AI Article Synopsis
- Researchers modified a β-tubulin-derived peptide to study how changes in amino acids near the phosphorylation site affect its interaction with GRK2.* -
- They discovered that anionic amino acids around the phosphorylation site significantly influence the peptide's affinity for GRK2.* -
- A modified peptide showed much stronger binding to GRK2 while displaying low binding to GRK5, indicating its potential as a selective and sensitive tool for GRK2 research.*
Article Abstract
A series of amino acid substitutions was made in a previously identified β-tubulin-derived GRK2 substrate peptide (DEMEFTEAESNMN) to examine the role of amino acid residues surrounding the phosphorylation site. Anionic amino acid residues surrounding the phosphorylation site played an important role in the affinity for GRK2. Compared to the original peptide, a modified peptide (Ac-EEMEFSEAEANMN-NH) exhibited markedly higher affinity for GRK2, but very low affinity for GRK5, suggesting that it can be a sensitive and selective peptide for GRK2.
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| http://dx.doi.org/10.1007/s00726-016-2345-6 | DOI Listing |
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