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IR, MS and CD investigations on several conformationally-different peptides

Domenii publicaţii > Chimie + Tipuri publicaţii > Articol în revistã ştiinţificã

Autori: Murariu, M., Dragan, E. S., Drochioiu, G.

Editorial: Int. J. Pept. Res. Therap., 15(4), p.303-311, 2009.

Rezumat:

Solid phase synthetic methodology has been
used to prepare four peptides which form a system able to
monitor metal ion binding to conformationally different
peptides. The 19-residues oligopeptides containing histidine
residues in various positions of Ala or Gly sequences,
namely GGGGHGGGGHGGGGHGGGG, GGGHGGGHG
GGHGGGGGGG, AAAAHAAAAHAAAA-HAAAA, and
AAAHAAAHAAAHAAAAAAA have been synthesized
by Fmoc strategy and characterized by Fourier transform
infrared spectroscopy (FT-IR) as well as electrospray ion
trap mass spectrometry (ESI-MS) and circular dichroism
(CD). The analysis of CD-spectra of the four peptides
revealed that the secondary structure depends much on the
amino acid sequence. Biological and medical consequences
of conformational changes of metal-bound peptides are
further discussed.

Cuvinte cheie: Peptide synthesis, Electrospray ion trap mass spectrometry, FT-IR, Metal binding

URL: http://www.springerlink.com/content/e0w2t342p1480083/