Identification of model peptides as affinity ligands for the purification of humanized monoclonal antibodies by means of phage display

Journal of Biochemical and Biophysical Methods

Volumn 49, Issue 1-3, 2001, Pages 443-454

  Ehrlich, G K ^a   Bailon, P ^a  

^a Pharmaceutical and Analytical RandD   (United States)

Author keywords

Affinity chromatography; Binding domain; Bioinformatics; Biopanning; Immunoglobulin G; Molecular modeling; Peptide; Peptidomimetics; Phage display; Protein A

Indexed keywords

AMINO ACID; IMMUNOGLOBULIN FC FRAGMENT; MONOCLONAL ANTIBODY; PEPSIN A; PEPTIDE; PROTEIN A;

AFFINITY CHROMATOGRAPHY; AMINO ACID SEQUENCE; ARTICLE; PEPTIDE SYNTHESIS; PHAGE DISPLAY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN IMMOBILIZATION; PROTEIN PURIFICATION; PROTEIN TARGETING; RECEPTOR AFFINITY; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ANTIBODIES, MONOCLONAL; CHROMATOGRAPHY, AFFINITY; HUMANS; IMMUNOGLOBULIN FRAGMENTS; LIGANDS; MOLECULAR SEQUENCE DATA; PEPSIN A; PEPTIDE FRAGMENTS; PEPTIDE LIBRARY; PEPTIDES; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; STAPHYLOCOCCAL PROTEIN A;

EID: 0035975866     PISSN: 0165022X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0165-022X(01)00212-3     Document Type: Article

References (23)

1. Minimizing a binding domain from Protein A
2. Design, synthesis, and application of a Protein A mimetic
3. Immunoglobulins specificity of TG19318: A novel synthetic ligand for antibody affinity purification
4. IRIS: An innovative Protein A-peptidomimetic solid phase medium for antibody purification
5. A synthetic ligand for IgA affinity purification
6. Affinity purification of mouse monoclonal IgE using a Protein A mimetic ligand [TG19318] immobilized on solid supports
7. Affinity purification of immunoglobulin M using a novel synthetic ligand
8. Identification of peptides that bind to the constant region of a humanized IgG1 monoclonal antibody using phage display
9. Molecular modeling and experimental approaches toward designing a minimalist protein having Fc-binding activity of Staphylococcal Protein A
10. The generation of process suitable, rugged, targeted affinity ligands using phage display technology
11. A humanized antibody that binds to the interleukin 2 receptor
12. Anti-Tac-H, a humanized antibody to the interleukin 2 receptor with new features for immunotherapy in malignant and immune disorders
13. Receptor-affinity chromatography: A one-step purification for recombinant interleukin-2
14. Receptor-affinity chromatography
15. Phage display technology: Affinity selection by biopanning
16. Complete sequence of the staphylococcal gene encoding Protein A. A gene evolved through multiple duplications
17. 15N nuclear magnetic resonance studies of the B domain of staphylococcal Protein A: Sequence specific assignments of the imide 15N resonances of the proline residues and the interaction with human immunoglobulin G
18. 1H NMR assignments and secondary structure of the B domain of staphylococcal Protein A: Structural changes between the free B domain in solution and the Fc-bound B domain in crystal
19. Three-dimensional solution structure of the B domain of staphylococcal Protein A: Comparisons of the solution and crystal structures
20. A synthetic IgG-binding domain based on staphylococcal Protein A
21. The mechanism of binding staphylococcal Protein A to immunoglobin G does not involve helix unwinding
22. An improved strategy for determining resonance assignments for isotopically enriched proteins and its application to an engineered domain of staphylococcal Protein A
23. Structures of bacterial immunoglobulin-binding domains and their complexes with immunoglobulins