Effect of the d-Phe2 residue on molecular conformation of an endogenous neuropeptide achatin-I Comparison of X-ray crystal structures of achatin-I (H-Gly-d-Phe-Ala-Asp-OH) and achatin-II (H-Gly-Phe-Ala-Asp-OH)

Add time:08/12/2019    Source:sciencedirect.com

The molecular conformation of achatin-II neutral form (H-Gly-Phe-Ala-Asp-OH), an endogenous peptide from the Achatina fulica ganglia, was elucidated by X-ray crystal analysis. The molecule takes an extended β-pleated structure stabilized by 5 intermolecular hydrogen bonds with the antiparallely arranged molecules. This is in contrast with the turn conformation of a neuroactive achatin-I (H-Gly-d-Phe-Ala-Asp-OH) [(1992) FEBS Lett. 276, 95–97]. The conformational comparison of both of the molecules makes clear the structural role which d-Phe residue of achatin-I plays in forming a definite active form.

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