کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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5220375 | 1383386 | 2012 | 4 صفحه PDF | دانلود رایگان |
The stability and stoichiometry of β3-peptide bundles is influenced by side-chain identity. Previously reported β3-peptides containing β3-homoleucine on one helical face assemble into octamers, whereas those containing β3-homovaline form tetramers. The side chains of β3-homoleucine and β3-homovaline differ in terms of both side-chain length and γ-carbon branching. To evaluate the extent to which these two parameters control β3-peptide bundle stoichiometry, we synthesized the β3-peptide Acid-3Y, which contains β3-homoisoleucine in place of β3-homoleucine or β3-homovaline on one helical face. Acid-3Y assembles into a stable tetramer whose stability resembles that of the previously characterized Acid-VY tetramer. These results suggest that β3-peptide bundle stoichiometry can be modulated by the presence or absence of γ-carbon branching on core side chains.
Journal: Tetrahedron - Volume 68, Issue 23, 10 June 2012, Pages 4342-4345