Nociceptin and its natural and specifically-modified fragments: Structural studies

Biopolymers
Edyta Podstawka-ProniewiczLeonard M Proniewicz

Abstract

The vibrational structures of Nociceptin (FQ), its short bioactive fragments, and specifically-modified [Tyr¹]FQ (1-6), [His¹]FQ (1-6), and [His(1,4)]FQ (1-6) fragments were characterized. We showed that in the solid state, all of the aforementioned peptides except FQ adopt mainly turn and disordered secondary structures with a small contribution from an antiparallel β-sheet conformation. FQ (1-11), FQ (7-17) [His¹]FQ (1-6), and [His(1,4)]FQ (1-6) have an α-helical backbone arrangement that could also slightly influence their secondary structure. The adsorption behavior of these peptides on a colloidal silver surface in an aqueous solution (pH = ∼8.3) was investigated by means of surface-enhanced Raman scattering (SERS). All of the peptides, excluding FQ (7-17), chemisorbed on the colloidal silver surfaces through a Phe⁴ residue, which for FQ, FQ (1-11), FQ (1-6), [Tyr¹]FQ (1-6), and [His¹]FQ (1-6) lies almost flat on this surface, while for FQ (1-13) and FQ (1-13)NH₂ adopts a slightly tilted orientation with respect to the surface. The Tyr¹ residue in [Tyr¹]FQ (1-6) does not interact with the colloidal silver surface, suggesting that the Tyr¹ and Phe⁴ side chains are located on the opposite sides of the peptide backbone, which...Continue Reading

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Citations

Sep 6, 2011·The Journal of Physical Chemistry. a·Edyta Podstawka-ProniewiczLeonard M Proniewicz
Oct 15, 2014·Journal of Colloid and Interface Science·Helena DominEdyta Proniewicz
Sep 26, 2016·Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy·Agnieszka TątaEdyta Proniewicz

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