IR, MS and CD Investigations on Several Conformationally-Different Histidine Peptides View Full Text


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Article Info

DATE

2009-12

AUTHORS

Manuela Murariu, Ecaterina Stela Dragan, Gabi Drochioiu

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. More... »

PAGES

303

References to SciGraph publications

  • 2008-12. Modern Solid Phase Peptide Synthesis and its Applications in INTERNATIONAL JOURNAL OF PEPTIDE RESEARCH AND THERAPEUTICS
  • 2008-11. Decision tree–driven tandem mass spectrometry for shotgun proteomics in NATURE METHODS
  • 2008-12. Development of a Method for the Solid-Phase Peptide Synthesis in Water in INTERNATIONAL JOURNAL OF PEPTIDE RESEARCH AND THERAPEUTICS
  • 2008-12. Solid Phase Synthesis and Application of Labeled Peptide Derivatives: Probes of Receptor-Opioid Peptide Interactions in INTERNATIONAL JOURNAL OF PEPTIDE RESEARCH AND THERAPEUTICS
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