Fmoc-diphenylalanine self-assembly mechanism induces apparent pk(a) shifts

C. Tang, A.M. Smith, R.F. Collins, R.V. Ulijn, A. Saiani

Research output: Contribution to journalArticle

258 Citations (Scopus)

Abstract

We report the effect of pH on the self-assembly process of Fmoc-diphenylalanine (Fmoc-FF) into fibrils consisting of antiparallel β-sheets, and show that it results in two apparent pKa shifts of 6.4 and 2.2 pH units above the theoretical pKa (3.5). Using Fourier transform infrared (FTIR) spectroscopy, transmission electron microscopy (TEM), wide angle X-ray scattering (WAXS), and oscillatory rheology, these two transitions were shown to coincide with significant structural changes. An entangled network of flexible fibrils forming a weak hydrogel dominates at high pH, while nongelling flat rigid ribbons form at intermediate pH values. Overall, this study provides further understanding of the self-assembly mechanism of aromatic short peptide derivatives.
Original languageEnglish
Pages (from-to)9447-9453
Number of pages6
JournalLangmuir
Volume25
Issue number16
DOIs
Publication statusPublished - 18 Aug 2009

Fingerprint

Self assembly
self assembly
Hydrogel
shift
X ray scattering
Rheology
Hydrogels
Peptides
Fourier transform infrared spectroscopy
Transmission electron microscopy
Derivatives
rheology
ribbons
peptides
infrared spectroscopy
transmission electron microscopy
diphenylalanine
scattering
x rays

Keywords

  • supramolecular hydrogels
  • reversed hydrolysis
  • peptide
  • mineralization
  • biomaterials
  • nanofibers
  • scaffolds
  • cells

Cite this

Tang, C. ; Smith, A.M. ; Collins, R.F. ; Ulijn, R.V. ; Saiani, A. / Fmoc-diphenylalanine self-assembly mechanism induces apparent pk(a) shifts. In: Langmuir. 2009 ; Vol. 25, No. 16. pp. 9447-9453.
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abstract = "We report the effect of pH on the self-assembly process of Fmoc-diphenylalanine (Fmoc-FF) into fibrils consisting of antiparallel β-sheets, and show that it results in two apparent pKa shifts of 6.4 and 2.2 pH units above the theoretical pKa (3.5). Using Fourier transform infrared (FTIR) spectroscopy, transmission electron microscopy (TEM), wide angle X-ray scattering (WAXS), and oscillatory rheology, these two transitions were shown to coincide with significant structural changes. An entangled network of flexible fibrils forming a weak hydrogel dominates at high pH, while nongelling flat rigid ribbons form at intermediate pH values. Overall, this study provides further understanding of the self-assembly mechanism of aromatic short peptide derivatives.",
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Tang, C, Smith, AM, Collins, RF, Ulijn, RV & Saiani, A 2009, 'Fmoc-diphenylalanine self-assembly mechanism induces apparent pk(a) shifts', Langmuir, vol. 25, no. 16, pp. 9447-9453. https://doi.org/10.1021/la900653q

Fmoc-diphenylalanine self-assembly mechanism induces apparent pk(a) shifts. / Tang, C.; Smith, A.M.; Collins, R.F.; Ulijn, R.V.; Saiani, A.

In: Langmuir, Vol. 25, No. 16, 18.08.2009, p. 9447-9453.

Research output: Contribution to journalArticle

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T1 - Fmoc-diphenylalanine self-assembly mechanism induces apparent pk(a) shifts

AU - Tang, C.

AU - Smith, A.M.

AU - Collins, R.F.

AU - Ulijn, R.V.

AU - Saiani, A.

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AB - We report the effect of pH on the self-assembly process of Fmoc-diphenylalanine (Fmoc-FF) into fibrils consisting of antiparallel β-sheets, and show that it results in two apparent pKa shifts of 6.4 and 2.2 pH units above the theoretical pKa (3.5). Using Fourier transform infrared (FTIR) spectroscopy, transmission electron microscopy (TEM), wide angle X-ray scattering (WAXS), and oscillatory rheology, these two transitions were shown to coincide with significant structural changes. An entangled network of flexible fibrils forming a weak hydrogel dominates at high pH, while nongelling flat rigid ribbons form at intermediate pH values. Overall, this study provides further understanding of the self-assembly mechanism of aromatic short peptide derivatives.

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KW - reversed hydrolysis

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KW - biomaterials

KW - nanofibers

KW - scaffolds

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