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Self-assembled peptide fibers from valylvaline bola-amphiphiles by a parallel β-sheet network

Authors
Journal
Biochimica et Biophysica Acta (BBA) - General Subjects
0304-4165
Publisher
Elsevier
Publication Date
Volume
1475
Issue
3
Identifiers
DOI: 10.1016/s0304-4165(00)00088-x
Keywords
  • Bola-Amphiphile
  • Peptide Fiber
  • L-Valyl-L-Valine
  • Self-Assembly
  • β-Sheet
  • Ft-Ir Spectroscopy

Abstract

Abstract A series of dipeptide-based bola-amphiphiles, bis( N-α-amide- L-valyl- L-valine) 1, n-alkane dicarboxylate ( n=4–12), have been synthesized. The bola-amphiphiles with n=4 and 6 self-assembled to form crystalline solids in water, whereas those with n=7–12 produced peptide fibers. FT-IR spectroscopy and X-ray diffraction patterns revealed that the peptide fibers have parallel-type β-sheet networks between the valylvaline units. FT-IR deconvolution study of carboxyl regions indicated that these crystalline solids and peptide fibers are stabilized by interlayer bifurcated and intralayer lateral hydrogen-bond networks between the end carboxylic acid groups, respectively.

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