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Bioinorganic Chemistry and Applications
Volume 2010, Article ID 820476, 13 pages
Research Article

Synthetic Peptides as Structural Maquettes of Angiotensin-I Converting Enzyme Catalytic Sites

1Department of Pharmacy, University of Patras, GR-26504, Patras, Greece
2Department of Chemistry, University of Patras, GR-26504, Patras, Greece

Received 15 January 2010; Accepted 16 March 2010

Academic Editor: Spyros Perlepes

Copyright © 2010 Zinovia Spyranti et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The rational design of synthetic peptides is proposed as an efficient strategy for the structural investigation of crucial protein domains difficult to be produced. Only after half a century since the function of ACE was first reported, was its crystal structure solved. The main obstacle to be overcome for the determination of the high resolution structure was the crystallization of the highly hydrophobic transmembrane domain. Following our previous work, synthetic peptides and Zinc(II) metal ions are used to build structural maquettes of the two Zn-catalytic active sites of the ACE somatic isoform. Structural investigations of the synthetic peptides, representing the two different somatic isoform active sites, through circular dichroism and NMR experiments are reported.