Generation and analyses of human synthetic antibody libraries and their application for protein microarrays

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Bibtex

@article{b31dd1d96a8f45558ebed985d831e0b1,
title = "Generation and analyses of human synthetic antibody libraries and their application for protein microarrays",
abstract = "Antibody-based proteomics offers distinct advantages in the analysis of complex samples for discovery and validation of biomarkers associated with disease. However, its large-scale implementation requires tools and technologies that allow development of suitable antibody or antibody fragments in a high-throughput manner. To address this we designed and constructed two human synthetic antibody fragment (scFv) libraries denoted HelL-11 and HelL-13. By the use of phage display technology, in total 466 unique scFv antibodies specific for 114 different antigens were generated. The specificities of these antibodies were analyzed in a variety of immunochemical assays and a subset was further evaluated for functionality in protein microarray applications. This high-throughput approach demonstrates the ability to rapidly generate a wealth of reagents not only for proteome research, but potentially also for diagnostics and therapeutics. In addition, this work provides a great example on how a synthetic approach can be used to optimize library designs. By having precise control of the diversity introduced into the antigen-binding sites, synthetic libraries offer increased understanding of how different diversity contributes to antibody binding reactivity and stability, thereby providing the key to future library optimization.",
keywords = "affinity proteomics, phage display technology, protein microarrays, scFv, synthetic antibody libraries",
author = "Anna S{\"a}ll and Maria Walle and Christer Wingren and Susanne M{\"u}ller and Tomas Nyman and Andrea Vala and Mats Ohlin and Borrebaeck, {Carl A K} and Helena Persson",
year = "2016",
month = "10",
day = "1",
doi = "10.1093/protein/gzw042",
language = "English",
volume = "29",
pages = "427--437",
journal = "Protein Engineering, Design and Selection",
issn = "1741-0126",
publisher = "Oxford University Press",
number = "10",

}