Antibodies, also known as immunoglobulins, are large Y-shaped glycoproteins produced by B cells as part of the immune response. They play a crucial role in identifying and neutralizing pathogens by binding to specific antigens .
Antibodies consist of four polypeptide chains: two identical heavy chains and two identical light chains, connected by disulfide bonds. Each chain is composed of domains, which are sequences of about 110 amino acids. The variable domains (VH and VL) form the antigen-binding site, while the constant domains (CH and CL) determine the antibody's class and effector functions .
| Component | Description |
|---|---|
| Heavy Chains | Contain VH and multiple CH domains |
| Light Chains | Contain VL and CL domains |
| Variable Domains | VH and VL form the antigen-binding site |
| Constant Domains | Determine antibody class and effector functions |
Antibodies bind to antigens through their variable regions, forming a complex that can neutralize pathogens or mark them for destruction by other immune cells. The strength of this binding is measured by affinity and avidity .
Recent research has focused on developing novel antibodies for therapeutic applications, such as bispecific antibodies and antibody-drug conjugates. For example, BL-B01D1 is a bispecific antibody targeting EGFR and HER3, showing promise in treating solid tumors .
| Antibody Type | Target | Application |
|---|---|---|
| Bispecific Antibodies | EGFR and HER3 | Solid Tumors |
| Monoclonal Antibodies | Specific Antigens | Various Diseases |