Spectroscopic characterization of the SH2- and active site-directed peptide sequences of a bivalent Src kinase inhibitor
| Autor: | Ruel Z. B. Desamero, Chrystel Dol, Jeonghee Kang, Adam A. Profit, Justina Chinwong, Karim Walters, Thulashie Sivarajah |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Absorption spectroscopy
Stereochemistry Phenylalanine Infrared spectroscopy Peptide src Homology Domains Catalytic Domain Spectroscopy Fourier Transform Infrared Computer Simulation Fourier transform infrared spectroscopy Phosphotyrosine Instrumentation Protein Kinase Inhibitors Spectroscopy chemistry.chemical_classification biology Chemistry Active site Fluorescence Amino acid src-Family Kinases Models Chemical biology.protein Solvents Peptides Proto-oncogene tyrosine-protein kinase Src |
| Zdroj: | Applied spectroscopy. 63(7) |
| ISSN: | 1943-3530 |
| Popis: | The spectral properties of the SH2 and active site-directed sequences of the bivalent Src kinase inhibitor Ac-EELL(F5)Phe-(GABA)3-pYEEIE-amide (1) have been determined. Ac-pYEEIE-amide (2) and Ac-EELL(F5)Phe-amide (3), as well as the amino acids phosphotyrosine (pTyr) and pentafluorophenylalanine (F5)Phe, have been characterized by electronic absorption, fluorescence, and vibrational spectroscopy. Specific and unique marker bands that originate from the phosphate group of pTyr and the fluorinated aromatic ring of (F5)Phe have been identified, with the latter showing some solvent dependence. Peptide 2 was found to have excitation and emission wavelengths emanating from pTyr at 268 and 295 nm, respectively, whereas peptide 3 displayed excitation and emission peaks attributable to (F5)Phe at 274 and 315 nm, respectively. Fourier transform infrared (FT-IR) analysis of the amino acid pTyr identified distinct marker bands at approximately 930, 1090, and 1330 cm−1 that could be attributed to the phosphate group. These markers were also observed in the IR spectrum of peptide 2. Likewise, peptide 3 displayed a characteristic C–F stretching mode at 961 cm−1 due to the presence of (F5)Phe, including two C–F reporting ring modes at 1509 and 1527 cm−1. Identifying and monitoring spectroscopic changes in these marker bands may afford a means to observe the molecular interactions that occur when peptides 1–3 bind to the Src kinase. |
| Databáze: | OpenAIRE |
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