Biotechnological applications of recombinant single-domain antibody fragments

Marco, Ario de

doi:10.1186/1475-2859-10-44

Cited by 147 publications

(100 citation statements)

References 191 publications

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“…While mAbs are effective therapeutic agents when the antigenic target is well-defined and accessible, such as in some cancers and autoimmune diseases, many diseases offer less accessible (e.g., intracellular), cryptic, or hypoallergenic targets [40,62]. In such circumstances, antibody fragments may provide advantages due to their smaller size and structure, and the ease with which they can be produced and genetically modified [11,21,27,47,[63][64][65][66]. Ab-fragment-related biomedical applications include tumor treatment and imaging [67], viral replication suppression [68][69][70], toxin and venom neutralization [41,71], and receptor blockage [36,72].…”

Section: Mabs and Their Fragments As Therapeutic Agentsmentioning

confidence: 99%

Antibody Fragments and Their Purification by Protein L Affinity Chromatography

Rodrigo¹,

Gruvegard²,

Alstine

2015

Antibodies

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Antibodies and related proteins comprise one of the largest and fastest-growing classes of protein pharmaceuticals. A majority of such molecules are monoclonal antibodies; however, many new entities are antibody fragments. Due to their structural, physiological, and pharmacological properties, antibody fragments offer new biopharmaceutical opportunities. In the case of recombinant full-length antibodies with suitable Fc regions, two or three column purification processes centered around Protein A affinity chromatography have proven to be fast, efficient, robust, cost-effective, and scalable. Most antibody fragments lack Fc and suitable affinity for Protein A. Adapting proven antibody purification processes to antibody fragments demands different affinity chromatography. Such technology must offer the unit operation advantages noted above, and be suitable for most of the many different types of antibody fragments. Protein L affinity chromatography appears to fulfill these criteria-suggesting its consideration as a key unit operation in antibody fragment processing.

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Section: Mabs and Their Fragments As Therapeutic Agentsmentioning

confidence: 99%

Antibody Fragments and Their Purification by Protein L Affinity Chromatography

Rodrigo¹,

Gruvegard²,

Alstine

2015

Antibodies

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“…Bispecific antibodies that are capable of simultaneous binding to two different antigens are further improving the prospects for clinical applications of conventional antibodies (Fitzgerald & Lugovskoy, 2011). Some shortcomings of antibodies, such as their lengthy timeframe and high cost of production, and their large size can be overcome by development of small single-domain antibody fragments of high stability with the unique capacity to recognize molecules that are inaccessible to conventional antibodies (de Marco, 2011). Several additional classes of ligand-binding proteins, including inactivated enzymes, penicillinbinding proteins, immunophilins and others, further expand the possibilities for diverse practical applications.…”

Section: Diversity Of Ligand-binding Proteinsmentioning

confidence: 99%

Ligand-Binding Proteins: Structure, Stability and Practical Application

Stepanenko¹,

Fonin²,

Stepanenko³

et al. 2012

Protein Structure

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“…[1][2][3]10,11,28,[34][35][36][37] Here, we focus on a number of examples, wherein nanobodies provide special advantages over other equivalent binders. These applications demonstrated a promising future of the use of nanobodies in versatile environments, including basic …”

Section: Versatile Applications Of Nanobodyderived Nanobiotechnologiesmentioning

confidence: 99%

Nanobody-derived nanobiotechnology tool kits for diverse biomedical and biotechnology applications

Wang

Fan

Shao

et al. 2016

IJN

122

107

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Owing to peculiar properties of nanobody, including nanoscale size, robust structure, stable and soluble behaviors in aqueous solution, reversible refolding, high affinity and specificity for only one cognate target, superior cryptic cleft accessibility, and deep tissue penetration, as well as a sustainable source, it has been an ideal research tool for the development of sophisticated nanobiotechnologies. Currently, the nanobody has been evolved into versatile research and application tool kits for diverse biomedical and biotechnology applications. Various nanobody-derived formats, including the nanobody itself, the radionuclide or fluorescent-labeled nanobodies, nanobody homo- or heteromultimers, nanobody-coated nanoparticles, and nanobody-displayed bacteriophages, have been successfully demonstrated as powerful nanobiotechnological tool kits for basic biomedical research, targeting drug delivery and therapy, disease diagnosis, bioimaging, and agricultural and plant protection. These applications indicate a special advantage of these nanobody-derived technologies, already surpassing the “me-too” products of other equivalent binders, such as the full-length antibodies, single-chain variable fragments, antigen-binding fragments, targeting peptides, and DNA-based aptamers. In this review, we summarize the current state of the art in nanobody research, focusing on the nanobody structural features, nanobody production approach, nanobody-derived nanobiotechnology tool kits, and the potentially diverse applications in biomedicine and biotechnology. The future trends, challenges, and limitations of the nanobody-derived nanobiotechnology tool kits are also discussed.

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Biotechnological applications of recombinant single-domain antibody fragments

Cited by 147 publications

References 191 publications

Antibody Fragments and Their Purification by Protein L Affinity Chromatography

Antibody Fragments and Their Purification by Protein L Affinity Chromatography

Ligand-Binding Proteins: Structure, Stability and Practical Application

Nanobody-derived nanobiotechnology tool kits for diverse biomedical and biotechnology applications

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