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Article title

Short Peptides in Minimalistic Biocatalyst Design

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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.
Publisher

Journal
Year
Volume
1
Issue
1
Physical description
Dates
online
1 - 9 - 2015
received
15 - 5 - 2015
accepted
5 - 8 - 2015
Contributors
  • WestCHEM/Department of Pure
    and Applied Chemistry, University of Strathclyde, Thomas Graham
    Building, 295 Cathedral Street, Glasgow, G1 1XL, UK
author
  • 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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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.-psjd-doi-10_1515_boca-2015-0005
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