Fiche publication
Date publication
mars 2019
Journal
Protein science : a publication of the Protein Society
Auteurs
Membres identifiés du Cancéropôle Est :
Dr VAN DORSSELAER Alain
Tous les auteurs :
Boutin JA, Tartar AL, van Dorsselaer A, Vaudry H
Lien Pubmed
Résumé
Many peptide chemistry scientists have been reporting extremely interesting work on the basis of chemical peptides for which the only characterization was their purity, mass, and biological activity. It seems slightly overenthusiastic, as many of these structures should be thoroughly characterized first to demonstrate the uniqueness of the structure, as opposed to the uniqueness of the sequence. Among the peptides of identical sequences in the final chemical preparation, what amount of well-folded peptide supports the measured activity? The activity of a peptide preparation cannot prove the purity of the desired peptide. Therefore, greater care should be taken in characterizing peptides, particularly those coming from chemical synthesis. At a time when the pharmaceutical industry is changing its paradigm by moving substantially from small molecules to biologics to better serve patients' needs, it is important to understand the limitations of the descriptions of these products and to start to apply the same 'good laboratory practices' to our peptide research. Here, we attempt to delineate how synthetic peptides are described and characterized and what will be needed to describe them in regards to how they are well-folded and homogeneous in their tertiary structure. Older studies were done when the tools were not yet discovered, but more recent publications are still lacking proper descriptions of these peptides. Modern tools of analysis are capable of segregating folded and unfolded peptides, even if the preparation is biologically active. This article is protected by copyright. All rights reserved.
Mots clés
characterization, peptides, solid-phase synthesis, structure
Référence
Protein Sci.. 2019 Mar 9;:
