Short peptides in minimalistic biocatalyst design

Krystyna Duncan, Rein V. Ulijn

Research output: Contribution to journalArticle

469 Downloads (Pure)

Abstract

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.
Original languageEnglish
Pages (from-to)67-81
Number of pages15
JournalBiocatalysis
Volume1
Issue number1
DOIs
Publication statusPublished - 1 Sep 2015

Keywords

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

Fingerprint Dive into the research topics of 'Short peptides in minimalistic biocatalyst design'. Together they form a unique fingerprint.

  • Cite this