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Solid-phase synthesis and cyclization of a large branched peptide from IgG Fc with affinity for Fc gammaRI.
- Source :
-
Journal of peptide science : an official publication of the European Peptide Society [J Pept Sci] 1999 Dec; Vol. 5 (12), pp. 555-62. - Publication Year :
- 1999
-
Abstract
- A solid phase approach has been used to synthesize a large branched disulphide peptide from IgG Fc, Ac-F-C*-A-K-V-N-N-K-D-L-P-A-P-I-E-K(Ac-E-L-L-G-G-P-S-V-F)-C*-I-NH2. This peptide combines the lower hinge region of IgG and a proximal beta-hairpin loop, both implicated in binding to Fc gammaRI. Solid phase Tl(tfa)3 cyclization of the linear branched peptide resulted in a poor yield of cyclic hinge-loop peptide (11%) most likely due to steric hindrance caused by the branch. However, if addition of the branch was preceded by solid phase Tl(tfa)3 cyclization of the loop, the yield was excellent at 75%. Cyclic hinge-loop peptide was active in displacing IgG2a from Fc gammaRI expressed on monocyte cell lines with an IC50 of 40 microM, whereas the linear form of this peptide was inactive. The Fc hinge-loop peptide demonstrates the potential for a non-mAb high affinity, immunomodulatory ligand for Fc gammaRI.
- Subjects :
- Amino Acid Sequence
Animals
Cell Line
Flow Cytometry
Humans
Immunoglobulin G metabolism
Magnetic Resonance Spectroscopy
Mice
Oxidation-Reduction
Peptide Fragments chemistry
Peptide Fragments metabolism
Protein Binding
Receptors, IgG metabolism
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Immunoglobulin G chemistry
Peptide Fragments chemical synthesis
Receptors, IgG chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1075-2617
- Volume :
- 5
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Journal of peptide science : an official publication of the European Peptide Society
- Publication Type :
- Academic Journal
- Accession number :
- 10628655
- Full Text :
- https://doi.org/10.1002/(SICI)1099-1387(199912)5:12<555::AID-PSC220>3.0.CO;2-G