Biomimetic Peptides and Proteins

Dear Colleagues,

Mimicry is known above all in relation to the world of organisms; however, molecular mimicry is just as widespread. The ability to mimic the functions of some molecules through the engineering of other molecules opened the route to a vast field of research, in both the design and development of biomimetic materials, which are treated in other volumes, and in the field of molecular biomimetics, which are the central topic of this Special Issue.

Proteins are the most versatile functional building blocks of cells and, in turn, are made up of combinations of protein domains, which mediate their interactions and, therefore, their functions.

For biotechnological purposes, the characteristics of proteins and/or their domains can be modified; however, in recent years, synthetic biology and biotechnology have gone further in design and engineering via the concept of functional reprogramming of proteins and protein domains to develop biomimetic molecules. Indeed, a protein or a domain can be attributed by extensive mutagenesis biomimetic characteristics, typical of molecules that are sometimes completely different. A classic example for biomimetic proteins and protein domains are DARPins, in which ankyrin repeat domain loop mutagenesis is used to mimic the hypervariable regions of antibodies and create an antibody-like protein. In general, protein domains in which variable loops are found, and that are easy-to-express, stable and—when needed—immunologically stealthy, are a good starting point for the design of scaffolding proteins, with biomimetic binding features to be used in diagnostics, therapy, biocatalysis, etc.

Protein domains are composed, in turn, of super-secondary structures, of which some mediate interactions crucial to signaling, via intra- and intermolecular binding among linear and or structural epitopes. In several instances, binding regions can be reproduced as synthetic peptides, which are able to mimic or counteract signaling mediated by the whole domain or protein. This allows us to design and develop a plethora of agonist and antagonist peptides, where solid-phase synthesis ensures high yields and a low cost, and allows scientists to be free from troubles with recombinant expression of the whole proteins/domains and their purification.

In addition, the incorporation of non-natural amino acids in synthetic peptidyl scaffolds has improved the field of enzymology and drug discovery. The ability to substitute natural amino acids with non-natural analogues is emerging as a promising approach to elucidate the molecular mechanisms underlying protein folding, stability, and function.

Once relevant binding regions are identified, reproduced as natural sequences of synthetic peptides, and validated for mimicry of a signal-mediating domain/protein, mutant versions can be drawn to design antagonists, and optimization of peptides can be performed to improve stability, delivery, specificity, and biocompatibility.

Dr. Francesco Filippini
Dr. Laura Acquasaliente
Guest Editors

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• molecular mimicry
• protein domain
• synthetic peptide
• scaffold protein
• antibody-like protein
• loop mutagenesis
• rational design
• computational design
• protein motif
• agonist
• antagonist
• non-natural amino acids
• synthetic biology
• structural biology
• biochemistry
• solid-phase synthesis
• binding site