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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D ¹H NMR

Published on: December 16, 2013

Cupryphans, metal-binding, redox-active, redesigned conopeptides.

Marco Barba¹, Anatoli P Sobolev, Cristina Romeo

¹Department of Biology, University Roma Tre, Rome, Italy.

Protein Science : a Publication of the Protein Society

|February 26, 2009

Summary

This summary is machine-generated.

Contryphans, peptides from marine snail venom, serve as robust scaffolds. Researchers engineered these peptides to bind copper ions and mimic superoxide dismutase activity, creating novel mini metalloproteins.

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Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

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Published on: September 7, 2019

Area of Science:

Biochemistry
Peptide Chemistry
Bioinorganic Chemistry

Background:

Contryphans are bioactive peptides from Conus marine snail venom.
They possess unique structural features like disulfide bond cyclization and conserved residues, conferring stability.
These peptides show potential as scaffolds for designing functional molecules.

Purpose of the Study:

To engineer Contryphan scaffolds for redox-active metallomolecule design.
To create novel peptides capable of binding metal ions and catalyzing reactions.
To explore the potential of Contryphans as versatile molecular platforms.

Main Methods:

Computational modeling to design copper-binding sites.
Synthesis and characterization of engineered peptides (Cupryphan and Arg-Cupryphan).
Spectroscopic techniques including optical, fluorescence, ESR, and NMR spectroscopy.
Metal ion binding affinity and superoxide dismutase mimic activity assays.

Main Results:

Engineered peptides, Cupryphan and Arg-Cupryphan, bind Cu(2+) with high affinity (100 nM Kd) and 1:1 stoichiometry.
These peptides exhibit significantly lower affinity for other divalent metals like Zn(2+) and Mg(2+).
Cupryphans demonstrate catalytic activity in superoxide anion dismutation, comparable to existing mimics.

Conclusions:

The Contryphan motif is a stable and adaptable scaffold for functional engineering.
Engineered Contryphans can be designed as catalytically active mini metalloproteins.
This work expands the possibilities for designing novel functional peptides and metalloenzymes.