Affibody molecules as engineered protein drugs
Open accessAbstract
Affibody molecules can be used as tools for molecular recognition in diagnostic and therapeutic applications. There are several preclinical studies reported on diagnostic and therapeutic use of this molecular class of alternative scaffolds, and early clinical evidence is now beginning to accumulate that suggests the Affibody molecules to be efficacious and safe in man. The small size and ease of engineering make Affibody molecules suitable for use in multispecific constructs where AffiMabs is one such that offers the option to potentiate antibodies for use in complex disease.
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A wide variety of binding specificities can be encoded in simple helical bundles.
“Consistent with previous observations with affibodies41, this result indicates that a wide variety of binding specificities can be encoded in simple helical bundles.”
From Design of protein-binding proteins from the target structure alone (2022) · cites this paper as [41]
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Novel affinity binders for neutralization of vascular endothelial growth factor (VEGF) signaling
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Early treatment with eculizumab in atypical haemolytic uraemic syndrome
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The clinical potential of Affibody-based inhibitors of C5 for therapeutic complement disruption
Berglund, M. M., & Strömberg, P. (2016) · Expert Review of Proteomics · doi:10.1586/14789450.2016.1148604 · Cited by 9 · see citing works
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Design of protein-binding proteins from the target structure alone
Cao, L., Coventry, B., Goreshnik, I., Huang, B., Sheffler, W., Park, J. S., Jude, K. M., Marković, I., Kadam, R. U., Verschueren, K. H. G., et al. (2022) · Nature · doi:10.1038/s41586-022-04654-9 · Cited by 577 · see citing works
Bai, J., Qiu, S.-Q., & Zhang, G. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01366-y · Cited by 217 · see citing works
“Several affibody molecules with high affinity to VEGFR2, EGFR, HER2, HER3, and IGF-1R have been demonstrated as probes for radionuclide or fluorescent molecular imaging in preclinical settings.(167,173) Clinical evaluation of radiolabeled affibody molecules has been explored for HER2 imaging and fluorescent dye-labele…”
BackgroundBertók, T., Lorencová, L., Chocholova, E., Jáné, E., Vikartovská, A., Kasák, P., & Tkáč, J. (2018) · ChemElectroChem · doi:10.1002/celc.201800848 · Cited by 180 · see citing works
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Engineered Protein Scaffolds as Next-Generation Therapeutics
Gebauer, M., & Skerra, A. (2020) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010818-021118 · Cited by 164 · see citing works
The Dawn of a New Era: Targeting the “Undruggables” with Antibody-Based Therapeutics
Qian, L., Lin, X., Gao, X., Khan, R. U., Liao, J., Du, S., Ge, J., Zeng, S., & Yao, S. Q. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.2c00915 · Cited by 156 · see citing works
Nonenzymatic Stereoselective S -Glycosylation of Polypeptides and Proteins
Wan, L.-Q., Zhang, X., Zou, Y., Shi, R., Cao, J.-G., Xu, S., Deng, L., Zhou, L., Gong, Y., Shu, X., et al. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c05156 · Cited by 131 · see citing works
Parisi, O. I., Francomano, F., Dattilo, M., Patitucci, F., Prete, S., Amone, F., & Puoci, F. (2022) · Journal of Functional Biomaterials · doi:10.3390/jfb13010012 · Cited by 134 · see citing works
“- affibodies (protein scaffolds), which are the result of protein engineering: they consist of a scaffold protein, made up of the IgG of a bacterial protein, on which a three-helix protein is inserted [62,72]; - RGD peptides, which are cyclic peptides formed of three amino acids, such as arginine, glycine and aspartic…”
BackgroundKaufman, N. E. M., Dhingra, S., Jois, S. D. S., & Vicente, M. G. H. (2021) · Molecules · doi:10.3390/molecules26041076 · Cited by 134 · see citing works
“Moreover, these small proteins can be conjugated to different imaging probes [128,129].”
BackgroundAntibody Fragment and Affibody ImmunoPET Imaging Agents: Radiolabelling Strategies and Applications
Fu, R., Carroll, L. S., Yahioglu, G., Aboagye, E. O., & Miller, P. W. (2018) · ChemMedChem · doi:10.1002/cmdc.201800624 · Cited by 126 · see citing works
Photodynamic Therapy: Targeting Cancer Biomarkers for the Treatment of Cancers
Wang, X.-N., Luo, D., & Basilion, J. (2021) · Cancers · doi:10.3390/cancers13122992 · Cited by 108 · see citing works
Hidradenitis suppurativa: new insights into disease mechanisms and an evolving treatment landscape
Krueger, J. G., Frew, J. W., Jemec, G. B. E., Kimball, A. B., Kirby, B., Bechara, F. G., Navrazhina, K., Prens, E. P., Reich, K., Cullen, E., et al. (2023) · British Journal of Dermatology · doi:10.1093/bjd/ljad345 · Cited by 115 · see citing works
Peltek, O. O., Muslimov, A. R., Zyuzin, M. V., & Timin, A. S. (2019) · Journal of Nanobiotechnology · doi:10.1186/s12951-019-0524-9 · Cited by 109 · see citing works
Soluble ligands as drug targets
Attwood, M. M., Jonsson, J., Rask‐Andersen, M., & Schiöth, H. B. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-0078-4 · Cited by 110 · see citing works
Advances in psoriasis research: From pathogenesis to therapeutics
Sugumaran, D., Yong, A. C. H., & Stanslas, J. (2024) · Life Sciences · doi:10.1016/j.lfs.2024.122991 · Cited by 108 · see citing works
From Whispering Gallery Mode Resonators to Biochemical Sensors
Loyez, M., Adolphson, M., Liao, J., & Yang, L. (2023) · ACS Sensors · doi:10.1021/acssensors.2c02876 · Cited by 107 · see citing works
Principles and Current Clinical Landscape of Multispecific Antibodies against Cancer
Elshiaty, M., Schindler, H., & Christopoulos, P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115632 · Cited by 98 · see citing works
Small-Format Drug Conjugates: A Viable Alternative to ADCs for Solid Tumours?
Deonarain, M. P., Yahioglu, G., Stamati, I., Pomowski, A., Clarke, J., Edwards, B. M., Diez-Posada, S., & Stewart, A. (2018) · Antibodies · doi:10.3390/antib7020016 · Cited by 92 · see citing works
“These are one of the oldest known non-antibody binding scaffolds (reported ~20 years ago) and have predominantly been developed as imaging or anti-inflammatory agents with clinical candidates [67,68].”
BackgroundIslam, T., Hasan, M. M., Awal, A., Nurunnabi, M., & Ahammad, A. J. S. (2020) · Molecules · doi:10.3390/molecules25245787 · Cited by 89 · see citing works
“These affibodies are often paired with various metal nanoparticles to further enhance their efficacy [99].”
BackgroundDesigner Oncolytic Adenovirus: Coming of Age
Baker, A. T., Hernandez, C. A., Halldén, G., & Parker, A. L. (2018) · Cancers · doi:10.3390/cancers10060201 · Cited by 84 · see citing works
“5 kDa), the ability to achieve picomolar affinities, and ability to correctly fold in the cytosol [242,243].”
BackgroundMiniproteins as a Powerful Modality in Drug Development
Crook, Z. R., Nairn, N. W., & Olson, J. M. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2019.12.008 · Cited by 87 · see citing works
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Imaging using radiolabelled targeted proteins: radioimmunodetection and beyond
Garousi, J., Orlova, A., Frejd, F. Y., & Максимилианович, Т. В. (2020) · EJNMMI Radiopharmacy and Chemistry · doi:10.1186/s41181-020-00094-w · Cited by 73 · see citing works
Self-citationProgress and Future Directions with Peptide-Drug Conjugates for Targeted Cancer Therapy
Lindberg, J., Nilvebrant, J., Nygren, P., & Lehmann, F. (2021) · Molecules · doi:10.3390/molecules26196042 · Cited by 72 · see citing works
Protein scaffolds: antibody alternatives for cancer diagnosis and therapy
Luo, R., Liu, H., & Cheng, Z. (2022) · RSC Chemical Biology · doi:10.1039/d2cb00094f · Cited by 71 · see citing works
Protein binders and their applications in developmental biology
Harmansa, S., & Affolter, M. (2018) · Development · doi:10.1242/dev.148874 · Cited by 69 · see citing works
Nanocarriers as Magic Bullets in the Treatment of Leukemia
Houshmand, M., Garello, F., Circosta, P., Stefanìa, R., Aime, S., Saglio, G. N., & Giachino, C. (2020) · Nanomaterials · doi:10.3390/nano10020276 · Cited by 63 · see citing works
“In contrast to antibodies that have the Fc-portion, however, they lack half-life extension and effector function modules [97].”
BackgroundMohiuddin, T. M., Zhang, C., Sheng, W., Al-Rawe, M., Zeppernick, F. A., Meinhold-Heerlein, I. M., & Hussain, A. F. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24032655 · Cited by 63 · see citing works
“However, NIRPIT can be applied to any cancer or regulatory cell in the tumor microenvironment if the available tumor antigens are overexpressed [47].”
BackgroundMethodInfluentialNatural Killer Cell Engagers (NKCEs): a new frontier in cancer immunotherapy
Zhang, M., Lam, K., & Xu, S. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1207276 · Cited by 67 · see citing works
Development and Differentiation in Monobodies Based on the Fibronectin Type 3 Domain
Chandler, P. G., & Buckle, A. M. (2020) · Cells · doi:10.3390/cells9030610 · Cited by 60 · see citing works
“The advantage of a tailored approach is that wildtype functions of each domain can be leveraged to overcome limitations of the traditional immunoglobulin fold, such as the modular construction of DARPins [7], convex binding surfaces of Affibodies [8] or protease targeting in Kunitz domains [9].”
BackgroundRecent Advances in Half-life Extension Strategies for Therapeutic Peptides and Proteins
Tan, H., Su, W., Zhang, W., Wang, P., Sattler, M., & Zou, P. (2019) · Current Pharmaceutical Design · doi:10.2174/1381612825666190206105232 · Cited by 59 · see citing works
“Affibody molecules, which can be efficiently produced in bacteria, are a class of small affinity proteins with high thermostability and anti-enzymatic properties that can be used as tools for molecular recognition in diagnostic and therapeutic applications [91, 92].”
BackgroundKlint, S., Feldwisch, J., Gudmundsdotter, L., Bergstedt, K. D., Gunneriusson, E., Höidén‐Guthenberg, I., Wennborg, A., Nyborg, A. C., Kamboj, A. P., Peloso, P. M. J., et al. (2023) · mAbs · doi:10.1080/19420862.2023.2209920 · Cited by 59 · see citing works
“6 kDa IL-17 ligand trap comprising one IL-17A-specific Affibody domain at each side of an albumin-binding domain (izokibep) (Figure 1a).(39) The ligand trap format of izokibep increased the inhibitory capacity when compared to the monomeric precursor.”
BackgroundSelf-citationDevelopment of light-responsive protein binding in the monobody non-immunoglobulin scaffold
Carrasco‐López, C., Zhao, E. M., Gil, A. A., Alam, N., Toettcher, J. E., & Avalos, J. L. (2020) · Nature Communications · doi:10.1038/s41467-020-17837-7 · Cited by 58 · see citing works
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Aligning physics and physiology: E ngineering antibodies for radionuclide delivery
Tsai, W. K., & Wu, A. M. (2018) · Journal of Labelled Compounds and Radiopharmaceuticals · doi:10.1002/jlcr.3622 · Cited by 50 · see citing works
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Tackling Undruggable Targets with Designer Peptidomimetics and Synthetic Biologics
Swenson, C., Mandava, G., Thomas, D. M., & Moellering, R. E. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00423 · Cited by 48 · see citing works
Modulation of virus-induced NF-κB signaling by NEMO coiled coil mimics
Sadek, J., Wuo, M. G., Rooklin, D. W., Hauenstein, A. V., Hong, S. H., Gautam, A. S., Wu, H., Zhang, Y., Cesarman, E., & Arora, P. S. (2020) · Nature Communications · doi:10.1038/s41467-020-15576-3 · Cited by 45 · see citing works
Recent Advances in the Molecular Design and Applications of Multispecific Biotherapeutics
Zhong, X., & D’Antona, A. M. (2021) · Antibodies · doi:10.3390/antib10020013 · Cited by 45 · see citing works
Bio-Nanocarriers for Lung Cancer Management: Befriending the Barriers
Rawal, S. U., & Patel, M. M. (2021) · Nano-Micro Letters · doi:10.1007/s40820-021-00630-6 · Cited by 45 · see citing works
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Application of Fluorescence-Guided Surgery to Subsurface Cancers Requiring Wide Local Excision
Samkoe, K. S., Bates, B. D., Elliott, J. T., LaRochelle, E. P. M., Gunn, J. R., Marra, K. A., Feldwisch, J., Ramkumar, D. B., Bauer, D. F., Paulsen, K. D., et al. (2018) · Cancer Control · doi:10.1177/1073274817752332 · Cited by 40 · see citing works
“Muscle was used as a reference tissue because it is known to be devoid of EGFR.”
BackgroundInfluentialShipunova, V. O., Sogomonyan, A. S., Zelepukin, I. V., Nikitin, M. P., & Deyev, S. M. (2021) · Molecules · doi:10.3390/molecules26133955 · Cited by 39 · see citing works
“These molecules are originally based on the Z domain (the immunoglobulin G binding domain) of protein A and are made via the randomization of 13 amino acids located in two alpha-helices involved in the target binding in the original protein [39,40].”
BackgroundReview on Metal-Based Theranostic Nanoparticles for Cancer Therapy and Imaging
Fernandes, D. A. (2023) · Technology in Cancer Research & Treatment · doi:10.1177/15330338231191493 · Cited by 44 · see citing works
Synthetic Control of Tertiary Helical Structures in Short Peptides
Wuo, M. G., Hong, S. H., Singh, A., & Arora, P. S. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b10082 · Cited by 38 · see citing works
Protein-Catalyzed Capture Agents
Agnew, H. D., Coppock, M. B., Idso, M. N., Lai, B. T., Liang, J., McCarthy, A., Warren, C. M., & Heath, J. R. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00660 · Cited by 38 · see citing works
Barozzi, A., Lavoie, R. A., Day, K. N., Prodromou, R., & Menegatti, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113769 · Cited by 37 · see citing works
“Thus, despite their therapeutic potential [28] and having received Food and Drug Administration (FDA) approval for clinical treatment [29], affibodies are available on the market in limited amounts and high price.”
BackgroundDriving CARs with alternative navigation tools – the potential of engineered binding scaffolds
Zajc, C. U., Salzer, B., Taft, J. M., Reddy, S. T., Lehner, M., & Traxlmayr, M. W. (2020) · FEBS Journal · doi:10.1111/febs.15523 · Cited by 37 · see citing works
Palladium-Mediated Incorporation of Carboranes into Small Molecules, Peptides, and Proteins
Gazvoda, M., Dhanjee, H. H., Rodriguez, J., Brown, J. S., Farquhar, C. E., Truex, N. L., Loas, A., Buchwald, S. L., & Pentelute, B. L. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c01932 · Cited by 37 · see citing works
A novel HPV16 E7-affitoxin for targeted therapy of HPV16-induced human cervical cancer
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Discovery, optimization and biodistribution of an Affibody molecule for imaging of CD69
Persson, J., Puuvuori, E., Zhang, B., Velikyan, I., Åberg, O., Müller, M., Nygren, P., Ståhl, S., Korsgren, O., Eriksson, O., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-97694-6 · Cited by 34 · see citing works
Near-Infrared Photoimmunotherapy Using a Small Protein Mimetic for HER2-Overexpressing Breast Cancer
Yamaguchi, H., Pantarat, N., Suzuki, T., & Evdokiou, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20235835 · Cited by 34 · see citing works
“Firstly, Affibody (6–7 kDa) has a rapid clearance and a good tumor penetration [15,16].”
BackgroundBam, R., Lown, P. S., Stern, L. A., Sharma, K., Wilson, K. E., Bean, G. R., Lutz, A. M., Paulmurugan, R., Hackel, B. J., Dahl, J., et al. (2020) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-19-1655 · Cited by 34 · see citing works
“Compared with antibodies, ABY exhibit faster renal clearance (33), greater stability at a wide range of physiologic pH and temperature, are cost-effective for larger-scale production, and enable site-specific conjugation (34).”
BackgroundRennig, M., Martínez, V., Mirzadeh, K., Dunås, F., Röjsäter, B., Daley, D. O., & Nørholm, M. H. H. (2017) · ACS Synthetic Biology · doi:10.1021/acssynbio.7b00200 · Cited by 33 · see citing works
Altai, M., Leitao, C. D., Rinne, S. S., Vorobyeva, A., Atterby, C., Ståhl, S., Максимилианович, Т. В., Löfblom, J., & Orlova, A. (2018) · Cells · doi:10.3390/cells7100164 · Cited by 33 · see citing works
“This is typical for affibody molecules as they have a size below the kidney cut-off (<60 kDa) [11].”
Engineering of binding functions into proteins
Gebauer, M., & Skerra, A. (2019) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2019.05.007 · Cited by 33 · see citing works
Recombinant immunotoxins development for HER2-based targeted cancer therapies
Mahmoudi, R., Dianat‐Moghadam, H., Poorebrahim, M., Siapoush, S., Poortahmasebi, V., Salahlou, R., & Rahmati, M. (2021) · Cancer Cell International · doi:10.1186/s12935-021-02182-6 · Cited by 34 · see citing works
Ahirwar, R. (2021) · Microchimica Acta · doi:10.1007/s00604-021-04963-2 · Cited by 33 · see citing works
Bispecific applications of non-immunoglobulin scaffold binders
Hober, S., Lindbo, S., & Nilvebrant, J. (2018) · Methods · doi:10.1016/j.ymeth.2018.09.010 · Cited by 32 · see citing works
PET imaging of a 68Ga labeled modified HER2 affibody in breast cancers: from xenografts to patients
Xu, Y., Wang, L., Pan, D., Yu, C., Mi, B., Huang, Q., Sheng, J., Yan, J., Wang, X., Yang, R., et al. (2019) · British Journal of Radiology · doi:10.1259/bjr.20190425 · Cited by 32 · see citing works
Liu, J., Jiang, Y., Chen, X., Chen, L., Zhang, X., Cui, D., Li, Y., Liu, Z., Zhao, Q., & Diao, A. (2022) · Chemical Engineering Journal · doi:10.1016/j.cej.2022.135208 · Cited by 31 · see citing works
Hansen, S., Zhang, Y., Hwang, S., Nabhan, A. N., Li, W., Fuhrmann, J., Kschonsak, Y. T., Zhou, L., Nile, A. H., Gao, X., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2207327119 · Cited by 30 · see citing works
“Examples include centyrins based on fibronectin type 3 domains (69), fynomers based on the SH3 domain of Fyn kinase (70), and three-helix domain affibodies (71), to name a few.”
BackgroundAntibodies as Biosensors’ Key Components: State-of-the-Art in Russia 2020–2021
Руденко, Н. В., Fursova, K. K., Shepelyakovskaya, A. O., Karatovskaya, A. P., & Brovko, F. A. (2021) · Sensors · doi:10.3390/s21227614 · Cited by 30 · see citing works
“Due to their small size, affibodies gain advantages for diagnostic imaging [35].”
BackgroundFluorescence Molecular Targeting of Colon Cancer to Visualize the Invisible
Lwin, T. M., Turner, M. A., Amirfakhri, S., Nishino, H., Hoffman, R. M., & Bouvet, M. (2022) · Cells · doi:10.3390/cells11020249 · Cited by 30 · see citing works
“Antibody mimetics have promising potential as therapeutic agents, and there is increasing interest in using these molecules as probes for FGS [58].”
BackgroundZhu, S., Chen, J., Xiong, Y., Kamara, S., Gu, M., Tang, W., Shao, C., Dong, H., Xue, X., Zheng, Z., et al. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008223 · Cited by 29 · see citing works
“molecules attractive for many medical applications, including in vivo molecular imaging, receptor signal blocking and delivery of toxin [21,22].”
BackgroundZhao, N., Ding, B., Zhang, Y., Klockow, J., Lau, K., Chin, F. T., Cheng, Z., & Liu, H. (2020) · Journal of Controlled Release · doi:10.1016/j.jconrel.2020.05.031 · Cited by 30 · see citing works
Shipunova, V. O., Komedchikova, E. N., Kotelnikova, P. A., Nikitin, M. P., & Deyev, S. M. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15030833 · Cited by 29 · see citing works
“Equally important is the ease of large-scale biotechnological production, in contrast to that of fullsize antibodies [45,56].”
BackgroundPEG Linker Improves Antitumor Efficacy and Safety of Affibody-Based Drug Conjugates
Li, Q., Li, W., Xu, K., Xing, Y., Shi, H., Jing, Z., Li, S., & Hong, Z. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041540 · Cited by 28 · see citing works
“Moreover, affibody molecules do not contain any cysteine residues; therefore, site-specific coupling with small molecule drugs can be realized by introducing an extra cysteine residue [23,31].”
BackgroundMorales, I. C., Dingfelder, F., Waibel, I., Turnbull, O. M., Patel, B., Cao, Z., Bjelke, J. R., Grell, S. N., Bennet, A., Hummer, A. M., et al. (2024) · mAbs · doi:10.1080/19420862.2024.2403156 · Cited by 27 · see citing works
“Relevant examples include VHH’s and other small de novo affinity ligands, 39,40 and many other examples involving Fc domains.”
BackgroundInhibition of Pore-Forming Proteins
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Engineering Saccharomyces cerevisiae for the production and secretion of Affibody molecules
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“Different configurations of the Z domain and the ABD domain, like the presence of multiple Z domains or an alternative localization of the ABD within the molecule, have shown to be effective in a range applications [7, 10, 11].”
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“, DARPin®, Affibody®).(29,30) In consequence, clinical and pre-clinical studies using unconventional molecules are increasing.”
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“Well-studied variants binding to several cancer-related targets exist [26].”
BackgroundApplication of a Novel 68Ga-HER2 Affibody PET/CT Imaging in Breast Cancer Patients
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“Due to its higher sensitivity and rapid penetration into target lesions (15, 16), affibody demonstrates superiority in molecular imaging compared with monoclonal antibody and antibody fragments, especially in the detection of metastases inaccessible to biopsies.”
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- Authors
- Frejd, F. Y., & Kim, K.-T.
- Affiliations
- Uppsala University (SE)
- Corresponding author
- Frejd, Fredrik Y
- ORCID
- Frejd, Fredrik Y
- Venue
- Experimental & Molecular Medicine
- Published
- 2017-03-24
- Volume
- 49
- Issue
- 3
- Pages
- e306-e306
- ISSN
- 1226-3613 (ISSN-L)
- 2092-6413
- PMC
- PMC5382565
- OpenAlex
- W2602095186
- Cited by
- 225
- References
- 96
- Citations by year
- 2026: 14 · 2025: 30 · 2024: 27 · 2023: 28 · 2022: 25 · 2021: 31 · 2020: 35 · 2019: 15 · 2018: 18 · 2017: 2
- FWCI
- 2.89
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Experimental & Molecular Medicine (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- KTH Publication Database DiVA (KTH Royal Institute of Technology) (submittedVersion, other-oa)
- Topics
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Radiopharmaceutical Chemistry and Applications
- Keywords
- Affibody molecules, molecular recognition, diagnostic applications, therapeutic applications, clinical efficacy and safety
- MeSH terms
- Animals, Antibodies, Monoclonal, Diagnostic Imaging, Humans, Protein Binding, Recombinant Fusion Proteins, Protein Engineering
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