A remarkable emergent property of spontaneous (amino acid content) symmetry breaking

TL;DR

This paper discusses the significance of amino acid symmetry breaking in protein folding and its potential implications for developing folding inhibition drugs that could reduce resistance in treatments, especially for viruses.

Contribution

It introduces the concept of symmetry breaking in amino acid content as an emergent property relevant to protein folding and drug design.

Findings

Amino acid symmetry breaking is a key property in protein folding.

Understanding this property can lead to new drug design strategies.

Folding inhibition may reduce drug resistance in viral treatments.

Abstract

Learning how proteins fold will hardly have any impact in the way conventional -- active site centered -- drugs are designed. On the other hand, this knowledge is proving instrumental in defining a new paradigm for the identification of drugs against any target protein: folding inhibition. Targeting folding renders drugs less prone to elicit spontaneous genetic mutations which in many cases, notably in connection with viruses like the Human Immunodeficiency Virus (HIV), can block therapeutic action. From the progress which has taken place during the last years in the understanding of the becoming of a protein, and how to read from the corresponding sequences the associated three-dimensional, biologically active, native structure, the idea of non-conventional (folding) inhibitors and thus of leads to eventual drugs to fight disease, arguably, without creating resistance, emerges as a distinct possibility.