Table 2 Global overview of major distinctions between natural versus synthetic Abs [1]
Properties | Natural Abs | Synthetic Abs |
|---|---|---|
Experimentations | In vivo | In vitro |
Associated technologies | Hybridoma | Molecular display (e.g. yeast, phage, ribosome) |
Epitope binding | Broad | Selective |
Output affinities | Limited | Expanded |
Antigen conformation | Undefined | Defined |
Sequential selections (for shared epitopes) | No | Yes |
Defined selection conditions (e.g. pH, ions, competitors) | No | Yes |
Molecular re-cloning (e.g. change format, add tag, dimerization, enzymatic fusion, autobiotinilation) | Difficult | Simple |
Directed evolution (e.g. improve affinity, specificity, expression, stability) | Difficult | Simple |
Ab framework | Limited | Broad |
Amino acid positional frequencies and identities | No | Yes |
Financial costs and resources | High | Low |
Time for isolation and production | Long | Short |
Integration into NGS platforms | Difficult | Easy |
Amenable to automation | No | Yes |
High-throughput | No | Yes |
Overcome immunological tolerance | Difficult | Easy |
Allows non-antibody scaffolds | No | Yes |
Specificity for protein sequences and conformations | No | Yes |
Target recognition (e.g. chemical modifications and small molecules) | Difficult | Simple |