Mechanistic insights into phosphatase triggered self-assembly including enhancement of biocatalytic conversion rate

Kate Thornton, Yousef M. Abul-Haija, Nigel Hodson, Rein V. Ulijn

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

We report on the mechanistic investigation of alkaline phosphatase (AP) triggered self-assembly and hydrogelation of Fmoc-tyrosine (Fmoc-Y). We studied separately the biocatalytic conversion using HPLC, changes in supramolecular interactions and chirality using CD and fluorescence spectroscopy, nanostructure formation by AFM and gelation by oscillatory rheometry. Three consecutive stages could be distinguished (which may overlap, depending on the enzyme concentration). Typically, the phosphorylated Fmoc-Y (Fmoc-pY) undergoes rapid and complete dephosphorylation, followed by formation of aggregates which reorganise into nanofibres and consequently give rise to gelation. We observed a remarkable enhancement of catalytic activity during the early stages of the self-assembly process, providing evidence for enhancement of enzymatic activation by the supramolecular structures formed. Overall, this study provides a further step in understanding biocatalytic self-assembly.
LanguageEnglish
Pages9430-9439
Number of pages10
JournalSoft Matter
Volume9
Issue number39
Early online date15 Aug 2013
DOIs
Publication statusPublished - 2013

Fingerprint

phosphatases
Phosphoric Monoester Hydrolases
Self assembly
self assembly
gelation
Gelation
augmentation
Chirality
tyrosine
Fluorescence spectroscopy
Nanofibers
chirality
Alkaline Phosphatase
Tyrosine
catalytic activity
enzymes
Nanostructures
Catalyst activity
Chemical activation
atomic force microscopy

Keywords

  • mechanistic insights
  • phosphatase triggered
  • biocatalytic conversion rate
  • self-assembly
  • enhancement

Cite this

Thornton, Kate ; Abul-Haija, Yousef M. ; Hodson, Nigel ; Ulijn, Rein V. / Mechanistic insights into phosphatase triggered self-assembly including enhancement of biocatalytic conversion rate. In: Soft Matter. 2013 ; Vol. 9, No. 39. pp. 9430-9439.
@article{5b8806e1bfb141fc8df3633fb8ff06d8,
title = "Mechanistic insights into phosphatase triggered self-assembly including enhancement of biocatalytic conversion rate",
abstract = "We report on the mechanistic investigation of alkaline phosphatase (AP) triggered self-assembly and hydrogelation of Fmoc-tyrosine (Fmoc-Y). We studied separately the biocatalytic conversion using HPLC, changes in supramolecular interactions and chirality using CD and fluorescence spectroscopy, nanostructure formation by AFM and gelation by oscillatory rheometry. Three consecutive stages could be distinguished (which may overlap, depending on the enzyme concentration). Typically, the phosphorylated Fmoc-Y (Fmoc-pY) undergoes rapid and complete dephosphorylation, followed by formation of aggregates which reorganise into nanofibres and consequently give rise to gelation. We observed a remarkable enhancement of catalytic activity during the early stages of the self-assembly process, providing evidence for enhancement of enzymatic activation by the supramolecular structures formed. Overall, this study provides a further step in understanding biocatalytic self-assembly.",
keywords = "mechanistic insights, phosphatase triggered, biocatalytic conversion rate, self-assembly, enhancement",
author = "Kate Thornton and Abul-Haija, {Yousef M.} and Nigel Hodson and Ulijn, {Rein V.}",
year = "2013",
doi = "10.1039/C3SM51177D",
language = "English",
volume = "9",
pages = "9430--9439",
journal = "Soft Matter",
issn = "1744-683X",
number = "39",

}

Mechanistic insights into phosphatase triggered self-assembly including enhancement of biocatalytic conversion rate. / Thornton, Kate; Abul-Haija, Yousef M.; Hodson, Nigel; Ulijn, Rein V.

In: Soft Matter, Vol. 9, No. 39, 2013, p. 9430-9439.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Mechanistic insights into phosphatase triggered self-assembly including enhancement of biocatalytic conversion rate

AU - Thornton, Kate

AU - Abul-Haija, Yousef M.

AU - Hodson, Nigel

AU - Ulijn, Rein V.

PY - 2013

Y1 - 2013

N2 - We report on the mechanistic investigation of alkaline phosphatase (AP) triggered self-assembly and hydrogelation of Fmoc-tyrosine (Fmoc-Y). We studied separately the biocatalytic conversion using HPLC, changes in supramolecular interactions and chirality using CD and fluorescence spectroscopy, nanostructure formation by AFM and gelation by oscillatory rheometry. Three consecutive stages could be distinguished (which may overlap, depending on the enzyme concentration). Typically, the phosphorylated Fmoc-Y (Fmoc-pY) undergoes rapid and complete dephosphorylation, followed by formation of aggregates which reorganise into nanofibres and consequently give rise to gelation. We observed a remarkable enhancement of catalytic activity during the early stages of the self-assembly process, providing evidence for enhancement of enzymatic activation by the supramolecular structures formed. Overall, this study provides a further step in understanding biocatalytic self-assembly.

AB - We report on the mechanistic investigation of alkaline phosphatase (AP) triggered self-assembly and hydrogelation of Fmoc-tyrosine (Fmoc-Y). We studied separately the biocatalytic conversion using HPLC, changes in supramolecular interactions and chirality using CD and fluorescence spectroscopy, nanostructure formation by AFM and gelation by oscillatory rheometry. Three consecutive stages could be distinguished (which may overlap, depending on the enzyme concentration). Typically, the phosphorylated Fmoc-Y (Fmoc-pY) undergoes rapid and complete dephosphorylation, followed by formation of aggregates which reorganise into nanofibres and consequently give rise to gelation. We observed a remarkable enhancement of catalytic activity during the early stages of the self-assembly process, providing evidence for enhancement of enzymatic activation by the supramolecular structures formed. Overall, this study provides a further step in understanding biocatalytic self-assembly.

KW - mechanistic insights

KW - phosphatase triggered

KW - biocatalytic conversion rate

KW - self-assembly

KW - enhancement

UR - http://www.scopus.com/inward/record.url?scp=84884369669&partnerID=8YFLogxK

UR - http://dx.doi.org/10.1039/C3SM51177D

U2 - 10.1039/C3SM51177D

DO - 10.1039/C3SM51177D

M3 - Article

VL - 9

SP - 9430

EP - 9439

JO - Soft Matter

T2 - Soft Matter

JF - Soft Matter

SN - 1744-683X

IS - 39

ER -