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Journal articles on the topic 'Nanobody'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Zeng, Ying, Yiying Hu, Ganying Chen, et al. "Development of an Anti-Zearalenone Nanobody Phage Display Library and Preparation of Specific Nanobodies." Current Issues in Molecular Biology 47, no. 3 (2025): 157. https://doi.org/10.3390/cimb47030157.

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Zearalenone (ZEN), a toxic estrogenic mycotoxin in cereals, threatens human and animal health through reproductive, immune, and cytotoxic effects, necessitating sensitive detection methods. While nanobodies offer advantages over conventional antibodies for on-site ZEN detection, their application remains unexplored. This study aimed to develop an anti-ZEN nanobody derived from an anti-ZEN phage display nanobody library. An alpaca was immunized with a ZEN-bovine serum albumin (ZEN-BSA) antigen, achieving peak serum antibody titers (1:25,600) following four immunizations. A high-capacity phage d

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2

Zang, Berlin, Jun Ren, Da Li, et al. "Freezing-assisted synthesis of covalent C–C linked bivalent and bispecific nanobodies." Organic & Biomolecular Chemistry 17, no. 2 (2019): 257–63. http://dx.doi.org/10.1039/c8ob02323a.

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3

Miao, Yinglong, and J. Andrew McCammon. "Mechanism of the G-protein mimetic nanobody binding to a muscarinic G-protein-coupled receptor." Proceedings of the National Academy of Sciences 115, no. 12 (2018): 3036–41. http://dx.doi.org/10.1073/pnas.1800756115.

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Protein–protein binding is key in cellular signaling processes. Molecular dynamics (MD) simulations of protein–protein binding, however, are challenging due to limited timescales. In particular, binding of the medically important G-protein-coupled receptors (GPCRs) with intracellular signaling proteins has not been simulated with MD to date. Here, we report a successful simulation of the binding of a G-protein mimetic nanobody to the M2 muscarinic GPCR using the robust Gaussian accelerated MD (GaMD) method. Through long-timescale GaMD simulations over 4,500 ns, the nanobody was observed to bin

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4

Deszyński, Piotr, Jakub Młokosiewicz, Adam Volanakis, et al. "INDI—integrated nanobody database for immunoinformatics." Nucleic Acids Research 50, no. D1 (2021): D1273—D1281. http://dx.doi.org/10.1093/nar/gkab1021.

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Abstract Nanobodies, a subclass of antibodies found in camelids, are versatile molecular binding scaffolds composed of a single polypeptide chain. The small size of nanobodies bestows multiple therapeutic advantages (stability, tumor penetration) with the first therapeutic approval in 2018 cementing the clinical viability of this format. Structured data and sequence information of nanobodies will enable the accelerated clinical development of nanobody-based therapeutics. Though the nanobody sequence and structure data are deposited in the public domain at an accelerating pace, the heterogeneit

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5

Su, Benchao, Yidan Wang, Hua Pei, et al. "Phage-mediated double-nanobody sandwich immunoassay for detecting alpha fetal protein in human serum." Analytical Methods 12, no. 39 (2020): 4742–48. http://dx.doi.org/10.1039/d0ay01407a.

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6

Chames, Patrick, and Ulrich Rothbauer. "Special Issue: Nanobody." Antibodies 9, no. 1 (2020): 6. http://dx.doi.org/10.3390/antib9010006.

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7

Vogt, Nina. "Conditional nanobody tools." Nature Methods 13, no. 8 (2016): 610–11. http://dx.doi.org/10.1038/nmeth.3950.

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8

Zou, Tao, Fatimata Dembele, Anne Beugnet, Lucie Sengmanivong, Ario de Marco, and Min-Hui Li. "Nanobody-functionalized polymersomes." Journal of Controlled Release 213 (September 2015): e79-e80. http://dx.doi.org/10.1016/j.jconrel.2015.05.132.

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9

Li, Shufeng, Kunpeng Jiang, Ting Wang, et al. "Nanobody against PDL1." Biotechnology Letters 42, no. 5 (2020): 727–36. http://dx.doi.org/10.1007/s10529-020-02823-2.

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10

Zhang, Yunxiao, Wan-Jin Lu, David P. Bulkley, et al. "Hedgehog pathway activation through nanobody-mediated conformational blockade of the Patched sterol conduit." Proceedings of the National Academy of Sciences 117, no. 46 (2020): 28838–46. http://dx.doi.org/10.1073/pnas.2011560117.

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Activation of the Hedgehog pathway may have therapeutic value for improved bone healing, taste receptor cell regeneration, and alleviation of colitis or other conditions. Systemic pathway activation, however, may be detrimental, and agents amenable to tissue targeting for therapeutic application have been lacking. We have developed an agonist, a conformation-specific nanobody against the Hedgehog receptor Patched1 (PTCH1). This nanobody potently activates the Hedgehog pathway in vitro and in vivo by stabilizing an alternative conformation of a Patched1 “switch helix,” as revealed by our cryoge

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11

Kunz, Sarah, Manon Durandy, Laetitia Seguin, and Chloe C. Feral. "NANOBODY® Molecule, a Giga Medical Tool in Nanodimensions." International Journal of Molecular Sciences 24, no. 17 (2023): 13229. http://dx.doi.org/10.3390/ijms241713229.

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Although antibodies remain the most widely used tool for biomedical research, antibody technology is not flawless. Innovative alternatives, such as Nanobody® molecules, were developed to address the shortcomings of conventional antibodies. Nanobody® molecules are antigen-binding variable-domain fragments derived from the heavy-chain-only antibodies of camelids (VHH) and combine the advantageous properties of small molecules and monoclonal antibodies. Nanobody® molecules present a small size (~15 kDa, 4 nm long and 2.5 nm wide), high solubility, stability, specificity, and affinity, ease of clo

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12

Bitsch, Peter, Eva S. Baum, Irati Beltrán Hernández, et al. "Penetration of Nanobody-Dextran Polymer Conjugates through Tumor Spheroids." Pharmaceutics 15, no. 10 (2023): 2374. http://dx.doi.org/10.3390/pharmaceutics15102374.

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Here we report the generation of nanobody dextran polymer conjugates (dextraknobs) that are loaded with small molecules, i.e., fluorophores or photosensitizers, for potential applications in cancer diagnostics and therapy. To this end, the molecules are conjugated to the dextran polymer which is coupled to the C-terminus of an EGFR-specific nanobody using chemoenzymatic approaches. A monovalent EGFR-targeted nanobody and biparatopic version modified with different dextran average molecular weights (1000, 5000, and 10,000) were probed for their ability to penetrate tumor spheroids. For monovale

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13

Ratnikova, Nataliya M., Yulia Kravchenko, Anna Ivanova, Vladislav Zhuchkov, Elena Frolova, and Stepan Chumakov. "A Novel Anti-CD47 Nanobody Tetramer for Cancer Therapy." Antibodies 13, no. 1 (2024): 2. http://dx.doi.org/10.3390/antib13010002.

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CD47 acts as a defense mechanism for tumor cells by sending a “don’t eat me” signal via its bond with SIRPα. With CD47’s overexpression linked to poor cancer outcomes, its pathway has become a target in cancer immunotherapy. Though monoclonal antibodies offer specificity, they have limitations like the large size and production costs. Nanobodies, due to their small size and unique properties, present a promising therapeutic alternative. In our study, a high-affinity anti-CD47 nanobody was engineered from an immunized alpaca. We isolated a specific VHH from the phage library, which has nanomola

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14

Wu, Tiantian, Manman Liu, Hai Huang, Yaping Sheng, Haihua Xiao, and Yangzhong Liu. "Clustered nanobody–drug conjugates for targeted cancer therapy." Chemical Communications 56, no. 65 (2020): 9344–47. http://dx.doi.org/10.1039/d0cc03396k.

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15

Moliner-Morro, Ainhoa, Daniel J. Sheward, Vivien Karl, et al. "Picomolar SARS-CoV-2 Neutralization Using Multi-Arm PEG Nanobody Constructs." Biomolecules 10, no. 12 (2020): 1661. http://dx.doi.org/10.3390/biom10121661.

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Multivalent antibody constructs have a broad range of clinical and biotechnological applications. Nanobodies are especially useful as components for multivalent constructs as they allow increased valency while maintaining a small molecule size. We here describe a novel, rapid method for the generation of bi- and multivalent nanobody constructs with oriented assembly by Cu-free strain promoted azide-alkyne click chemistry (SPAAC). We used sortase A for ligation of click chemistry functional groups site-specifically to the C-terminus of nanobodies before creating C-to-C-terminal nanobody fusions

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16

Hendrickx, Maarten L. V., Monika Zatloukalova, Gholamreza Hassanzadeh-Ghassabeh, Serge Muyldermans, Ann Gils, and Paul J. Declerck. "In vitro and in vivo characterisation of the profibrinolytic effect of an inhibitory anti-rat TAFI nanobody." Thrombosis and Haemostasis 111, no. 05 (2014): 824–32. http://dx.doi.org/10.1160/th13-08-0645.

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SummaryOne of the main disadvantages of current t-PA thrombolytic treatment is the increased bleeding risk. Upon activation, thrombin activatable fibrinolysis inhibitor (TAFI) is a very powerful antifibrinolytic enzyme. Therefore, co-administration of a TAFI inhibitor during thrombolysis could reduce the required t-PA dose without compromising the thrombolytic efficacy. In this study we generated and characterised a nanobody that is inhibitory towards rat TAFI and evaluated its profibrinolytic property in vitro and in vivo. Nanobody VHH-rTAFI-i81 inhibits (at a 16-fold molar ratio nanobody ove

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Khatibi, Azadeh Sharif, Nasim Hayati Roodbari, Keivan Majidzade-A, Parichehreh Yaghmaei та Leila Farahmand. "In vivo tumor-suppressing and anti-angiogenic activities of a recombinant anti-CD3ε nanobody in breast cancer mice model". Immunotherapy 11, № 18 (2019): 1555–67. http://dx.doi.org/10.2217/imt-2019-0068.

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Aim: Achievements in cancer immunotherapy require augmentation of a host's anti-tumor immune response for anti-cancer modality. Materials & methods: Different concentrations of recombinant anti-CD3 nanobody were administered at predetermined time intervals during a 24-day treatment period and then expression of angiogenic biomarkers including VEGFR2, MMP9 and CD31, as well as tumor cell proliferation marker ki67, was determined in tumor sections by immunohistochemistry. Furthermore, expression of cytokines was examined in peripheral blood of mice. Results: Based on our results, administrat

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18

Verkhivker, Gennady. "Allosteric Determinants of the SARS-CoV-2 Spike Protein Binding with Nanobodies: Examining Mechanisms of Mutational Escape and Sensitivity of the Omicron Variant." International Journal of Molecular Sciences 23, no. 4 (2022): 2172. http://dx.doi.org/10.3390/ijms23042172.

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Structural and biochemical studies have recently revealed a range of rationally engineered nanobodies with efficient neutralizing capacity against the SARS-CoV-2 virus and resilience against mutational escape. In this study, we performed a comprehensive computational analysis of the SARS-CoV-2 spike trimer complexes with single nanobodies Nb6, VHH E, and complex with VHH E/VHH V nanobody combination. We combined coarse-grained and all-atom molecular simulations and collective dynamics analysis with binding free energy scanning, perturbation-response scanning, and network centrality analysis to

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19

Xu, Li, Hanyu Cao, Chundong Huang, and Lingyun Jia. "Oriented Immobilization and Quantitative Analysis Simultaneously Realized in Sandwich Immunoassay via His-Tagged Nanobody." Molecules 24, no. 10 (2019): 1890. http://dx.doi.org/10.3390/molecules24101890.

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Despite the advantages of the nanobody, the unique structure limits its use in sandwich immunoassay. In this study, a facile protocol of sandwich immunoassay using the nanobody was established. In brief, β amyloid and SH2, an anti-β amyloid nanobody, were used as capture antibody and antigen, respectively. The SH2 fused with His-tag was first purified and absorbed on Co2+-NTA functional matrix and then immobilized through H2O2 oxidation of Co2+ to Co3+ under the optimized conditions. Then, 150 mM imidazole and 20 mM EDTA were introduced to remove the unbound SH2. The immobilized SH2 showed hig

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20

Hong, Haofei, Zhifang Zhou, Kun Zhou, Shaozhong Liu, Zhongwu Guo, and Zhimeng Wu. "Site-specific C-terminal dinitrophenylation to reconstitute the antibody Fc functions for nanobodies." Chemical Science 10, no. 40 (2019): 9331–38. http://dx.doi.org/10.1039/c9sc03840j.

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A practical strategy to reconstitute the Fc functions of nanobody was developed by nanobody C-terminal dinitrophenylation. The Fc functions are successfully reinstated as proved by the potent ADCC and CDC in vitro and anti-tumor efficacies in vivo.

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21

Ye, Gang, Fan Bu, Ruangang Pan, et al. "Structure-guided in vitro evolution of nanobodies targeting new viral variants." PLOS Pathogens 20, no. 9 (2024): e1012600. http://dx.doi.org/10.1371/journal.ppat.1012600.

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A major challenge in antiviral antibody therapy is keeping up with the rapid evolution of viruses. Our research shows that nanobodies—single-domain antibodies derived from camelids—can be rapidly re-engineered to combat new viral strains through structure-guided in vitro evolution. Specifically, for viral mutations occurring at nanobody-binding sites, we introduce randomized amino acid sequences into nanobody residues near these mutations. We then select nanobody variants that effectively bind to the mutated viral target from a phage display library. As a proof of concept, we used this approac

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22

Stathopoulou, Chaido, Jessica Hong, Mitchell Ho, and Raffit Hassan. "Abstract 1786: Mesothelin-targeting, nanobody-based CAR T cells effectively target solid tumors in fully immunocompetent hosts." Cancer Research 83, no. 7_Supplement (2023): 1786. http://dx.doi.org/10.1158/1538-7445.am2023-1786.

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Abstract Nanobody-based chimeric antigen receptor (CAR) T cells are currently being tested in early phase clinical trials against blood and solid tumor antigens. Owing to the low molecular weight, increased stability, and low immunogenicity of nanobodies, nanobody-based CAR T cells are an attractive alternative to antibody-based CAR T cells for improving in vivo persistence and overcoming loss of antigen in solid tumors. However, no such agent has been described that can target mesothelin, a tumor antigen that is highly expressed in mesotheliomas, pancreatic, ovarian, and lung carcinomas. Here

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Percipalle, Mathias, Yamanappa Hunashal, Jan Steyaert, Federico Fogolari, and Gennaro Esposito. "Structure of Nanobody Nb23." Molecules 26, no. 12 (2021): 3567. http://dx.doi.org/10.3390/molecules26123567.

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Background: Nanobodies, or VHHs, are derived from heavy chain-only antibodies (hcAbs) found in camelids. They overcome some of the inherent limitations of monoclonal antibodies (mAbs) and derivatives thereof, due to their smaller molecular size and higher stability, and thus present an alternative to mAbs for therapeutic use. Two nanobodies, Nb23 and Nb24, have been shown to similarly inhibit the self-aggregation of very amyloidogenic variants of β2-microglobulin. Here, the structure of Nb23 was modeled with the Chemical-Shift (CS)-Rosetta server using chemical shift assignments from nuclear m

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24

Sinha, Gunjan. "Ablynx drops lead nanobody." Nature Biotechnology 30, no. 2 (2012): 124. http://dx.doi.org/10.1038/nbt0212-124a.

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25

Keller, Laura, Nicolas Bery, Claudine Tardy, et al. "Selection and Characterization of a Nanobody Biosensor of GTP-Bound RHO Activities." Antibodies 8, no. 1 (2019): 8. http://dx.doi.org/10.3390/antib8010008.

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RHO (Ras HOmologous) GTPases are molecular switches that activate, in their state bound to Guanosine triphosphate (GTP), key signaling pathways, which involve actin cytoskeleton dynamics. Previously, we selected the nanobody RH12, from a synthetic phage display library, which binds the GTP-bound active conformation of RHOA (Ras Homologous family member A). However, when expressed as an intracellular antibody, its blocking effect on RHO signaling led to a loss of actin fibers, which in turn affected cell shape and cell survival. Here, in order to engineer an intracellular biosensor of RHOA-GTP

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Guenter, Rachael, Yuvasri Golivi, Lucinda Hall, et al. "Abstract 574: Detection of tumor cell surface calreticulin after doxorubicin treatment using a novel radiolabeled nanobody." Cancer Research 85, no. 8_Supplement_1 (2025): 574. https://doi.org/10.1158/1538-7445.am2025-574.

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Abstract Background: Targeted agents, such as nanobodies, can be covalently linked to radionuclide chelators for theranostics. Nanobodies are single-domain immunoglobulin variable regions with a short blood half-lives and high specificity. Calreticulin (CALR) is endoplasmic reticular (ER) protein that translocates to the cell surface upon induction with certain agents, namely doxorubicin. We hypothesized surface CALR on tumors could be targeted using a novel nanobody after induction with doxorubicin. Methods: Studies were conducted using in vitro and in vivo models of pancreatic ductal adenoca

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Bao, Chaolemeng, Quanli Gao, Lin-Lin Li, et al. "The Application of Nanobody in CAR-T Therapy." Biomolecules 11, no. 2 (2021): 238. http://dx.doi.org/10.3390/biom11020238.

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Chimeric antigen receptor (CAR) T therapy represents a form of immune cellular therapy with clinical efficacy and a specific target. A typical chimeric antigen receptor (CAR) construct consists of an antigen binding domain, a transmembrane domain, and a cytoplasmic domain. Nanobodies have been widely applied as the antigen binding domain of CAR-T due to their small size, optimal stability, high affinity, and manufacturing feasibility. The nanobody-based CAR structure has shown a proven function in more than ten different tumor-specific targets. After being transduced in Jurkat cells, natural k

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Vester, Susan K., Anna M. Davies, Rebecca L. Beavil, et al. "Expanding the Anti-Phl p 7 Antibody Toolkit: An Anti-Idiotype Nanobody Inhibitor." Antibodies 12, no. 4 (2023): 75. http://dx.doi.org/10.3390/antib12040075.

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We have previously produced a toolkit of antibodies, comprising recombinant human antibodies of all but one of the human isotypes, directed against the polcalcin family antigen Phl p 7. In this work, we complete the toolkit of human antibody isotypes with the IgD version of the anti-Phl p 7 monoclonal antibody. We also raised a set of nanobodies against the IgD anti-Phl p 7 antibody and identify and characterize one paratope-specific nanobody. This nanobody also binds to the IgE isotype of this antibody, which shares the same idiotype, and orthosterically inhibits the interaction with Phl p 7.

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Liu, Bingying, and Daiwen Yang. "Validation and Optimization of PURE Ribosome Display for Screening Synthetic Nanobody Libraries." Antibodies 14, no. 2 (2025): 39. https://doi.org/10.3390/antib14020039.

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Background/Objectives: PURE (Protein synthesis Using Recombinant Elements), an ideal system for ribosome display, has been successfully used for nanobody selection. However, its limitations in nanobody selection, especially for synthetic nanobody libraries, have not been clearly elucidated, thereby restricting its utilization. Methods: The PURE ribosome display selection process was closely monitored using RNA agarose gel electrophoresis to assess the presence of mRNA molecules in each fraction, including the flow-through, washing, and elution fractions. Additionally, a real-time validation me

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Krol, Viktoria E., Aditya Bansal, Manasa Kethamreddy, et al. "Synthesis and In Vitro Evaluation of a Scandium-44 Radiolabeled Nanobody as a PD-L1 PET Imaging Probe." Pharmaceutics 17, no. 6 (2025): 796. https://doi.org/10.3390/pharmaceutics17060796.

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Background/Objective: Noninvasive PET imaging-based assessment of PD-L1 expression is of high clinical value for better patient selection and treatment response rates to PD-L1 immunotherapies. Due to their shorter biological half-life and faster clearance from the blood pool, radiolabeled antibody fragments are an attractive alternative for imaging than their full-length IgG counterpart. This work investigated the radiosynthesis and in vitro cell uptake of anti-PD-L1-B11-nanobody radiolabeled with 44Sc (t1/2 = 4.04 h) as an alternative to anti-PD-L1-B11-IgG, better suited for longer half-life

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Cheng, Xin, Jiewen Wang, Guangbo Kang, et al. "Homology Modeling-Based in Silico Affinity Maturation Improves the Affinity of a Nanobody." International Journal of Molecular Sciences 20, no. 17 (2019): 4187. http://dx.doi.org/10.3390/ijms20174187.

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Affinity maturation and rational design have a raised importance in the application of nanobody (VHH), and its unique structure guaranteed these processes quickly done in vitro. An anti-CD47 nanobody, Nb02, was screened via a synthetic phage display library with 278 nM of KD value. In this study, a new strategy based on homology modeling and Rational Mutation Hotspots Design Protocol (RMHDP) was presented for building a fast and efficient platform for nanobody affinity maturation. A three-dimensional analytical structural model of Nb02 was constructed and then docked with the antigen, the CD47

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Scholler, Nathalie, Catherine Yin, khushboo sharma, et al. "In vivo validation of a novel anti-mesothelin nanobody for early detection of mesothelin-expressing cancers." Journal of Immunology 198, no. 1_Supplement (2017): 76.20. http://dx.doi.org/10.4049/jimmunol.198.supp.76.20.

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Abstract Antibodies and antibody fragments are widely used in oncology for nanotechnology-based diagnostic, therapeutic, and prognostic assays. Recombinant antibodies that recognize mesothelin, a differentially expressed cancer biomarker with limited normal expression that is upregulated in a variety of epithelial tumors, are important for developing next generation diagnostic or therapeutic platforms and immunosensors because of the flexibility to incorporate various tags or functional groups for site-specific and oriented attachment of antibody fragments to surfaces, labeling reagents or the

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Zhao, Shuai, Wanting Zeng, Fang Yu, et al. "Visual and High-Efficiency Secretion of SARS-CoV-2 Nanobodies with Escherichia coli." Biomolecules 15, no. 1 (2025): 111. https://doi.org/10.3390/biom15010111.

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Nanobodies have gained attention as potential therapeutic and diagnostic agents for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) due to their ability to bind and neutralize the virus. However, rapid, scalable, and robust production of nanobodies for SARS-CoV-2 remains a crucial challenge. In this study, we developed a visual and high-efficiency biomanufacturing method for nanobodies with Escherichia coli by fusing the super-folder green fluorescent protein (sfGFP) to the N-terminus or C-terminus of the nanobody. Several receptor-binding domain (RBD)-specific nanobodies of the S

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Temple, William C., Matthew A. Nix, Akul Naik, et al. "Framework humanization optimizes potency of anti-CD72 nanobody CAR-T cells for B-cell malignancies." Journal for ImmunoTherapy of Cancer 11, no. 11 (2023): e006985. http://dx.doi.org/10.1136/jitc-2023-006985.

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BackgroundApproximately 50% of patients who receive anti-CD19 CAR-T cells relapse, and new immunotherapeutic targets are urgently needed. We recently described CD72 as a promising target in B-cell malignancies and developed nanobody-based CAR-T cells (nanoCARs) against it. This cellular therapy design is understudied compared with scFv-based CAR-T cells, but has recently become of significant interest given the first regulatory approval of a nanoCAR in multiple myeloma.MethodsWe humanized our previous nanobody framework regions, derived from llama, to generate a series of humanized anti-CD72 n

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Hansen, Anders H., Kasper I. H. Andersen, Li Xin, et al. "A HER2 Specific Nanobody–Drug Conjugate: Site-Selective Bioconjugation and In Vitro Evaluation in Breast Cancer Models." Molecules 30, no. 2 (2025): 391. https://doi.org/10.3390/molecules30020391.

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A human epidermal growth factor receptor 2 (HER2)-specific nanobody called 2Rs15d, containing a His3LysHis6 segment at the C-terminus, was recombinantly produced. Subsequent site-selective acylation on the C-terminally activated lysine residue allowed installation of the cytotoxin monomethyl auristatin E-functionalized cathepsin B-sensitive payload to provide a highly homogenous nanobody–drug conjugate (NBC), which demonstrated high potency and selectivity for HER2-positive breast cancer models.

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Chen, Yi, Guanggang Qu, Hongkun Quan, et al. "A Novel Cost-Effective Nanobody against Fumonisin B1 Contaminations: Efficacy Test in Dairy Milk and Chickens." Toxins 14, no. 12 (2022): 821. http://dx.doi.org/10.3390/toxins14120821.

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Background: Fumonisin B1 (FB1) is a secondary metabolite produced mainly by Fusarium verticillioides or Fusarium proliferatum. It poses a huge threat to the sustainable animal industry and human health as well via food chains (egg, meat and milk). Although E. coli-expressed nanobodies are documented for diagnostic applications, nanobodies remain elusive as FB1 detoxifiers in feed and food. Results: In the present study, the E. coli-expressed nanobody was assessed to remove FB1 in fresh milk, embryonated eggs and broilers. Firstly, 2 alpacas received intramuscularly FB1-adjuvanted BSA 6 times,

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Fernández-Quintero, Monica L., Eugene F. DeRose, Scott A. Gabel, Geoffrey A. Mueller, and Klaus R. Liedl. "Nanobody Paratope Ensembles in Solution Characterized by MD Simulations and NMR." International Journal of Molecular Sciences 23, no. 10 (2022): 5419. http://dx.doi.org/10.3390/ijms23105419.

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Variable domains of camelid antibodies (so-called nanobodies or VHH) are the smallest antibody fragments that retain complete functionality and therapeutic potential. Understanding of the nanobody-binding interface has become a pre-requisite for rational antibody design and engineering. The nanobody-binding interface consists of up to three hypervariable loops, known as the CDR loops. Here, we structurally and dynamically characterize the conformational diversity of an anti-GFP-binding nanobody by using molecular dynamics simulations in combination with experimentally derived data from nuclear

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Sohier, Jean S., Clémentine Laurent, Andy Chevigné та ін. "Allosteric inhibition of VIM metallo-β-lactamases by a camelid nanobody". Biochemical Journal 450, № 3 (2013): 477–86. http://dx.doi.org/10.1042/bj20121305.

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MβL (metallo-β-lactamase) enzymes are usually produced by multi-resistant Gram-negative bacterial strains and have spread worldwide. An approach on the basis of phage display was used to select single-domain antibody fragments (VHHs, also called nanobodies) that would inhibit the clinically relevant VIM (Verona integron-encoded MβL)-4 MβL. Out of more than 50 selected nanobodies, only the NbVIM_38 nanobody inhibited VIM-4. The paratope, inhibition mechanism and epitope of the NbVIM_38 nanobody were then characterized. An alanine scan of the NbVIM_38 paratope showed that its binding was driven

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Jakobs, Barbara D., Lisa Spannagel, Vladimir Purvanov, Edith Uetz-von Allmen, Christoph Matti, and Daniel F. Legler. "Engineering of Nanobodies Recognizing the Human Chemokine Receptor CCR7." International Journal of Molecular Sciences 20, no. 10 (2019): 2597. http://dx.doi.org/10.3390/ijms20102597.

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The chemokine receptor CCR7 plays a pivotal role in health and disease. In particular, CCR7 controls homing of antigen-bearing dendritic cells and T cells to lymph nodes, where adaptive immune responses are initiated. However, CCR7 also guides T cells to inflamed synovium and thereby contributes to rheumatoid arthritis and promotes cancer cell migration and metastasis formation. Nanobodies have recently emerged as versatile tools to study G-protein-coupled receptor functions and are being tested in diagnostics and therapeutics. In this study, we designed a strategy to engineer novel nanobodies

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Ge, Qiuhan, Tianyuan Sun, Yanlin Bian, Xiaodong Xiao, and Jianwei Zhu. "Generating a Novel Bispecific Nanobody to Enhance Antitumor Activity." Pharmaceutical Fronts 02, no. 02 (2020): e100-e108. http://dx.doi.org/10.1055/s-0040-1714138.

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AbstractTumor cells express high levels of human epidermal growth factor receptor 2 (HER2) and vascular endothelial growth factor receptor 2 (VEGFR2), which are closely related to their proliferation and survival. Cancer treatments that target a single signaling pathway may result in immune pathway escape or drug resistance. Based on the correlation between the HER2 and VEGFR2 signaling pathways, we speculated that targeting the two pathways simultaneously may produce a synergistic effect and avoid occurrence of drug resistance, resulting in improved efficacy. Anti-VEGFR2 nanobody 3VGR19–3 and

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Liu, Ze-Hui, Kai-Xia Lei, Guang-Wei Han, Hui-Ling Xu, and Fang He. "Novel Lentivirus-Based Method for Rapid Selection of Inhibitory Nanobody against PRRSV." Viruses 12, no. 2 (2020): 229. http://dx.doi.org/10.3390/v12020229.

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The emergence and re-emergence of porcine reproductive and respiratory syndrome virus (PRRSV) has resulted in huge economic losses for the swine industry. Current vaccines are of limited efficacy against endemic circulating PRRSV variants. New strategies against PRRSV infection are in urgent need. Here, a nanobody library in Marc-145 cells is constructed for antiviral nanobodies. Nanobody encoding sequences from two non-immunized llamas were cloned to generate a pseudotyped lentiviral library. Several candidates were selected from survival cells post-PRRSV inoculation and further characterized

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Devasani, Jagadeeswara Reddy, Girijasankar Guntuku, Nalini Panatula, Murali Krishna Kumar Muthyala, Mary Sulakshana Palla, and Teruna J. Siahaan. "Innovative CDR grafting and computational methods for PD-1 specific nanobody design." Frontiers in Bioinformatics 4 (January 17, 2025). https://doi.org/10.3389/fbinf.2024.1488331.

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IntroductionThe development of nanobodies targeting Programmed Cell Death Protein-1 (PD-1) offers a promising approach in cancer immunotherapy. This study aims to design and characterize a PD-1-specific nanobody using an integrated computational and experimental approach.MethodsAn in silico design strategy was employed, involving Complementarity-Determining Region (CDR) grafting to construct the nanobody sequence. The three-dimensional structure of the nanobody was predicted using AlphaFold2, and molecular docking simulations via ClusPro were conducted to evaluate binding interactions with PD-

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Swaminathan, Rishabha, and John Dingus. "Investigating AlphaFold’s handling of nanobody-antigen complex prediction." Journal of Emerging Investigators, 2025. https://doi.org/10.59720/24-111.

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AlphaFold2 revolutionized our ability to predict a protein’s structure from its sequence. However, predicting antibody structures and antibody-antigen complexes remains a challenge. To investigate this issue further, we analyzed AlphaFold’s accuracy in predicting nanobody-antigen complexes. Nanobodies are the smallest and simplest antibody derivatives capable of binding antigens. They represent the variable portions of a special type of antibody, called a heavy-chain antibody, which lacks light chains, reducing the structural complexity of their bound complexes. We first benchmarked AlphaFold’

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Alfadhli, Ayna, Timothy A. Bates, Robin Lid Barklis, CeAnn Romanaggi, Fikadu G. Tafesse, and Eric Barklis. "A nanobody interaction with SARS-COV-2 Spike allows the versatile targeting of lentivirus vectors." Journal of Virology, August 29, 2024. http://dx.doi.org/10.1128/jvi.00795-24.

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ABSTRACT While investigating methods to target gene delivery vectors to specific cell types, we examined the potential of using a nanobody against the SARS-CoV-2 Spike protein receptor-binding domain to direct lentivirus infection of Spike-expressing cells. Using four different approaches, we found that lentiviruses with surface-exposed nanobody domains selectively infect Spike-expressing cells. Targeting is dependent on the fusion function of the Spike protein, and conforms to a model in which nanobody binding to the Spike protein triggers the Spike fusion machinery. The nanobody–Spike intera

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"Nanobody tools." Nature Methods 13, no. 2 (2016): 116. http://dx.doi.org/10.1038/nmeth.3748.

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Foley, John F. "Nanobody pharmacology." Science Signaling 17, no. 837 (2024). http://dx.doi.org/10.1126/scisignal.adq4734.

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Hao, Shuai, Shuyi Xu, Liangzhu Li, et al. "Tumour inhibitory activity on pancreatic cancer by bispecific nanobody targeting PD-L1 and CXCR4." BMC Cancer 22, no. 1 (2022). http://dx.doi.org/10.1186/s12885-022-10165-7.

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Abstract Background: Antibodies and derivative drugs targeting immune checkpoints have been approved for the treatment of several malignancies, but there are fewer responses in patients with pancreatic cancer. Here, we designed a nanobody molecule with bi-targeting on PD-L1 and CXCR4, as both targets are overexpressed in many cancer cells and play important roles in tumorigenesis. We characterized the biochemical and anti-tumour activities of the bispecific nanobodies in vitro and in vivo. Methods: A nanobody molecule was designed and constructed. The nanobody sequences targeting PD-L1 and CXC

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Padhi, Aditya K., Ashutosh Kumar, Ken-ichi Haruna, et al. "An integrated computational pipeline for designing high-affinity nanobodies with expanded genetic codes." Briefings in Bioinformatics, August 20, 2021. http://dx.doi.org/10.1093/bib/bbab338.

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Abstract Protein engineering and design principles employing the 20 standard amino acids have been extensively used to achieve stable protein scaffolds and deliver their specific activities. Although this confers some advantages, it often restricts the sequence, chemical space, and ultimately the functional diversity of proteins. Moreover, although site-specific incorporation of non-natural amino acids (nnAAs) has been proven to be a valuable strategy in protein engineering and therapeutics development, its utility in the affinity-maturation of nanobodies is not fully explored. Besides, curren

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Kunz, Patrick, Aurelio Ortale, Norbert Mücke, Katinka Zinner та Jörg D. Hoheisel. "Nanobody stability engineering by employing the ΔTm shift; a comparison with apparent rate constants of heat-induced aggregation". Protein Engineering, Design and Selection, 24 липня 2019. http://dx.doi.org/10.1093/protein/gzz017.

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Abstract The antigen-binding domains of camelid heavy-chain antibodies, also called nanobodies, gained strong attention because of their unique functional and biophysical properties. They gave rise to an entire spectrum of applications in biotechnology, research and medicine. Despite several reports about reversibly refolding nanobodies, protein aggregation plays a major role in nanobody thermoresistance, asking for strategies to engineer their refolding behavior. Here, we use measurements of nanobody aggregation kinetics to validate structural features in the nanobody fold that are suppressin

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De Groeve, Manu, Bram Laukens, and Peter Schotte. "Optimizing expression of Nanobody® molecules in Pichia pastoris through co-expression of auxiliary proteins under methanol and methanol-free conditions." Microbial Cell Factories 22, no. 1 (2023). http://dx.doi.org/10.1186/s12934-023-02132-z.

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Abstract Background Ablynx NV, a subsidiary of Sanofi, has a long-standing focus on the development of Nanobody® molecules as biopharmaceuticals (Nanobody® is a registered trademark of Ablynx NV). Nanobody molecules are single variable domains, and they have been met with great success part due to their favorable expression properties in several microbial systems. Nevertheless, the search for the host of the future is an ongoing and challenging process. Komagataella phaffi (Pichia pastoris) is one of the most suitable organisms to produce Nanobody molecules. In addition, genetic engineering of

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