Short Peptides in Minimalistic Biocatalyst Design

• Authors: Krystyna L. Duncan , Rein V. Ulijn
• Languages of publication: EN

Abstracts

EN

We review recent developments in the use of
short peptides in the design of minimalistic biocatalysts
focusing on ester hydrolysis. A number of designed peptide
nanostructures are shown to have (modest) catalytic
activity. Five features are discussed and illustrated by
literature examples, including primary peptide sequence,
nanosurfaces/scaffolds, binding pockets, multivalency
and the presence of metal ions. Some of these are derived
from natural enzymes, but others, such as multivalency
of active sites on designed nanofibers, may give rise to
new features not found in natural enzymes. Remarkably,
it is shown that each of these design features give rise to
similar rate enhancements in ester hydrolysis. Overall,
there has been significant progress in the development of
fundamental understanding of the factors that influence
binding and activity in recent years, holding promise for
increasingly rational design of peptide based biocatalysts.

Keywords

EN

primary sequence; histidine; nano-surface/scaffold; multivalency; metals; rational design; catalysis; ester hydrolysis

• Publisher: De Gruyter Open
• Journal: Biocatalysis
• Year: 2014
• Volume: 1
• Issue: 1

Dates

online

1 - 9 - 2015

received

15 - 5 - 2015

accepted

5 - 8 - 2015

Contributors

author

Krystyna L. Duncan

• WestCHEM/Department of Pure
  and Applied Chemistry, University of Strathclyde, Thomas Graham
  Building, 295 Cathedral Street, Glasgow, G1 1XL, UK

author

Rein V. Ulijn

• WestCHEM/Department of Pure
  and Applied Chemistry, University of Strathclyde, Thomas Graham
  Building, 295 Cathedral Street, Glasgow, G1 1XL, UK
• Advanced Science Research
  Center (ASRC) and Hunter College, City University of New York, 85 St
  Nicholas Terrace, New York, NY10031, USA

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Identifiers

DOI

10.1515/boca-2015-0005