Self-assembly of short biopeptides onto skin tissue components studied using QCM-D

To enable the discovery of more effective formulations for cosmetic and dermatological applications by understanding the interactions of widely used bioactive ingredients with skin biomolecular components.

Affinities of six common oligopeptide utilized in biomedical application to five primary skin biomolecules (collagen, elastin, laminin, fibronectin and hyaluronic acid) were measured by monitoring their adsorption and subsequent self-assembly using quartz crystal microbalance with dissipation (QCM-D).

Chemical compositions of both the adsorbates (oligo peptides) and the substrates (skin constituents) influence the adsorption behaviour. Notably, the acetylated elastin-like peptide exhibits minimal adsorption, but the same peptide with a palmitoyl tail shows an order of magnitude higher adsorption, possibly due to the formation of self-assembled aggregates. However, the palmitoyl tail does not have the same effect on a collagen-like sequence. Collagen is the most adhesive skin component for the peptides; fibronectin, elastin and laminin are similar with reduced affinity, and hyaluronic acid has the least affinity. A collagen-binding peptide derived from the collagen- binding domain of the von Willebrand factor shows the fastest kinetics. These observed adsorption behaviours can be understood in terms of noncovalent electrostatic and hydrophobic interactions between the adsorbates and substrates.

Adsorption studies of cosmetic product ingredients onto endogenous extracellular matrix components in the skin reported here are expected to provide valuable insights for evaluating their potential efficacy.