Reformat into scFv

In the recent years, apart from intact full length antibodies made up of separate heavy and light chains, single-chain antibody fragments (scFvs) including minibodies, diabodies and scFv-Fcs have drawn increasing interest for a variety of diagnostic and therapeutic applications. With years of experience in the protein and antibody engineering, Creative Biolabs offers the first class antibody reformatting services to help your obtain scFvs to promote your antibody design and drug discovery progress.

Features of scFv

scFv is an antibody fragments composed of the variable regions of the heavy (V_H) and light chains (V_L) of antibodies, fused by a short linker peptide of 10 to 25 amino acids. Generally, scFvs produce well in bacterial systems and are the preferred format for a number of antibody phage display libraries. Larger single chain fragments add mass and function, such as scFv-Fc (scFvs fused to full Fc regions, ~110 kDa), and dimeric scFv-C_H3 fusions (minibodies, ~80 kDa). Diabody is the smallest bivalent fragment, about 50–55 kDa, which is generated when the linker in a scFv is shortened (3–10 residues) to induce dimerization.

Reformat into scFv

In general, engineering antibodies with enhanced properties, such as stability, have commonly been accomplished by mutating single or combinations of key amino acid residues. According to different goals and applications, Creative Biolabs is able to routinely reformat the selected antibodies into scFvs. We have developed an advanced in silico platform comprised several techniques, such as homology modeling, molecular dynamics simulation, in-house algorithm, and antibody molecule model analysis. By means of these advanced techniques, we are able to identification the main residues affecting the certain characteristic of the target antibody, and then the mutation on these amino acid residues can be performed. In this way, the target antibody molecule can maintain a relatively stable physicochemical property after reformat into scFv and keep the original affinity and function.

Fig 1. Structure of the CD3-ε/δ/UCHT1-scFv complex and topology of the CD3-ε/δ dimer. (Arnett, K. L., 2004)

Reformat into scFv-Fc

scFv-Fc keeps the specificity of the original immunoglobulin, and importantly, it outperforms whole IgG in production speed, production yield, and engineering flexibility. Besides, it has many advantages over the phage display-derived scFv, such as longer half-life, bivalent binding, as well as Fc-mediated effector functions. Creative Biolabs has built an extremely efficient in silico platform to reformat antibodies into scFv-Fc. With these well-developed technologies, we are confident in offering optimal scFv-Fc molecular model for customers, to help you produce the desired scFv-Fc with good stability, high affinity, as well as ideal specificity.

With our comprehensive structure-based antibody reformatting platform, we are confident in providing high quality scFv reformatting services for our clients. We customize the service according to the specific requirements from the customers. We also provide other structure-based antibody reformatting services. Please contact us for more information and a detailed quote.

References

1. Li, K., (2015). “A fully human scFv phage display library for rapid antibody fragment reformatting.” Protein Engineering, Design and Selection, 28(10), 307-316.
2. Rodrigo, G., (2015). “Antibody fragments and their purification by protein L affinity chromatography.” Antibodies, 4(3), 259-277.
3. Arnett, K. L., (2004). “Crystal structure of a human CD3-ε/δ dimer in complex with a UCHT1 single-chain antibody fragment.” Proceedings of the National Academy of Sciences of the United States of America, 101(46), 16268-16273.

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