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The Effect of Fluoro Substitution upon the β-Hairpin Fold of a β-Tetrapeptide in Methanol

✍ Scribed by Stephan Bachmann; Bernhard Jaun; Wilfred F. van Gunsteren; Dongqi Wang

Publisher
John Wiley and Sons
Year
2010
Tongue
German
Weight
791 KB
Volume
93
Category
Article
ISSN
0018-019X

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✦ Synopsis

The importance of b-peptides lies in their ability to mimic the conformational behavior of a-peptides, even with a much shorter chain length, and in their resistance to proteases. To investigate the effect of substitution of b-peptides on their dominant fold, we have carried out a molecular-dynamics (MD) simulation study of two tetrapeptides, Ac-(2R,3S)-b 2,3 hVal(aMe)-(2S)-b 2 hPhe-(R)-b 3 hLys-(2R,3S)-b 2,3 -Ala(aMe)-NH 2 , differing in the substitution at the C a of Phe2 (pepF with F, and pepH with H). Three simulations, unrestrained (UNRES), using 3 J-coupling biasing with local elevation in combination with either instantaneous (INS) or time-averaging (AVE) NOE distance restraining, were carried out for each peptide. In the unrestrained simulations, we find three (pepF) and two (pepH) NOE distance bound violations of maximally 0.22 nm that involve the terminal residues. The restrained simulations match both the NOE distance bounds and 3 J-values derived from experiment. The fluorinated peptide shows a slightly larger conformational variability than the non-fluorinated one.

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