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Letteratura scientifica selezionata sul tema "Antibody affinity"

Autore: Grafiati

Pubblicato: 4 giugno 2021

Ultima modifica: 14 febbraio 2022

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Articoli di riviste sul tema "Antibody affinity"

1

Azimzadeh, A., and M. H. V. Van Regenmortel. "Antibody affinity measurements." Journal of Molecular Recognition 3, no. 3 (June 1990): 108–16. http://dx.doi.org/10.1002/jmr.300030304.

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van Regenmortel, Marc H. V., and Agnëgs Azimzadeh. "Determination of Antibody Affinity." Journal of Immunoassay 21, no. 2-3 (May 2000): 211–34. http://dx.doi.org/10.1080/01971520009349534.

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Wabl, Matthias, Marilia Cascalho, and Charles Steinberg. "Hypermutation in antibody affinity maturation." Current Opinion in Immunology 11, no. 2 (April 1999): 186–89. http://dx.doi.org/10.1016/s0952-7915(99)80031-4.

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4

Webster, D. M., S. Roberts, J. C. Cheetham, R. Griest, and A. R. Rees. "Engineering antibody affinity and specificity." International Journal of Cancer 41, S3 (1988): 13–16. http://dx.doi.org/10.1002/ijc.2910410804.

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5

Nervig, Christine S., and Shawn C. Owen. "Affinity-bound antibody–drug conjugates." Nature Biomedical Engineering 3, no. 11 (November 2019): 850–51. http://dx.doi.org/10.1038/s41551-019-0478-0.

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Griswold, William R. "A Quantitative Relationship Between Antibody Affinity and Antibody Avidity." Immunological Investigations 16, no. 2 (January 1987): 97–106. http://dx.doi.org/10.3109/08820138709030567.

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Yu, Guimei, Kunpeng Li, and Wen Jiang. "Antibody-based affinity cryo-EM grid." Methods 100 (May 2016): 16–24. http://dx.doi.org/10.1016/j.ymeth.2016.01.010.

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8

Steward, Michael W., Carolynne Stanley, and Maria D. Furlong. "Antibody affinity maturation in selectively bred high and low-affinity mice." European Journal of Immunology 16, no. 1 (1986): 59–63. http://dx.doi.org/10.1002/eji.1830160112.

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Makabe, Koki. "Molecular basis of flexible peptide recognition by an antibody." Journal of Biochemistry 167, no. 4 (February 6, 2020): 343–45. http://dx.doi.org/10.1093/jb/mvaa017.

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Abstract Antibodies can recognize various types of antigens with high specificity and affinity and peptide is one of their major targets. Understanding an antibody’s molecular recognition mechanism for peptide is important for developing clones with a higher specificity and affinity. Here, the author reviews recent progresses in flexible peptide recognition by an antibody using several biophysical techniques, including X-ray crystallography, molecular dynamics simulations and calorimetric measurements. A set of two reports highlight the importance of intramolecular hydrogen bonds that form in an unbound flexible state. Such intramolecular hydrogen bonds restrict the fluctuation of the peptide and reduce the conformational entropy, resulting in the destabilization of the unbound state and increasing the binding affinity by increasing the free energy change. These detailed analyses will aid in the antibody design in the future.

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Fukunishi, Hiroaki, Jiro Shimada, and Kenji Shiraishi. "Antigen–Antibody Interactions and Structural Flexibility of a Femtomolar-Affinity Antibody." Biochemistry 51, no. 12 (March 13, 2012): 2597–605. http://dx.doi.org/10.1021/bi3000319.

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Tesi sul tema "Antibody affinity"

1

Low, Nigel Murray. "Mimicking antibody affinity maturation." Thesis, University of Cambridge, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.364567.

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Molari, Marco. "Modeling and Bayesian inference for antibody affinity maturation." Thesis, Université Paris sciences et lettres, 2020. http://www.theses.fr/2020UPSLE017.

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La Maturation d’Affinité (MA) est le processus biologique grâce auquel notre système immunitaire génère de puissants anticorps contre les nouveaux agents pathogènes rencontrés. Ce processus est également à la base de la vaccination, l’une des procédures médicales les plus efficaces jamais mises au point, qui permet de sauver des millions de vies chaque année. La MA présentent encore de nombreuses questions ouvertes, dont les réponses peuvent améliorer la manière dont nous vaccinons. Les mécanismes à la base de la MA sont extrêmement complexes, avec des interactions non linéaires entre nombreux cellules différentes. Dans ce contexte, les modèles théoriques et l’inférence Bayésienne sont des outils précieux pour relier les hypothèses qualitatives aux descriptions quantitatives et extraire informations des données expérimentales. Dans ce manuscrit, nous utilisons ces outils pour aborder certaines questions ouvertes, comme l’effet du dosage de l’antigène sur la qualité de la vaccination<br>Affinity Maturation (AM) is the biological process through which our Immune System generates potent Antibodies (Abs) against newly encountered pathogens. This process is also at the base of vaccination, one of the most successful and cost-effective medical procedures ever developed, responsible for saving millions of lives every year. AM still present many open questions, whose answers have the potential of improving the way we vaccinate. The mechanisms at the base of AM are extremely complex, involving non-linear interactions between many different cellular agents. In this context theoretical models and Bayesian Inference are invaluable tools, respectively to link qualitative hypothesis to quantitative descriptions and to extract information from experimental data. In this manuscript we make use of these tools to tackle some of the open questions, such as the non-trivial effect of Ag dosage on the outcome of vaccination

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Lang, Birthe Agnetha. "Nanofibrous affinity membranes containing non-antibody binding proteins." Thesis, University of Leeds, 2016. http://etheses.whiterose.ac.uk/15326/.

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The specific removal of molecules from various media is an area receiving increasing attention. Affnity membranes, i.e. membranes containing ligands, which can specifically capture target molecules, can meet this demand. One important area, in which the use of affinity membranes will be beneficial, is blood filtration, specifically haemodialysis treatments. The specific removal of toxins can reduce treatment time and/or frequency and therefore increase patients' quality of life as well as reduce costs for the health care sector. The presented research investigates the feasibility of combining a new class of nonantibody binding proteins (AdhironTM binders), which can be specifically designed to capture target molecules, with electrospun nanofibrous polysulphone (PSu) membranes to create an affinity membrane for the specific removal of target molecules. Adhiron binders against a model target protein (modified green fluorescent protein (mGFP)) were successfully produced and characterised. Suitable parameters for the electrospinning of PSu into smooth bead-free fibres were identified. Two different approaches for the functionalisation of PSu fibres were evaluated: incorporation of the Adhiron binders within the fibre and attachment of the binders to the functionalised PSu fibre surfaces. With the latter approach functionalisation was achieved by means of attaching Adhiron binders to surface functionalised fibres, on which the Adhiron binders were immobilised via a biotin-streptavidin bridge. The functionalised membrane specifically removed target molecules out of simple and complex solutions.

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Attiya, Said. "Antibody labeling methods for automated affinity electrophoresis on microchips." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0010/NQ59926.pdf.

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Hey, Carolyn McKenzie. "Antibody Purification from Tobacco by Protein A Affinity Chromatography." Thesis, Virginia Tech, 2010. http://hdl.handle.net/10919/42645.

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Antibodies represent the largest group of biopharmaceuticals. Due to the nature of their clinical applications, they often need to be produced in large quantities. Plants have distinct advantages of producing large quantities of recombinant proteins, and tobacco is arguably the most promising plant for plant-made-pharmaceuticals (PMP) due to its high biomass yields and robust transformation technology. However, to produce proteins using transgenic tobacco for human applications, purification of the proteins is challenging. On the other hand, Protein A, a bacterial cell wall protein isolated from Staphylococcus aureus that binds to the Fc regions of immunoglobulins, is useful to the isolation and purification of antibodies. An affinity chromatography purification step utilizing Protein A resin introduced early in the purification process can reduce successive unit operations, thereby reducing the overall process cost. However, directly applying tobacco extract to Protein A chromatography columns may be problematic due to the non-specific binding of native tobacco proteins (NTP). In this project, three different Protein A resins, ProSepvA High Capacity, ProSep-vA Ultra, and ProSep Ultra Plus, marketed by Millipore, were studied to provide valuable information for future downstream processes for antibody purification from transgenic tobacco. The efficiency of the post load wash buffer to reduce non-specific binding of NTP to the ProSep A resins were evaluated by altering the ionic strength and pH. Lower salt concentrations of sodium chloride (NaCl) in the post load wash preformed best at reducing the non-specific binding of NTP to the ProSep A resins, while higher salt concentrations were more effective at reducing the amount of NTP contaminants present during elution of the columns. Using a post load wash buffer with an intermediate pH between the binding buffer and the elution buffer was more efficient at eluting our model antibody, human IgG. However, lowering the ionic strength and the pH of the post load wash buffer resulted in a greater presence of IgG prematurely eluting from the ProSep A resins. The non-specific binding of NTP to the resins reduced the dynamic binding capacity (DBC) of the resins after repeated cycles of tobacco extract samples were loaded onto the column. Nevertheless, cleaning the columns with denaturing solutions, such as urea or guanidine hydrochloride, every 8-10 cycles was effective in regenerating the DBC of the resins and prolonging the life cycle of the resins. This is important to evaluating the economic feasibility of directly using Protein A chromatography to recover antibodies from tobacco extract. Of the three Protein A resins studied, ProSep Ultra Plus performed best for antibody purification from tobacco using a PBS wash buffer with a lower ionic strength of 140mM NaCl and an intermediate pH of 5.<br>Master of Science

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Sundberg, Mårten. "Protein microarrays for validation of affinity binders." Licentiate thesis, KTH, Proteomik, 2011. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-48256.

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Is specificity an important issue regarding affinity reagents? What about the validation of affinity reagents today, is it good enough? This depends on the application and the producer of the reagent. Validation should be the most important marketing argument that can be found.Today there is a continuous growth of both the number of affinity reagents that are produced and the different types of affinity reagents that are developed. In proteomics they become more and more important in exploring the human proteome. Therefore, validated affinity reagents should be on top of every proteomic researcher’s list. How should this be accomplished?Better international agreements on how affinity reagents should be tested to be regarded as functional reagents are needed. One of the most important issues is the specificity of the affinity reagent. An international standard for which specific validation that is needed for different kinds of applications would be very useful.In this thesis, it is shown that the protein microarray platform that was established within the HPA project at KTH is a very good tool to determine the specificity of different affinity binders.In the first study, the production of mono-specific antibodies for tissue profiling in the Human Protein Atlas (HPA) project is presented. The section describing the use of protein microarrays for validation of the antibodies is relevant for this thesis. The implementation of protein microarrays in the HPA workflow was an important addition, because a deeper insight of the specificity of all the antibodies produced were now available.In a second study, bead based arrays were compared to planar protein microarrays used in the HPA project. In this study, 100 different bead identities were coupled with 100 different antigens and mixed together to generate an array. The correlation between the two types of assays was very high and the conclusion was that the methods can be used as backup to each other.A third study was a part of an international initiative to produce renewable affinity binders against proteins containing SH2 domain. Here, the HPA protein microarrays were modified to analyze different types of reagents produced at six laboratories around the world. Monoclonal antibodies, single chain fragment and fibronectin scaffolds were tested as well as mono-specific antibodies. It was shown to be possible to adapt protein microarrays used in the HPA project to validate other kinds of affinity reagents.<br>QC 20111117<br>Development and applications of protein microarrays<br>The Swedish Human Proteome Resource (HPR) program

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Qundos, Ulrika. "Antibody based plasma protein profiling." Doctoral thesis, KTH, Proteomik och nanobioteknologi, 2013. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-126270.

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This thesis is about protein profiling in serum and plasma using antibody suspension bead arrays for the analysis of biobanked samples and in the context of prostate cancer biomarker discovery. The influence of sample preparation methods on antibody based protein profiles were investigated (Papers I-III) and a prostate cancer candidate biomarker identified and verified (Papers III-V). Furthermore, a perspective on the research area affinity proteomics and its’ employment in biomarker discovery, for improved understanding and potentially improved disease diagnosis, is provided. Paper I presents the results of a comparative plasma and serum protein profiling study, with a targeted biomarker discovery approach in the context of metabolic syndrome. The study yielded a higher number of significant findings and a low experimental variability in blood samples prepared as plasma. Paper II investigated the effects from post-centrifugation delays at different temperatures prior sample storage of serum and plasma samples. Minor effects were found on the detected levels of more than 300 predicted or known plasma proteins. In Paper III, the detectability of proteins in plasma was explored by exposing samples to different pre-analytical heat treatments, prior target capture. Heat induced epitope retrieval was observed for approximately half of the targeted proteins, and resulted in the discovery of different candidate markers for prostate cancer. Several antibodies towards the prostate cancer candidate biomarker CNDP1 were generated, epitope mapped and evaluated in a bead based sandwich immunoassay, as presented in Papers IV and V. Furthermore, the developed sandwich immunoassay targeting multiple distinct CNDP1 epitopes in more than 1000 samples, confirmed the association of CNDP1 levels to aggres- sive prostate cancer and more specifically to prostate cancer patients with regional lymph node metastasis (Paper V). As an outcome of the present investigations and in parallel to studies within the Biobank profiling research group, valuable lessons from study design and multiplex antibody analysis of plasma within biomarker discovery to experimental, technical and biological verifications have been collected.<br><p>QC 20130821</p>

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Ye, Jianmin. "The relationship between antibody redox structure and affinity in rainbow trout." W&M ScholarWorks, 2008. https://scholarworks.wm.edu/etd/1539616918.

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Teleost immunoglobulin M (IgM), an 800 kDa tetramer, possesses considerable structural diversity due to the non-uniform disulfide polymerization of its halfmeric or monomeric subunits. However, to date, no plausible functional role for this diversity has been demonstrated or proposed. This research was, therefore, designed to investigate the possible functional role(s) for this diversity using the trout model. The possible relationship between this structural diversity and affinity was specifically addressed. The relationship between high levels of disulfide polymerization and high affinity was demonstrated by selective immunoadsorption and analysis of antibodies isolated during the process of affinity maturation. A pivotal determinative role of antigen/BCR affinity in conferring graded levels of disulfide bonding was demonstrated by the induction of high and mixed affinity antibodies from a single lymphocyte source in vitro. Additionally, transfer of immunopurified antibodies and labeled non-immune immunoglobulins revealed a direct effect of polymerization on antibody half-life, with selective removal of less polymerized Igs and/or retention of more fully polymerized Igs. Thus, this differential effect on half-life also results in an increase of average affinity, accentuating the process of affinity maturation. The converse, modulation of affinity by disulfide variation; however, could not be demonstrated.

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Midelfort, Katarina Senn. "Biophysical characterization of high affinity engineered single chain Fv antibody fragments." Thesis, Massachusetts Institute of Technology, 2004. http://hdl.handle.net/1721.1/30051.

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Thesis (Ph. D. in Molecular Systems Toxicology and Pharmacology)--Massachusetts Institute of Technology, Biological Engineering Division, 2004.<br>Vita.<br>Includes bibliographical references.<br>High affinity antibody binding interactions are important for both pharmaceutical and biotechnological uses. However, designing higher affinity interactions has remained difficult. Both high affinity interactions from nature and the results from directed evolution affinity maturation processes may yield clues about the important structural and energetic contributions to attain these tight associations. In this Thesis, we investigate affinity maturation of antibodies for very high affinity binding. Two single chain antigen-binding fragment (scFv) antibody systems that were engineered to obtain higher affinity interactions through directed evolution were probed using biophysical techniques to illuminate affinity modulation in proteins. First, anti-c-erbB-2 antibodies and their binding partner, the extracellular domain of the glycoprotein tumor antigen c-erbB-2, were examined. Thermodynamic studies were carried out on the originally identified human scFv and three higher affinity mutants. Although the first two steps included either entropic or enthalpic gains to affinity, the third improvement came from both types. This study demonstrates that a single energetic component is not generally responsible for the increased affinity within a given protein-protein affinity maturation pathway. Second, a family of anti-fluorescein antibodies and their binding to the small molecule fluorescein-biotin were explored. The femtomolar affinity matured anti-fluorescein antibody, 4M5.3, was compared to its wildtype high affinity precursor, 4-4-20. Affinity, thermodynamic, kinetic, and structural characterization of the binding identified 4M5.3 as one of the highest engineered affinity protein binding interactions known and<br>(cont.) illuminated how subtle structural changes can lead to large consequences for the kinetics and free energy of binding. The affinity mechanisms were further studied by the creation of a series of partial mutants. Context dependent and independent mutational effects on binding affinity indicated the extent of complexity in higher affinity mechanisms attained through directed evolution affinity maturation processes. These studies emphasize the importance of a large number of residues working in concert to create a very high affinity binding molecule. Based on these results, both rational design and directed evolution studies will need to allow for mutations in a spatially broad range around the binding site and involve many biophysical contributions to the binding free energy to reach very high antigen binding affinities.<br>by Katarina S. Midelfort.<br>Ph.D.in Molecular Systems Toxicology and Pharmacology

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Fernandes, Telma Godinho Barroso Maciel. "Functional monolithic platforms for antibody purification." Doctoral thesis, Faculdade de Ciências e Tecnologia, 2014. http://hdl.handle.net/10362/11550.

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Dissertação para obtenção do Grau de Doutor em Química Sustentável<br>Fundação para a Ciência e Tecnologia - contracts PEst-C/EQB/LA0006/2011, MIT-Pt/BS-CTRM/0051/2008, PTDC/EBB-BIO/102163/2008, PTDC/EBBBIO/ 098961/2008, PTDC/EBB-BIO/118317/2010 and doctoral grant SFRH/ BD/62475/2009, and Fundação Calouste Gulbenkian

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Più fonti

Libri sul tema "Antibody affinity"

1

1933-, Voss Edward W., ed. Anti-DNA antibodies in SLE. Boca Raton, Fla: CRC Press, 1988.

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Capitoli di libri sul tema "Antibody affinity"

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Frenzel, André, Lorin Roskos, Scott Klakamp, Meina Liang, Rosalin Arends, and Larry Green. "Antibody Affinity." In Handbook of Therapeutic Antibodies, 115–40. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2014. http://dx.doi.org/10.1002/9783527682423.ch6.

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Martineau, Pierre. "Affinity Measurements by Competition ELISA." In Antibody Engineering, 657–65. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-01144-3_41.

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Boschert, Verena, and Peter Scheurich. "Affinity Measurements with Radiolabeled Antibodies." In Antibody Engineering, 695–704. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-01144-3_44.

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Kuroda, Daisuke, and Kouhei Tsumoto. "Antibody Affinity Maturation by Computational Design." In Antibody Engineering, 15–34. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8648-4_2.

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Barderas, Rodrigo, Johan Desmet, Philippe Alard, and J. Ignacio Casal. "Affinity Maturation by Semi-rational Approaches." In Antibody Engineering, 463–86. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-974-7_27.

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Johansson, Thomas. "Affinity Measurements Using Quartz Crystal Microbalance (QCM)." In Antibody Engineering, 683–93. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-01144-3_43.

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Takkinen, Kristiina, Ari Hemminki, and Hans Söderlund. "Affinity and Specificity Maturation by CDR Walking." In Antibody Engineering, 540–45. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-662-04605-0_38.

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Thie, Holger. "Affinity Maturation by Random Mutagenesis and Phage Display." In Antibody Engineering, 397–409. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-01144-3_26.

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Bumke, Maja A., and Dario Neri. "Affinity Measurements by Band Shift and Competition ELISA." In Antibody Engineering, 385–96. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-662-04605-0_28.

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Even-Desrumeaux, Klervi, and Patrick Chames. "Affinity Determination of Biotinylated Antibodies by Flow Cytometry." In Antibody Engineering, 443–49. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-974-7_25.

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Atti di convegni sul tema "Antibody affinity"

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Berkner, J. A., G. Mitra, and J. W. Bloom. "MONOCLONAL ANTIBODY BINDING TO FACTOR VIII:C." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644063.

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The interactions of monoclonal antibodies with highly purified Factor VIII:c have been studied utilizing the ELISA technique. ELISA plates were coated with Factor VIII:c, protein A purified monoclonal IgG was then added and bound antibody detected with peroxidase labeled antimouse IgG. A Scatchard-Sips plot approach to data analysis was used to calculate binding constants. The binding constants for four antibodies designated BD10, AD7, C7F7 and 39MH8 were as follows: BD10, KO = 7.1 x 108 M-1, n = 1.1 (moles antibody/moles ligand); AD7, KO = 3.1 x 108 M-1, n = 2.7; C7F7, KO = 3.6 x 1011M-1, n = 0.03; 39MH8, K = 6.0 x 1011 M-1, n = 0.03. The binding constants for C7F7 to the purified carboxy-terminal (residues 1649-2332) 80 kD functional region of the Factor VIII:c molecule were also determined: KO = 1.0 x 1011 M-1, n = 0.55. On the basis of these results the following conclusions can be drawn: 1) the antibodies can be divided into two groups: high affinity (suitable for use in immunopurification), C7F7 and 39MH8; low affinity: BD10 and AD7; 2) the antibodies in the low affinity group have valance values two orders of magnitude higher than the high affinity antibodies, C7F7 and 39MH8. The difference might be explained by the high affinity antibody epitopes on the immobilized Factor VIII:c being less exposed to the solution; 3) C7F7 binding to the 80 kD polypeptide, compared to the whole Factor VIII:c molecule, gave virtually identical Kc values, but dramatically different valance values. This suggests that the C7F7 epitope is more accessible on the 80 kD polypeptide.

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Ryu, Tomiko, Akiko Nakayama, Atsushi Oguchi, Tadatoshi Kinoshita, Mutsuyoshi Kazama, and Takeshi Abe. "MONOCLONAL ANTIBODY WITH PREFERENTIAL AFFINITY FOR LARGE MULTIMERS OF VON WILLEBRAND FACTOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644081.

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von Willebrand factor (vWF) consists of a series of multimers of 270,000 mol. wt. subunits. Ristocetin cofactor activity (vWF:RCo) and capacity of binding to platelets of vWF are associated with large multimers, and Type IIA von Willebrand's disease (vWD) is characterized by lack of the large multimers. The significance of multimeric structure in relation to vWF function remains unclear. We obtained a monoclonal antibody (MAb) to human vWF which inhibited ristocetin-induced platelet aggregation. This antibody proved to bind preferentially to larger multimers by the finding that the MAb-conjugated Sepharose adsorbed large multimers of vWF from cryoprecipitates, leaving small multimers unadsorbed. vWF:Ag levels of noraml subjects determined by ELISA using the MAb correlated well with those by ELISA using polyclonal antibody (PAb) to vWF. When the plasma from patients with Type IIA vWD and platelet type vWD were examined, the values obtained by the MAb ELISA had a good correlation with vWF:RCo, but were lower than the values obtained by the PAb ELISA. In gel filtration of factor VIII concentrate, vWF:Ag detected by the MAb and vWF:RCo were present in the void volume and large size fractions, whereas vWF:Ag detectable with PAb appeared broadly from the void volume to smaller size fractions. The MAb inhibited ristocetin-dependent binding of vWF to platelets, but did not affect ADP-induced binding of vWF to platelets. These findings suggest that the large multimers have a function-associated specific structure which is absent in the small multimers, and the MAb will be useful for the investigation of multimer-function relationship of vWF.

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Zhou, Zhenhao. "Abstract 340: Development of high affinity anti-CLDN18.2 antibody to treat gastric cancers." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-340.

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Haber, Edgar, Marchall T. Runge, Christoph Bode, Betsy Branscomb, and Janet Schnee. "ANTIBODY TARGETED FIBRINOLYSIS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643723.

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Chemical conjugates of fibrin-specificantibodies and plasminogen activators. Urokinase or tPA were linked covalently toamonoclonal antibody specific for the amino terminus of the beta chain of human fibrin (59D8) by means of the unidirectionalcross-linking reagent SPDP. The fibrinolytic potency of the conjugates at equal amidolytic activities was compared to the native plasminogen activators in an assay measuring lysis of 1251-fibrin monomer covalently linked to Sepharose CL-4B. Urokinase was least potent, tPA exhibited a 10fold increase in fibrinolysis whereas both the urokinase and tPA antibody conjugates and a urokinase-Fab conjugate were 250fold more potent than urokinase and 25 fold more potent than tPA. Enhanced fibrinolysis was fully inhibited by b peptide indicating its dependence on antigen binding. In a plasma assay conjugates of tPA orUK to antibody produced a 3.2- to 4.5-fold enhancement in clot lysis in human plasma over that of the respective unconjugated plasminogen activator. However, the UK-59D8 conjugate was only as potent as tPAalone. Antibody-conjugated tPA or UK consumed less fibrinogen, alpha 2-antiplasminand plasminogen than did the unconjugatedactivators, at equipotent thrombolytic concentrations. In a quantitative rabbit thrombolysis model, the activity of the purified conjugate was compared with that oftPA alone and that of a conjugate betweentPA and a digoxin-specific monoclonal antibody. After correction for spontaneous lysis, tPA-59D8 was shown to be 2.8 to,9.6times more potent than tPA alone. Unconjugated tPA and tPA-digoxin were equipotent.At equivalent thrombolytic concentrations, tPA-59D8 degraded less fibrinogen and consumed less alpha 2-antiplasmin than did tPA alone. These results suggest that tPA can be efficiently directed to the site of a thrombus by conjugation to an antifibrin monoclonal antibody, resulting in both more potent and more selective thrombolysis.A recombinant fusion protein comprising a fibrin-specific antibody site and theB chain of tPA. The rearranged 59D8 heavychain gene was cloned and combined in theexpression vector pSV2gpt withsequence coding for a portion of the Gamma 2b constant region and the catalytic beta chain of t-PA. This construct was transfected into heavy chain loss variant cells derived from the 59D8 hybridoma. Recombinant protein was purified by affinitychromatography and analyzed with Western blots. These revealed a 65-kD heavy chain-t-PA fusion protein that is secreted in association with the 59D8 light chain in the form of a 170-kD disulfide linked dimer. A chromogenic substrate assay showed the fusion protein to have 70 percent of the peptidolytic activity of native t-PA and to activate plasminogen as efficiently as t-PA. In a competitive binding assay, reconstituted antibody was shown to have a binding profile similar to that of native 59D8. Thus by recombinant techniques we have produced a novel hybrid protein capable of high affinity fibrin binding andplasminogen activation.Chemical conjugates between a fibrin-specific and a tPA-specific antibody. A heteroantibody duplex (duplex) with specificities for both tPA and fibrin was synthesized by conjugating iminothiolane-modified anti-tPA monoclonal antibody (TCL8) toantifibrin antibody 59D8. Addition of both duplex and tPA to a plasma clot assay gave more lysis (200 units produced 23.1 lysis; 400 units, 29.5 lysis) than did tPAalone (200 units, 1.8% lysis; 400 units,19% lysis). Despite increased potency associated with duplex addition, fibrinogen and alpha-2-antiplasmin levels at equal tPA concentrations did not differ. Thus, itis possible to concentrate tPA (added separately) to the site of a thrombus in plasma using a heteroantibody duplex with specificities for both tPA and fibrin.Biosynthetically produced heteroduplexantibodies that are both fibin and tPA-specific. The bispecific antibodies were prepared in two ways. First, polyethylene glycol-mediated fusions were performed with two different hybridoma cell lines: anti-fribrin b chain producer, 59D8 and anti-tPA producer, TCL8. TCL8 cells were selected for HPRT-minus variants and then fused with TK-deficient 59D8 cells. One cell line, F36.23, possessed both anti-human fibrin and anti-human t-PA immunoreactivities. A second method yielded another bispecific antibody, F32.1. This cell line was selected after fusing TCL8 (HPRT-minus) cells with spleen cells from a mouseimmunized with a fibrin-like peptide corresponding to the amino terminus of fibrinalpha-chains. Affinity-purified F32.1 andF36.23 retained anti-fibrin and anti-t-PAactivity and enhanced fibrinolytic potency of tPA by a factor of 10.

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Pontes, Larissa, Marcus Bezerra, Marcela Fonseca, Marcos Lourenzoni, and Gilvan Furtado. "Construction, by rational design, and initial characterization of affinity mutants of Rituximab fragment antibody." In IV International Symposium on Immunobiologicals & VII Seminário Anual Científico e Tecnológico. Instituto de Tecnologia em Imunobiológicos, 2019. http://dx.doi.org/10.35259/isi.sact.2019_32703.

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Ishihara, Jun, Ako Ishihara, Aslan Mansurov, Koichi Sasaki, Steve S. Lee, John-Michael Williford, Lambert Potin, et al. "Abstract 1553: Collagen affinity improves safety and efficacy of antibody and cytokine cancer immunotherapies." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-1553.

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Eun, So-Young, Mijung Lee, Hye-Young Park, Miyoung Oh, Hye In Yum, Aerin Yoon, Eunhee Lee, et al. "Abstract LB-113: Enhanced anti-tumor efficacy of CEACAM1-targeting antibody after affinity maturation." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-lb-113.

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Ishihara, Jun, Ako Ishihara, Aslan Mansurov, Koichi Sasaki, Steve S. Lee, John-Michael Williford, Lambert Potin, et al. "Abstract 1553: Collagen affinity improves safety and efficacy of antibody and cytokine cancer immunotherapies." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-1553.

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Doran, Ben, Christy Ritchie, Babu Dhokia, Paul Rogers, and David Jones. "Abstract B128: Affinity optimization of an anti‐MUC1 antibody, (HuHMFG1) also enhances ADCC activity." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 15-19, 2009; Boston, MA. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/1535-7163.targ-09-b128.

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YOUNG, D., M. W. GRIFFITHS, and L. BROVKO. "USE OF BIOLUMINESCENCE FOR THE EVALUATION OF AFFINITY CONSTANTS FOR BACTERIAL CELL-ANTIBODY INTERACTIONS." In Bioluminescence and Chemiluminescence - Progress and Current Applications - 12th International Symposium on Bioluminescence (BL) and Chemiluminescence (CL). WORLD SCIENTIFIC, 2002. http://dx.doi.org/10.1142/9789812776624_0098.

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