CEACAM5 is a gene encoding carcinoembryonic antigen (CEA). The gene was first identified in 1965 from human colon cancer tissue extracts. CEA is a highly glycosylated β-glycoprotein belonging to the CEA-associated cell adhesion molecule (CEACAM) family of the immunoglobulin (Ig) gene superfamily. CEA is closely related to the proteins encoded by CEACAM1, CEACAM3, CEACAM4, CEACAM6, CEACAM7 and CEACAM8. Previous studies have shown that CEA is also expressed at low levels in a polarized manner in normal tissues of epithelial origin, only present in the luminal part of cells, not on the basolateral surface. CEA in normal tissues is now thought to protect luminal organs from microbial infection by binding and capturing infectious microorganisms. Notably, CEA is frequently highly expressed in various colon, lung, thyroid, uterine, ovarian, pancreatic, and medullary thyroid cancers. Cancer cells not only lost the polarized expression of CEA, but also actively stripped CEA from the cell surface by phospholipases, resulting in elevated serum CEA concentrations. Serum CEA levels can be monitored to detect response to cancer treatment or disease recurrence and as a prognostic indicator in patients with various cancers, in which elevated serum CEA levels are indicative of poor prognosis and are associated with reduced overall survival. Therefore, cell-bound CEA has become a target for tumor imaging and various cancer treatments.

Our Services

• Targeted protein structural analysis

Use X-ray single crystal diffraction technology or 3D structural simulation of homologous molecules in the database to obtain structural information of the binding site of CEA molecules;

• Analysis of target protein properties

The structural properties of CEA binding sites, such as electrostatic field, hydrophobic field, hydrogen bond site distribution, etc., were analyzed by molecular simulation software in the field of structural biology;

• Lead Candidate Search

Use database search software (DOCK, F1exX and GOLD) or new drug molecular design technology to identify molecules whose molecular morphology and physicochemical properties match the CEA action site;

• Candidate Compound Validation

Synthesized and tested for biological activity, and after several rounds of screening, suitable lead compounds can be found.

Our Advantage

• Use DRID, GREEN, HSITE and other active site analysis software, combined with software based on Monte Carlo and simulated annealing technology to quickly and accurately find atoms or groups that interact well with the active site of biological macromolecules;
• Flexible selection of ligand-based (commonly used software such as Catalyst and Unity, etc.) and receptor-based (commonly used software such as DOCK, F1exX and GOLD, etc.) search methods for database search;
• For cases where suitable lead compounds cannot be found in the compound database, we can design new compounds through software such as LUDI, Leapfrog, GROW, SPROU and LigBuilder.

Our Capabilities

In each therapeutic area, CD ComputaBio has accumulated deep expertise in discovery informatics, computational chemistry/molecular modeling, medicinal chemistry, structural biology, in vivo and in vitro pharmacology, and translational science. During the drug discovery process, our team focuses on early lead compounds in different target classes and uses a wide range of techniques, including molecular screening, molecular modeling, medicinal chemistry, structural biology, bioinformatics and computational chemistry, to identify new target the direction of drug development, and then select suitable drug candidates through low-cost, high-efficiency computer simulations to ensure high efficiency and low risk in the later drug development process. Our computational biology team has extensive experience in the research of CEA targets. Please consult our professional team for details.

References

1. inkenzeller D, et al.; cea5, a structurally divergent member of the murine carcinoembryonic antigen gene family, is exclusively expressed during early placental development in trophoblast giant cells. J Biol Chem. 1997 Dec 12;272(50):31369-76.
2. Duffy MJ, et al. Carcinoembryonic antigen as a marker for colorectal cancer: is it clinically useful? Clinical Chemistry. 2001, 47 (4): 624–30.
3. Thomas SN, et al. Carcinoembryonic antigen and CD44 variant isoforms cooperate to mediate colon carcinoma cell adhesion to E- and L-selectin in shear flow. The Journal of Biological Chemistry. 2008, 283 (23): 15647–55.