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Updated: Oct 1, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
The Structural Distinction of α- and α,γ-Hybrid Peptides Influences Their Zn(II)-Coordinated Supramolecular
Sanjit Dey1, Souvik Roy1, Sandip U Toraskar1
1Department of Chemistry, Indian Institute of Science Education and Research (IISER), Pune, India.
Abstract:
The integration of protein secondary structures with metal ions offers a promising strategy for designing highly ordered self-assembled structures with enhanced stability and functionality. The nature of the amino acids plays a crucial role in dictating the secondary structures of peptides. Here, we report highly stable and porous ZnCl2-helix-frameworks from the α,γ-hybrid peptide containing terminal 4-pyridyl groups, whereas the control α-peptide showed a ZnCl2-coordinated left-handed superhelix network. The stable, porous 12-helix frameworks of the α,γ-hybrid peptide have been further explored as hosts to encapsulate guest solvent molecules such as nitromethane and 1,2-dichloroethane after soaking the metal-coordinated-helix-frameworks. Overall, the substitution of an α-amino acid in a short α-peptide sequence with a γ-amino acid leads to a change in the helical structure as well as in its coordination ability.
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