Abstract
In this article, we report the distinct solution behavior of a set of urea-dipeptides to that of natural sequence. The urea-dipeptides adopt β-folding conformations and form into β-sheetlike assembly in chloroform. Most surprisedly, the urea-dipeptides tend to form interpeptide H-bonding interactions even at a concentration of as low as 0.1mM, while the natural sequence shows H-bonding propensity at a concentration of about 7mM, indicating that the urea-dipeptides show much stronger H-bonding propensity to nucleate formation of β-sheetlike assembly than the natural sequence. CD spectra reveal that the investigated urea-dipeptides have two negative CD bands, respectively, around 217nm and 224nm, supporting the β-folding conformations and in turn formation of β-sheetlike assembly. The β-sheetlike assembly is also confirmed by the XRD reflections, which give two typical d-spacings of 12.7 and 4.8Å, respectively, corresponding to stacking periodicity of the β-sheets and the spacing between peptide backbones running orthogonal to the β-sheet axis.
Published Version
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