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首页> 美国卫生研究院文献>Biochemistry and Biophysics Reports >Selection and characterization of high affinity VEGFR1 antibodies from a novel human binary code scFv phage library
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Selection and characterization of high affinity VEGFR1 antibodies from a novel human binary code scFv phage library

机译：从新型人类二进制代码scFv噬菌体文库中选择高亲和力VEGFR1抗体并进行表征

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摘要

VEGFR1 is a receptor tyrosine kinase that has been implicated in cancer pathogenesis. It is upregulated in angiogenic endothelial cells and expressed on human tumor cells as well. VEGFR1 positive hematopoietic progenitor cells home to sites of distant metastases prior to the arrival of the tumor cells thus establishing a pre-metastatic niche. To discover high affinity human antibodies selective for VEGFR1 molecular imaging or for molecularly targeted therapy, a novel phage display scFv library was assembled and characterized. The library was constructed from the humanized 4D5 framework that was mostly comprised tyrosine and serine residues in four complimentarity determining regions (CDRs). The library produced diverse and functional antibodies against a panel of proteins, some of which are of biomedical interest including, CD44, VEGFA, and VEGFR1. After panning, these antibodies had affinity strong enough for molecular imaging or targeted drug delivery without the need for affinity maturation. One of the anti-VEGFR1 scFvs recognized its cognate receptor and was selective for the VEGFR1.
机译：VEGFR1是一种酪氨酸激酶受体，与癌症的发病机理有关。它在血管生成内皮细胞中上调，并在人肿瘤细胞中表达。 VEGFR1阳性造血祖细胞在肿瘤细胞到达之前就已经转移到远处转移，从而建立了转移前的生态位。为了发现对VEGFR1分子成像或分子靶向治疗具有选择性的高亲和力人类抗体，组装并表征了新型噬菌体展示scFv文库。该文库是从人源化4D5框架构建的，该框架主要在四个互补决定区（CDR）中包含酪氨酸和丝氨酸残基。该文库产生了针对一组蛋白质的多种功能抗体，其中一些具有生物医学意义，包括CD44，VEGFA和VEGFR1。淘选后，这些抗体具有足够强的亲和力，可以进行分子成像或靶向药物递送，而无需亲和力成熟。一种抗VEGFR1 scFvs识别其同源受体，并且对VEGFR1具有选择性。

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