Synthesis and structure-activity relationship studies of IgG-binding peptides focused on the C-terminal histidine residue
2019
Currently, IgG-binding peptides are widely utilized as a research tool, as a molecule that guides substrates to the Fc site for the site-selective antibody modification, leading to preparation of a homogeneous antibody-drug conjugate. In this study, a structure activity relationship study of an IgG-binding peptide, 15-IgBP that focused on its C-terminal His residue was performed in an attempt to create more potent peptides. A peptide with a substitution of His17 by 2-pyridylalanine (2-Pya) showed a good binding affinity (15-His17(2-Pya), Kd = 76 nM). In combination with a previous result, we obtained 15-Lys8Leu/His17(2-Pya)-OH that showed a potent binding affinity (Kd = 2.5 nM) and avoided three synthetic problems concerning the p-hydroxybenzyl amidation at the C-terminus, the difficulty associated with coupling at the His7 position and the racemization of 2-Pya.
Keywords:
- Correction
- Source
- Cite
- Save
- Machine Reading By IdeaReader
27
References
1
Citations
NaN
KQI