Peptides and their
conjugates (to lipids, bulky N-terminals, or
other groups) can self-assemble into nanostructures such as fibrils,
nanotubes, coiled coil bundles, and micelles, and these can be used
as platforms to present functional residues in order to catalyze a
diversity of reactions. Peptide structures can be used to template
catalytic sites inspired by those present in natural enzymes as well
as simpler constructs using individual catalytic amino acids, especially
proline and histidine. The literature on the use of peptide (and peptide
conjugate) α-helical and β-sheet structures as well as
turn or disordered peptides in the biocatalysis of a range of organic
reactions including hydrolysis and a variety of coupling reactions
(e.g., aldol reactions) is reviewed. The simpler design rules for
peptide structures compared to those of folded proteins permit ready
ab initio
design (minimalist approach) of effective catalytic
structures that mimic the binding pockets of natural enzymes or which
simply present catalytic motifs at high density on nanostructure scaffolds.
Research on these topics is summarized, along with a discussion of
metal nanoparticle catalysts templated by peptide nanostructures,
especially fibrils. Research showing the high activities of different
classes of peptides in catalyzing many reactions is highlighted. Advances
in peptide design and synthesis methods mean they hold great potential
for future developments of effective bioinspired and biocompatible
catalysts.