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31 de May de 2021

How to get peptides with the Phage Display technique

Phage Display is an in vitro peptide ligand selection technique from genomic libraries, as explained on here.

What is the phage display:

O phage display is a powerful technique for the identification and selection of peptides., proteins or antibodies with high affinity and specificity for a specific target.

First described in 1985, this technology has influenced work and discoveries made in the fields of cell biology, immunology, pharmacology, in addition to allowing the study of the molecular interactions of a single molecule or cell.

How to get quality peptides:

Recently, a article published in Nature Comunication chamado “A minimalistic cyclic ice-binding peptide from phage display”, published by Stevens et al., a new theory was discussed to create an alternative to the development of synthetic mimetics of Ice-binding proteins (IBP) using the phage display.
PPIs are a diverse class of proteins that help the organism survive in the presence of ice in cold climates.. They have different origins in many organisms., including bacteria, fungi, plants, insects and fish. This mechanism occurs because freezing is lethal to most organisms and the formation of ice crystals can damage cell membranes., which results in cell disruption.

Between as IBPs, one of the most used are antifreeze proteins, that inhibit the formation of large ice grains inside cells that can damage cell organelles or cause cell death.
But the synthesis of peptides that mimic interactions between IBPs and ice, particularly in large-scale productions, are very variable these days.
Due to this, an alternative is to use the phage display to find peptides that can simplify this binding cycle, once phage display usually leads to selection of short peptides that are composed of naturally occurring amino acids., which can increase the synthetic accessibility of new ice-binding peptides.

recent results:

And the work demonstrated an excellent application of the phage display to find successful short IBP mimetic peptides, complementing traditional design approaches, demonstrating a diversity of peptides that can be screened for potential binding to ice crystals.
This can be used as a promising tool in industrial applications such as cryobiology, food storage, agriculture and technology for development and maintenance by lyophilization of proteins and immunobiologicals.

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