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Synthetic peptides as structural maquettes of Angiotensin-I converting enzyme catalytic sites.

Spyranti Z, Galanis AS, Pairas G, Spyroulias GA, Manessi-Zoupa E, Cordopatis P - Bioinorg Chem Appl (2010)

Bottom Line: 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.Structural investigations of the synthetic peptides, representing the two different somatic isoform active sites, through circular dichroism and NMR experiments are reported.

View Article: PubMed Central - PubMed

Affiliation: Department of Pharmacy, University of Patras, GR-26504, Patras, Greece.

ABSTRACT
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.

No MeSH data available.


Fingerprint regions of 600 MHz TOCSY ((a) ACEC(37) and (b) ACEN(37)) and NOESY ((c) ACEC(37) and (d) ACEN(37)) spectra recorded at T = 298 K. The sequential connectivity pattern shown indicates the peptide sequence-specific resonance assignment.
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fig5: Fingerprint regions of 600 MHz TOCSY ((a) ACEC(37) and (b) ACEN(37)) and NOESY ((c) ACEC(37) and (d) ACEN(37)) spectra recorded at T = 298 K. The sequential connectivity pattern shown indicates the peptide sequence-specific resonance assignment.

Mentions: Thirty-six out of 37 residues of the backbone of both Zn2+-ACE peptides have been identified through the analysis of the TOCSY spectra (Figure 5). 1H spin systems of the His, Phe and Tyr aromatic rings were identified with the combined use of [1H- 1H]- TOCSY and NOESY spectra (Tables 1 and 2). The two proline residues existing in each construct were found to be at trans conformation for both peptides manifested by strong Hδ(i)Pro- Hα(i-1) NOE connectivities.


Synthetic peptides as structural maquettes of Angiotensin-I converting enzyme catalytic sites.

Spyranti Z, Galanis AS, Pairas G, Spyroulias GA, Manessi-Zoupa E, Cordopatis P - Bioinorg Chem Appl (2010)

Fingerprint regions of 600 MHz TOCSY ((a) ACEC(37) and (b) ACEN(37)) and NOESY ((c) ACEC(37) and (d) ACEN(37)) spectra recorded at T = 298 K. The sequential connectivity pattern shown indicates the peptide sequence-specific resonance assignment.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2902127&req=5

fig5: Fingerprint regions of 600 MHz TOCSY ((a) ACEC(37) and (b) ACEN(37)) and NOESY ((c) ACEC(37) and (d) ACEN(37)) spectra recorded at T = 298 K. The sequential connectivity pattern shown indicates the peptide sequence-specific resonance assignment.
Mentions: Thirty-six out of 37 residues of the backbone of both Zn2+-ACE peptides have been identified through the analysis of the TOCSY spectra (Figure 5). 1H spin systems of the His, Phe and Tyr aromatic rings were identified with the combined use of [1H- 1H]- TOCSY and NOESY spectra (Tables 1 and 2). The two proline residues existing in each construct were found to be at trans conformation for both peptides manifested by strong Hδ(i)Pro- Hα(i-1) NOE connectivities.

Bottom Line: 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.Structural investigations of the synthetic peptides, representing the two different somatic isoform active sites, through circular dichroism and NMR experiments are reported.

View Article: PubMed Central - PubMed

Affiliation: Department of Pharmacy, University of Patras, GR-26504, Patras, Greece.

ABSTRACT
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.

No MeSH data available.