-binding affibody molecules. Eur. J. Nucl. Med. Mol. Imaging 36 (2009), 692–701.
    • (2009) Eur. J. Nucl. Med. Mol. Imaging , vol.36 , pp. 692-701
    • Tolmachev, V.1
  • 105
    • 85027934622 scopus 로고    scopus 로고
    • Site-specific radioiodination of HER2-targeting affibody molecules using 4-Iodophenethylmaleimide decreases renal uptake of radioactivity
    • Strand, J., et al. Site-specific radioiodination of HER2-targeting affibody molecules using 4-Iodophenethylmaleimide decreases renal uptake of radioactivity. ChemistryOpen 4 (2015), 174–182.
    • (2015) ChemistryOpen , vol.4 , pp. 174-182
    • Strand, J.1
  • 106
    • 84937136212 scopus 로고    scopus 로고
    • Conformation-dependent binding and tumor-targeted delivery of siRNA by a designed TRBP2: affibody fusion protein
    • Dar, G.H., et al. Conformation-dependent binding and tumor-targeted delivery of siRNA by a designed TRBP2: affibody fusion protein. Nanomedicine 11 (2015), 1455–1466.
    • (2015) Nanomedicine , vol.11 , pp. 1455-1466
    • Dar, G.H.1
  • 107
    • 84960118391 scopus 로고    scopus 로고
    • Feasibility of affibody-based bioorthogonal chemistry-mediated radionuclide pretargeting
    • Altai, M., et al. Feasibility of affibody-based bioorthogonal chemistry-mediated radionuclide pretargeting. J. Nucl. Med. 57 (2016), 431–436.
    • (2016) J. Nucl. Med. , vol.57 , pp. 431-436
    • Altai, M.1
  • 108
    • 84954489812 scopus 로고    scopus 로고
    • Feasibility of affibody molecule-based pna-mediated radionuclide pretargeting of malignant tumors
    • Honarvar, H., et al. Feasibility of affibody molecule-based pna-mediated radionuclide pretargeting of malignant tumors. Theranostics 6 (2016), 93–103.
    • (2016) Theranostics , vol.6 , pp. 93-103
    • Honarvar, H.1
  • 109
    • 84939628085 scopus 로고    scopus 로고
    • Design, preparation, and characterization of PNA-based hybridization probes for affibody-molecule-mediated pretargeting
    • Westerlund, K., et al. Design, preparation, and characterization of PNA-based hybridization probes for affibody-molecule-mediated pretargeting. Bioconjug. Chem. 26 (2015), 1724–1736.
    • (2015) Bioconjug. Chem. , vol.26 , pp. 1724-1736
    • Westerlund, K.1
  • 110
    • 84905566532 scopus 로고    scopus 로고
    • Bispecific antibody complex pre-targeting and targeted delivery of polymer drug conjugates for imaging and therapy in dual human mammary cancer xenografts: targeted polymer drug conjugates for cancer diagnosis and therapy
    • Khaw, B.A., et al. Bispecific antibody complex pre-targeting and targeted delivery of polymer drug conjugates for imaging and therapy in dual human mammary cancer xenografts: targeted polymer drug conjugates for cancer diagnosis and therapy. Eur. J. Nucl. Med. Mol. Imaging 41 (2014), 1603–1616.
    • (2014) Eur. J. Nucl. Med. Mol. Imaging , vol.41 , pp. 1603-1616
    • Khaw, B.A.1
  • 111
    • 85008394558 scopus 로고    scopus 로고
    • An in vitro demonstration of overcoming drug resistance in SKOV3 TR and MCF7 ADR with targeted delivery of polymer pro-drug conjugates
    • Bhattarai, P., et al. An in vitro demonstration of overcoming drug resistance in SKOV3 TR and MCF7 ADR with targeted delivery of polymer pro-drug conjugates. J. Drug Target. 25 (2017), 436–450.
    • (2017) J. Drug Target. , vol.25 , pp. 436-450
    • Bhattarai, P.1
  • 112
    • 84893061341 scopus 로고    scopus 로고
    • Modular adeno-associated virus (rAAV) vectors used for cellular virus-directed enzyme prodrug therapy
    • Hagen, S., et al. Modular adeno-associated virus (rAAV) vectors used for cellular virus-directed enzyme prodrug therapy. Sci. Rep., 4, 2014, 3759.
    • (2014) Sci. Rep. , vol.4 , pp. 3759
    • Hagen, S.1
  • 113
    • 84975461212 scopus 로고    scopus 로고
    • Targeted delivery of deoxycytidine kinase to Her2-positive cells enhances the efficacy of the nucleoside analog fludarabine
    • Koduvayur, S.P., et al. Targeted delivery of deoxycytidine kinase to Her2-positive cells enhances the efficacy of the nucleoside analog fludarabine. PLoS One, 11, 2016, e0157114.
    • (2016) PLoS One , vol.11 , pp. e0157114
    • Koduvayur, S.P.1
  • 114
    • 84930903226 scopus 로고    scopus 로고
    • A new prodrug form of affibody molecules (pro-affibody) is selectively activated by cancer-associated proteases
    • Sandersjoo, L., et al. A new prodrug form of affibody molecules (pro-affibody) is selectively activated by cancer-associated proteases. Cell. Mol. Life Sci. 72 (2015), 1405–1415.
    • (2015) Cell. Mol. Life Sci. , vol.72 , pp. 1405-1415
    • Sandersjoo, L.1
  • 115
    • 85006892930 scopus 로고    scopus 로고
    • Affibody-displaying bio-nanocapsules effective in EGFR, typical biomarker, expressed in various cancer cells
    • Nishimura, Y., et al. Affibody-displaying bio-nanocapsules effective in EGFR, typical biomarker, expressed in various cancer cells. Bioorg. Med. Chem. Lett. 27 (2017), 336–341.
    • (2017) Bioorg. Med. Chem. Lett. , vol.27 , pp. 336-341
    • Nishimura, Y.1
  • 116
    • 85008941857 scopus 로고    scopus 로고
    • DNA-affibody nanoparticles for inhibiting breast cancer cells overexpressing HER2
    • Zhang, Y., et al. DNA-affibody nanoparticles for inhibiting breast cancer cells overexpressing HER2. Chem. Commun. (Camb) 53 (2017), 573–576.
    • (2017) Chem. Commun. (Camb) , vol.53 , pp. 573-576
    • Zhang, Y.1
  • 117
    • 84959539506 scopus 로고    scopus 로고
    • Improved therapeutic activity of HER2 affibody-targeted cisplatin liposomes in HER2-expressing breast tumor models
    • Alavizadeh, S.H., Improved therapeutic activity of HER2 affibody-targeted cisplatin liposomes in HER2-expressing breast tumor models. Expert Opin. Drug Deliv. 13 (2016), 325–336.
    • (2016) Expert Opin. Drug Deliv. , vol.13 , pp. 325-336
    • Alavizadeh, S.H.1
  • 118
    • 84922238908 scopus 로고    scopus 로고
    • Nanobubble-affibody: novel ultrasound contrast agents for targeted molecular ultrasound imaging of tumor
    • Yang, H., et al. Nanobubble-affibody: novel ultrasound contrast agents for targeted molecular ultrasound imaging of tumor. Biomaterials 37 (2015), 279–288.
    • (2015) Biomaterials , vol.37 , pp. 279-288
    • Yang, H.1
  • 119
    • 84957989602 scopus 로고    scopus 로고
    • Smart cancer cell targeting imaging and drug delivery system by systematically engineering periodic mesoporous organosilica nanoparticles
    • Lu, N., et al. Smart cancer cell targeting imaging and drug delivery system by systematically engineering periodic mesoporous organosilica nanoparticles. ACS Appl. Mater. Interfaces 8 (2016), 2985–2993.
    • (2016) ACS Appl. Mater. Interfaces , vol.8 , pp. 2985-2993
    • Lu, N.1
  • 120
    • 84955099141 scopus 로고    scopus 로고
    • Bioengineered yeast-derived vacuoles with enhanced tissue-penetrating ability for targeted cancer therapy
    • Gujrati, V., et al. Bioengineered yeast-derived vacuoles with enhanced tissue-penetrating ability for targeted cancer therapy. Proc. Natl. Acad. Sci. U. S. A. 113 (2016), 710–715.
    • (2016) Proc. Natl. Acad. Sci. U. S. A. , vol.113 , pp. 710-715
    • Gujrati, V.1
  • 121
    • 85007545211 scopus 로고    scopus 로고
    • Engineering hepatitis B virus core particles for targeting HER2 receptors in vitro and in vivo
    • Mohamed Suffian, I.F., Engineering hepatitis B virus core particles for targeting HER2 receptors in vitro and in vivo. Biomaterials 120 (2017), 126–138.
    • (2017) Biomaterials , vol.120 , pp. 126-138
    • Mohamed Suffian, I.F.1
  • 122
    • 84946867392 scopus 로고    scopus 로고
    • Photosensitizer and peptide-conjugated PAMAM dendrimer for targeted in vivo photodynamic therapy
    • Narsireddy, A., et al. Photosensitizer and peptide-conjugated PAMAM dendrimer for targeted in vivo photodynamic therapy. Int. J. Nanomed. 10 (2015), 6865–6878.
    • (2015) Int. J. Nanomed. , vol.10 , pp. 6865-6878
    • Narsireddy, A.1
  • 123
    • 84902335869 scopus 로고    scopus 로고
    • Targeted in vivo photodynamic therapy with epidermal growth factor receptor-specific peptide linked nanoparticles
    • Narsireddy, A., et al. Targeted in vivo photodynamic therapy with epidermal growth factor receptor-specific peptide linked nanoparticles. Int. J. Pharm. 471 (2014), 421–429.
    • (2014) Int. J. Pharm. , vol.471 , pp. 421-429
    • Narsireddy, A.1
  • 124
    • 85000717966 scopus 로고    scopus 로고
    • Multifunctional conjugated polymer nanoparticles for image-guided photodynamic and photothermal therapy
    • Feng, G., et al. Multifunctional conjugated polymer nanoparticles for image-guided photodynamic and photothermal therapy. Small, 13, 2017.
    • (2017) Small , vol.13
    • Feng, G.1
  • 125
    • 78650180317 scopus 로고    scopus 로고
    • Affinity recovery of eight HER2-binding affibody variants using an anti-idiotypic affibody molecule as capture ligand
    • Wallberg, H., et al. Affinity recovery of eight HER2-binding affibody variants using an anti-idiotypic affibody molecule as capture ligand. Protein Exp. Purif. 76 (2011), 127–135.
    • (2011) Protein Exp. Purif. , vol.76 , pp. 127-135
    • Wallberg, H.1
  • 126
    • 0037102973 scopus 로고    scopus 로고
    • Anti-idiotypic protein domains selected from protein A-based affibody libraries
    • Eklund, M., et al. Anti-idiotypic protein domains selected from protein A-based affibody libraries. Proteins 48 (2002), 454–462.
    • (2002) Proteins , vol.48 , pp. 454-462
    • Eklund, M.1
  • 127
    • 85013082953 scopus 로고    scopus 로고
    • Affibody scaffolds improve sesquiterpene production in Saccharomyces cerevisiae
    • Tippmann, S., et al. Affibody scaffolds improve sesquiterpene production in Saccharomyces cerevisiae. ACS Synth. Biol. 6 (2016), 19–28.
    • (2016) ACS Synth. Biol. , vol.6 , pp. 19-28
    • Tippmann, S.1
  • 128
    • 84994424564 scopus 로고    scopus 로고
    • One-pot construction of Quenchbodies using antibody-binding proteins
    • Jeong, H.-J., et al. One-pot construction of Quenchbodies using antibody-binding proteins. Anal. Methods 8 (2016), 7774–7779.
    • (2016) Anal. Methods , vol.8 , pp. 7774-7779
    • Jeong, H.-J.1
  • 129
    • 85000866066 scopus 로고    scopus 로고
    • Plug-and-playable fluorescent cell imaging modular toolkits using the bacterial superglue, SpyTag/SpyCatcher
    • Moon, H., et al. Plug-and-playable fluorescent cell imaging modular toolkits using the bacterial superglue, SpyTag/SpyCatcher. Chem. Commun. (Camb) 52 (2016), 14051–14054.
    • (2016) Chem. Commun. (Camb) , vol.52 , pp. 14051-14054
    • Moon, H.1
  • 130
    • 84920140497 scopus 로고    scopus 로고
    • Analytical applications of affibodies
    • Justino, C.I.L., et al. Analytical applications of affibodies. TrAC Trends Anal. Chem. 65 (2015), 73–82.
    • (2015) TrAC Trends Anal. Chem. , vol.65 , pp. 73-82
    • Justino, C.I.L.1
  • 131
    • 44849128916 scopus 로고    scopus 로고
    • Generation of affibody ligands binding interleukin-2 receptor alpha/CD25
    • Gronwall, C., et al. Generation of affibody ligands binding interleukin-2 receptor alpha/CD25. Biotechnol. Appl. Biochem. 50 (2008), 97–112.
    • (2008) Biotechnol. Appl. Biochem. , vol.50 , pp. 97-112
    • Gronwall, C.1
  • 132
    • 0142184270 scopus 로고    scopus 로고
    • Inhibition of the CD28-CD80 co-stimulation signal by a CD28-binding affibody ligand developed by combinatorial protein engineering
    • Sandström, K., et al. Inhibition of the CD28-CD80 co-stimulation signal by a CD28-binding affibody ligand developed by combinatorial protein engineering. Protein Eng. 16 (2003), 691–697.
    • (2003) Protein Eng. , vol.16 , pp. 691-697
    • Sandström, K.1
  • 133
    • 62849118728 scopus 로고    scopus 로고
    • Selection and characterization of affibody ligands to the transcription factor c-Jun
    • Lundberg, E., et al. Selection and characterization of affibody ligands to the transcription factor c-Jun. Biotechnol. Appl. Biochem. 52 (2009), 17–27.
    • (2009) Biotechnol. Appl. Biochem. , vol.52 , pp. 17-27
    • Lundberg, E.1
  • 134
    • 0034832744 scopus 로고    scopus 로고
    • Recombinant human factor VIII-specific affinity ligands selected from phage-displayed combinatorial libraries of protein A
    • Nord, K., et al. Recombinant human factor VIII-specific affinity ligands selected from phage-displayed combinatorial libraries of protein A. Eur. J. Biochem. 268 (2001), 4269–4277.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4269-4277
    • Nord, K.1
  • 135
    • 33748525178 scopus 로고    scopus 로고
    • Selection and characterization of an HIV-1 gp120-binding affibody ligand
    • Wikman, M., et al. Selection and characterization of an HIV-1 gp120-binding affibody ligand. Biotechnol. Appl. Biochem. 45 (2006), 93–105.
    • (2006) Biotechnol. Appl. Biochem. , vol.45 , pp. 93-105
    • Wikman, M.1
  • 136
    • 0036275295 scopus 로고    scopus 로고
    • Human immunoglobulin A (IgA)-specific ligands from combinatorial engineering of protein A
    • Ronnmark, J., et al. Human immunoglobulin A (IgA)-specific ligands from combinatorial engineering of protein A. Eur. J. Biochem. 269 (2002), 2647–2655.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2647-2655
    • Ronnmark, J.1
  • 137
    • 84885003922 scopus 로고    scopus 로고
    • High-affinity binding to staphylococcal protein A by an engineered dimeric affibody molecule
    • Lindborg, M., et al. High-affinity binding to staphylococcal protein A by an engineered dimeric affibody molecule. Protein Eng. Des. Sel. 26 (2013), 635–644.
    • (2013) Protein Eng. Des. Sel. , vol.26 , pp. 635-644
    • Lindborg, M.1
  • 138
    • 0033103888 scopus 로고    scopus 로고
    • An in vitro selected binding protein (affibody) shows conformation-dependent recognition of the respiratory syncytial virus (RSV) G protein
    • Hansson, M., et al. An in vitro selected binding protein (affibody) shows conformation-dependent recognition of the respiratory syncytial virus (RSV) G protein. Immunotechnology 4 (1999), 237–252.
    • (1999) Immunotechnology , vol.4 , pp. 237-252
    • Hansson, M.1
  • 139
    • 0032717780 scopus 로고    scopus 로고
    • Affinity maturation of a Taq DNA polymerase specific affibody by helix shuffling
    • Gunneriusson, E., Affinity maturation of a Taq DNA polymerase specific affibody by helix shuffling. Protein Eng. 12 (1999), 873–878.
    • (1999) Protein Eng. , vol.12 , pp. 873-878
    • Gunneriusson, E.1
  • 140
    • 77953131705 scopus 로고    scopus 로고
    • Affinity maturation of a TNFalpha-binding affibody molecule by Darwinian survival selection
    • Lofdahl, P.A., Nygren, P.A., Affinity maturation of a TNFalpha-binding affibody molecule by Darwinian survival selection. Biotechnol. Appl. Biochem. 55 (2010), 111–120.
    • (2010) Biotechnol. Appl. Biochem. , vol.55 , pp. 111-120
    • Lofdahl, P.A.1    Nygren, P.A.2
  • 141
    • 36448987572 scopus 로고    scopus 로고
    • Affibody-mediated transferrin depletion for proteomics applications
    • Gronwall, C., et al. Affibody-mediated transferrin depletion for proteomics applications. Biotechnol. J. 2 (2007), 1389–1398.
    • (2007) Biotechnol. J. , vol.2 , pp. 1389-1398
    • Gronwall, C.1
  • 142
    • 85015956694 scopus 로고    scopus 로고
    • A gradient of sitewise diversity promotes evolutionary fitness for binder discovery in a three-helix bundle protein scaffold
    • Woldring, D.R., et al. A gradient of sitewise diversity promotes evolutionary fitness for binder discovery in a three-helix bundle protein scaffold. Biochemistry 56 (2017), 1656–1671.
    • (2017) Biochemistry , vol.56 , pp. 1656-1671
    • Woldring, D.R.1
  • 143
    • 84880724831 scopus 로고    scopus 로고
    • PASylation: a biological alternative to PEGylation for extending the plasma half-life of pharmaceutically active proteins
    • Schlapschy, M., et al. PASylation: a biological alternative to PEGylation for extending the plasma half-life of pharmaceutically active proteins. Protein Eng. Des. Sel. 26 (2013), 489–501.
    • (2013) Protein Eng. Des. Sel. , vol.26 , pp. 489-501
    • Schlapschy, M.1
  • 144
    • 84991510807 scopus 로고    scopus 로고
    • Extension of in vivo half-life of biologically active molecules by XTEN protein polymers
    • Podust, V.N., et al. Extension of in vivo half-life of biologically active molecules by XTEN protein polymers. J. Control. Release 240 (2016), 52–66.
    • (2016) J. Control. Release , vol.240 , pp. 52-66
    • Podust, V.N.1
  • 145
    • 84924964395 scopus 로고    scopus 로고
    • Optimization of liganded polyethylenimine polyethylene glycol vector for nucleic acid delivery
    • Joubran, S., et al. Optimization of liganded polyethylenimine polyethylene glycol vector for nucleic acid delivery. Bioconjug. Chem. 25 (2014), 1644–1654.
    • (2014) Bioconjug. Chem. , vol.25 , pp. 1644-1654
    • Joubran, S.1
  • 146
    • 67649240316 scopus 로고    scopus 로고
    • Targeting of epidermal growth factor receptor (EGFR)-expressing tumor cells with sterically stabilized affibody liposomes (SAL)
    • Beuttler, J., et al. Targeting of epidermal growth factor receptor (EGFR)-expressing tumor cells with sterically stabilized affibody liposomes (SAL). Bioconjug. Chem. 20 (2009), 1201–1208.
    • (2009) Bioconjug. Chem. , vol.20 , pp. 1201-1208
    • Beuttler, J.1
  • 147
    • 84990060473 scopus 로고    scopus 로고
    • Human serum albumin and HER2-binding affibody fusion proteins for targeted delivery of fatty acid-modified molecules and therapy
    • Dong, D., et al. Human serum albumin and HER2-binding affibody fusion proteins for targeted delivery of fatty acid-modified molecules and therapy. Mol. Pharm. 13 (2016), 3370–3380.
    • (2016) Mol. Pharm. , vol.13 , pp. 3370-3380
    • Dong, D.1
  • 148
    • 47649128420 scopus 로고    scopus 로고
    • Engineering of a femtomolar affinity binding protein to human serum albumin
    • Jonsson, A., et al. Engineering of a femtomolar affinity binding protein to human serum albumin. Protein Eng. Des. Sel. 21 (2008), 515–527.
    • (2008) Protein Eng. Des. Sel. , vol.21 , pp. 515-527
    • Jonsson, A.1
  • 149
    • 84886143165 scopus 로고    scopus 로고
    • Half-life extension by binding to albumin through an albumin binding domain
    • R. Kontermann Wiley-VCH Verlag GmbH & Co. KGaA
    • Frejd, F.Y., Half-life extension by binding to albumin through an albumin binding domain. Kontermann, R., (eds.) Therapeutic Proteins: Strategies to Modulate their Plasma Half-Lives, 2012, Wiley-VCH Verlag GmbH & Co. KGaA, 269–283, 10.1002/9783527644827.ch14.
    • (2012) Therapeutic Proteins: Strategies to Modulate their Plasma Half-Lives , pp. 269-283
    • Frejd, F.Y.1
  • 150
    • 79953131275 scopus 로고    scopus 로고
    • Extending half-life by indirect targeting of the neonatal Fc receptor (FcRn) using a minimal albumin binding domain
    • Andersen, J.T., et al. Extending half-life by indirect targeting of the neonatal Fc receptor (FcRn) using a minimal albumin binding domain. J. Biol. Chem. 286 (2011), 5234–5241.
    • (2011) J. Biol. Chem. , vol.286 , pp. 5234-5241
    • Andersen, J.T.1
  • 151
    • 84922005237 scopus 로고    scopus 로고
    • A GLP-1 receptor agonist conjugated to an albumin-binding domain for extended half-life
    • Lindgren, J., et al. A GLP-1 receptor agonist conjugated to an albumin-binding domain for extended half-life. Biopolymers 102 (2014), 252–259.
    • (2014) Biopolymers , vol.102 , pp. 252-259
    • Lindgren, J.1
  • 152
    • 84915818878 scopus 로고    scopus 로고
    • An engineered affibody molecule with pH-dependent binding to FcRn mediates extended circulatory half-life of a fusion protein
    • Seijsing, J., et al. An engineered affibody molecule with pH-dependent binding to FcRn mediates extended circulatory half-life of a fusion protein. Proc. Natl. Acad. Sci. U. S. A. 111 (2014), 17110–17115.
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 17110-17115
    • Seijsing, J.1


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