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Supramolecular Structures of Enzyme Clusters.

Nadeem Javid1, Karsten Vogtt, Sangita Roy

  • 1WestCHEM, Department of Pure & Applied Chemistry and Department of Chemical and Process Engineering, University of Strathclyde , Glasgow G1 1XJ, United Kingdom ; WestCHEM, Department of Pure & Applied Chemistry and Department of Chemical and Process Engineering, University of Strathclyde , Glasgow G1 1XJ, United Kingdom.

The Journal of Physical Chemistry Letters
|June 25, 2013
PubMed
Summary

Subtilisin enzyme concentration dictates the formation of fractal-like clusters, influencing biocatalytic self-assembly. These tunable supramolecular enzyme structures offer novel templates for advanced biomaterials.

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Area of Science:

  • Biocatalysis
  • Supramolecular Chemistry
  • Materials Science

Background:

  • Subtilisin enzymes self-assemble into supramolecular structures in aqueous solutions.
  • These structures are known to induce order in the self-assembly of Fmoc-dipeptides.
  • Understanding the structural basis of these clusters is key to controlling self-assembly.

Purpose of the Study:

  • To characterize the mesoscale structure of subtilisin clusters.
  • To investigate the influence of enzyme concentration on cluster formation and dynamics.
  • To explore the potential of these clusters as tunable templates for biocatalytic self-assembly.

Main Methods:

  • Synchrotron small-angle X-ray scattering (SAXS).
  • Dynamic light scattering (DLS).
  • Static light scattering (SLS).

Main Results:

  • Subtilisin clusters exhibit fractal-like arrangements (fractal dimension 1.8–2.6) at low to moderate concentrations.
  • Increasing enzyme concentration leads to structural transitions towards more compact clusters.
  • Dynamic light scattering revealed significantly slower relaxation dynamics in more compact structures.

Conclusions:

  • Enzyme concentration is a critical factor in controlling subtilisin supramolecular cluster architecture.
  • The concentration-dependent fractal nature and structural transitions offer tunable properties.
  • These findings establish subtilisin clusters as versatile templates for directed biocatalytic self-assembly.