Positional effects of phosphoserine on β-hairpin stability.

Alexander J Riemen, Marcey L Waters

Department of Chemistry, CB 3290, University of North Carolina, Chapel Hill, NC 27599, USA.

Organic & biomolecular chemistry 2010 Dec 7

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A disruptive interaction of phosphoserine with tryptophan in peptides that autonomously fold into a β-hairpin structure in aqueous solution was explored in a positional context within the hairpin structure. All the peptides presented here have a serine or phosphoserine directly cross strand from a tryptophan residue in the β-hairpin structure. It was observed that positioning of phosphoserine-tryptophan had a less destabilizing effect if the phosphoserine was on the C-terminus as opposed to the N-terminus. Greater destabilization was observed when the phosphoserine was positioned closer to the nucleating turn sequence rather than the termini of the hairpin. Multiple phosphorylations in a hairpin designed with two cross-strand serine-tryptophan pairs resulted in a greater decrease in hairpin formation with additional incorporations of phosphoserine. The work presented here gives further insight to destabilizing phosphoserine-tryptophan interaction within the β-hairpin model system.

Citation

Alexander J Riemen, Marcey L Waters. Positional effects of phosphoserine on β-hairpin stability. Organic & biomolecular chemistry. 2010 Dec 7;8(23):5411-7