Isolation of a new human scFv antibody recognizing a cell surface binding site to CEACAM1. Large yield production,...

Area of Science:

• Oncology
• Immunology
• Biochemistry

Background:

• The CEACAM1 cell adhesion molecule is re-expressed in advanced stages of various malignancies, making it a potential tumor target antigen.
• CEACAM1 is implicated in solid tumors like malignant melanoma and non-small cell lung cancer.

Purpose of the Study:

• To describe the expression, purification, and characterization of a new single chain variable fragment (scFv) antibody, DIATHIS1.
• To evaluate the stability, activity, and potential in vivo applications of scFv DIATHIS1 targeting CEACAM1.

Main Methods:

• Expression and purification of the scFv DIATHIS1 antibody.
• Biophysical and thermal stability characterization at various temperatures and concentrations.
• Isolation and characterization of monomer and dimer forms of scFv DIATHIS1.

Main Results:

• The production process for scFv DIATHIS1 is robust and reproducible across three validation batches.
• scFv DIATHIS1 is biophysically stable, remains biologically active for at least 24 months, and exhibits favorable thermal stability at 37°C.
• Both monomer and dimer forms of scFv DIATHIS1 show high reactivity for CEACAM1, with the dimer acting as a monomer reservoir.

Conclusions:

• scFv DIATHIS1 is a stable and active antibody fragment targeting CEACAM1.
• The unique monomer-dimer composition of scFv DIATHIS1 may offer improved pharmacokinetic parameters for in vivo applications.
• DIATHIS1 represents a promising candidate for targeted cancer therapies against CEACAM1-expressing tumors.