The use of precision information in biology includes the development of designed antibodies.
Current antibody drugs have increasingly fewer adverse effects due to their high specificity. As a result, therapeutic antibodies have become the predominant class of new drugs developed in recent years. Antibodies have become the best-selling drugs in the pharmaceutical market.
Humans are susceptible to infection by existing and future pathogenic organisms. The immune system continuously evolves its capability to eliminate infectious organisms.
The immune response uses antibodies that are immunoglobulin proteins produced and secreted by plasma cells present in bone marrow. Certain antibodies can be designed, produced and unfused in humans to protect against and to cure diseases.
Some designed antibody treatments provide both act as protection against and therapy for a disease negating the need for a protection-only vaccine.
No cures exist for viral infections. Anti-viral treatment medications often provide only a small benefit as they are minimally effective in stopping further virus production in the body
Mammals generally have similar immune systems. Molecules from humans are recognized as foreign by other species, e.g. mice.
Blood serum from an immunized animal can bind to and kill human tissues, such as cancer cells, in vitro. The serum, however, cannot be used for therapy in humans because it is foreign provokes an adverse response that can be severe.
Monoclonal antibodies are laboratory-produced molecules engineered to serve as substitute antibodies. These monoclonal antibodies are made by identical immune cells that are all clones of a unique parent cell.
Monoclonal antibodies can bind to the part of an a toxin or other foreign substance (known as an antigen) that is recognized by the antibody. An antigen is a molecule or molecular structure, which in particular may be present at the outside of a toxin or other foreign substance (a pathogen), that can be bound to by an antigen-specific antibody. Polyclonal antibodies bind to multiple parts of an antigen and are usually made by several different antibody secreting immune cell lineages.
These engineered antibodies are a tool in biochemistry and medicine. When used as medications, non-proprietary drug names end in “mab” (monoclonal antibodies).
Fully biologic methods takes years to produce viable therapeutics. The process of harvesting, isolating, determining sequence, and finally humanizing animal antibodies is time consuming.
In silico designs (computer modeling and simulation) utilize bioinformatics and computation to save years in the development process. In addition, antibodies can be designed against antigens too toxic to inject into a living creature.
In silico designs are not without flaws. The designed antibodies produced only are as good as the algorithm that produces them.
Pharmaceutical companies develop and produce antibody cocktail products that treat certain diseases such as HIV, Ebola and COVID-19. A cocktail of several antibodies help retain effectiveness even if virus mutations render a single antibody therapy less effective over time. These companies screen billions of antibodies in their human antibody libraries to identify antibody candidates for a specific disease.
Designed antibodies currently are used to treat:
Inflammation (arthritis, colitis, Crohn’s, spondylitis, asthma, transplant rejection)
Cancer (leukemia, lymphoma, squamous cell, colorectal, breast with HER2/neu)
Viral (hepatitis C)
Other (Respiratory Syncytial Virus in children, coagulation in coronary angioplasty)
Dozens of additional designed antibody therapeutics are in clinical trials and will become available over the next few years.