IR, MS and CD Investigations on Several Conformationally-Different Histidine Peptides |
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Authors: | Manuela Murariu Ecaterina Stela Dragan Gabi Drochioiu |
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Institution: | (1) “Petru Poni” Institute of Macromolecular Chemistry, Aleea Grigore Ghica Voda 41 A, 700487 Iasi, Romania;(2) Faculty of Chemistry, “Al. I. Cuza” University of Iasi, 11 Carol I, 700506 Iasi, Romania; |
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Abstract: | 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, GGGHGGGHGGGHGGGGGGG, 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. |
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Keywords: | |
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