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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.


Circular dichroism spectra (left) and corresponding diagrams (right) of helical content through data analysis by CDNN software of (a) 2,2,2-trifluoroethanol (TFE) range from 0% to 100% of Zn2+-ACEN(37) samples, at pH = 5.0, T = 25°C, 50 mM Tris-HCl, and 200 mM NaCl and (b) of pH range from 2.6 to 7 of Zn2+-ACEN(37) samples, at 65% TFE, T = 25°C, 50 mM Tris-HCl, and 200 mM NaCl.
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fig4: Circular dichroism spectra (left) and corresponding diagrams (right) of helical content through data analysis by CDNN software of (a) 2,2,2-trifluoroethanol (TFE) range from 0% to 100% of Zn2+-ACEN(37) samples, at pH = 5.0, T = 25°C, 50 mM Tris-HCl, and 200 mM NaCl and (b) of pH range from 2.6 to 7 of Zn2+-ACEN(37) samples, at 65% TFE, T = 25°C, 50 mM Tris-HCl, and 200 mM NaCl.

Mentions: The Circular Dichroism (CD) experiments provided a qualitative determination of the peptide secondary structure elements in different TFE concentrations, pH values, and metal addition, leading to the determination of high resolution experimental conditions (Figure 4).


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)

Circular dichroism spectra (left) and corresponding diagrams (right) of helical content through data analysis by CDNN software of (a) 2,2,2-trifluoroethanol (TFE) range from 0% to 100% of Zn2+-ACEN(37) samples, at pH = 5.0, T = 25°C, 50 mM Tris-HCl, and 200 mM NaCl and (b) of pH range from 2.6 to 7 of Zn2+-ACEN(37) samples, at 65% TFE, T = 25°C, 50 mM Tris-HCl, and 200 mM NaCl.
© Copyright Policy - open-access
Related In: Results  -  Collection

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getmorefigures.php?uid=PMC2902127&req=5

fig4: Circular dichroism spectra (left) and corresponding diagrams (right) of helical content through data analysis by CDNN software of (a) 2,2,2-trifluoroethanol (TFE) range from 0% to 100% of Zn2+-ACEN(37) samples, at pH = 5.0, T = 25°C, 50 mM Tris-HCl, and 200 mM NaCl and (b) of pH range from 2.6 to 7 of Zn2+-ACEN(37) samples, at 65% TFE, T = 25°C, 50 mM Tris-HCl, and 200 mM NaCl.
Mentions: The Circular Dichroism (CD) experiments provided a qualitative determination of the peptide secondary structure elements in different TFE concentrations, pH values, and metal addition, leading to the determination of high resolution experimental conditions (Figure 4).

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.