When our bodies are placed under stress, such as sun exposure, pollution or inflammation, our cells produce heat shock proteins as part of our natural defence mechanism.
Amélie Gafari, Global Product Manager at Symrise, explains how this class of chaperone proteins helps protect the proteome as we accumulate damages – and does a deep dive into the role of small heat shock proteins, introducing a new ingredient developed to enhance these proteins in the epidermis.
Proteins are responsible for many biological processes in living organisms. In the skin they provide structure (such as keratin, collagen, elastin) and ensure functional processes (cellular respiration, repair, cell communication, waste elimination).
For each protein, the amino acid composition and sequence determines an intricate and highly specific 3D shape that defines what it does and how it works.
Among many families of proteins present in the skin there is one named ‘chaperones’. The role of chaperone proteins is to supervise proper folding (ie, 3D shape) of ‘client’ proteins. They stabilise new proteins to ensure correct folding. When cells undergo stress, proteins are damaged and they misfold. Chaperones will bind to misfolded proteins to prevent irreversible aggregation and they will also refold damaged proteins into their correct shape.