Abstract
The specific recognition and binding of biological molecules by antibodies is fundamentally important. Natural antibodies are multivalent, having at least two identical ligand-binding sites; this permits them to bind tightly at cell surfaces, which present multiple copies of their target ligands. Antibodies that bind to soluble monovalent ligands, such as most small molecules, do not share this multivalent advantage. Nor do engineered fragments of antibodies, such as single-chain Fv proteins or Fab fragments, which generally possess only a single ligand-binding site. Engineered monovalent antibody/ligand pairs that retain the binding specificity of the antibody, but do not dissociate, are promising components of new delivery systems. These are based on a combination of genetic manipulation of the protein and chemical synthesis of appropriate ligands, examples of which are reviewed here.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1383-1388 |
| Number of pages | 6 |
| Journal | Advanced Drug Delivery Reviews |
| Volume | 60 |
| Issue number | 12 |
| DOIs | |
| State | Published - Sep 15 2008 |
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Keywords
- Affinity label
- Antibody
- Bifunctional chelating agent
- DOTA
- Macrocycle
- Mutagenesis
- Protein engineering
- Receptor
ASJC Scopus subject areas
- Pharmaceutical Science
Cite this
The chemistry of irreversible capture. / Meares, Claude F.
In: Advanced Drug Delivery Reviews, Vol. 60, No. 12, 15.09.2008, p. 1383-1388.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The chemistry of irreversible capture
AU - Meares, Claude F.
PY - 2008/9/15
Y1 - 2008/9/15
N2 - The specific recognition and binding of biological molecules by antibodies is fundamentally important. Natural antibodies are multivalent, having at least two identical ligand-binding sites; this permits them to bind tightly at cell surfaces, which present multiple copies of their target ligands. Antibodies that bind to soluble monovalent ligands, such as most small molecules, do not share this multivalent advantage. Nor do engineered fragments of antibodies, such as single-chain Fv proteins or Fab fragments, which generally possess only a single ligand-binding site. Engineered monovalent antibody/ligand pairs that retain the binding specificity of the antibody, but do not dissociate, are promising components of new delivery systems. These are based on a combination of genetic manipulation of the protein and chemical synthesis of appropriate ligands, examples of which are reviewed here.
AB - The specific recognition and binding of biological molecules by antibodies is fundamentally important. Natural antibodies are multivalent, having at least two identical ligand-binding sites; this permits them to bind tightly at cell surfaces, which present multiple copies of their target ligands. Antibodies that bind to soluble monovalent ligands, such as most small molecules, do not share this multivalent advantage. Nor do engineered fragments of antibodies, such as single-chain Fv proteins or Fab fragments, which generally possess only a single ligand-binding site. Engineered monovalent antibody/ligand pairs that retain the binding specificity of the antibody, but do not dissociate, are promising components of new delivery systems. These are based on a combination of genetic manipulation of the protein and chemical synthesis of appropriate ligands, examples of which are reviewed here.
KW - Affinity label
KW - Antibody
KW - Bifunctional chelating agent
KW - DOTA
KW - Macrocycle
KW - Mutagenesis
KW - Protein engineering
KW - Receptor
UR - http://www.scopus.com/inward/record.url?scp=46849112799&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=46849112799&partnerID=8YFLogxK
U2 - 10.1016/j.addr.2008.04.010
DO - 10.1016/j.addr.2008.04.010
M3 - Article
C2 - 18538444
AN - SCOPUS:46849112799
VL - 60
SP - 1383
EP - 1388
JO - Advanced Drug Delivery Reviews
JF - Advanced Drug Delivery Reviews
SN - 0169-409X
IS - 12
ER -