ISSN:
1573-3904
Keywords:
Circular dichroism spectroscopy
;
Peptide conformation
;
O-phosphotyrosine peptide
;
Solid-phase peptide synthesis
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Summary The continuous-flow Fmoc solid-phase synthesis methodology was used together with the derivative Fmoc-Tyr(PO3Bzl2)-OH to successfully prepare an O-phosphorylated tyrosine analogue of a heptadecapeptide which was designed to adopt an α-helical conformation in solution. Comprehensive chemical characterization, including ion-spray mass spectrometry, confirmed the high purity of the synthetic peptide and the presence of the tyrosine O-phosphate moiety. Circular dichroism spectroscopic analysis showed that, in water and at low concentration, the peptide has a greater degree of helicity or possibly a longer helix chain length than the non-O-phosphorylated form. A similar phenomenon was observed in the membrane-mimicking solvent octyl β-glucoside. The increase in the helicity during trifluoroethanol titration and the absence of apparent coiled coil-type aggregation further demonstrated the intrinsic ability of the peptides to form α-helices. The data, taken together, indicate that, at least for this peptide, the α-helix secondary structural element is more pronounced following tyrosine O-phosphorylation.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00128500
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