Serpins’ role in skin treatment: structure, active fragments and mechanism of inhibition

Serpins (serine protease inhibitors) is the gene family including peptides with similar structure but showing different activity. Their crucial role is to control the action of proteases, enzymes involved in peptide bond hydrolysis [1]. One of serpins is Serpin A1 (S-A1), which has an ability to influence on collagen degradation process and is highly concerned with tissue remodelling pathways [2]. In case of S-A1 it was noticed that biological activity – except already known Reactive Centre Loop – is served also by 36 amino acid sequence situated on C-terminus. Sandwich ELISA test demonstrated significant role of Ac-MGKVVNPTQ-NH2 peptide (S-A1-III) in increased level of collagen, despite the presence of collagenase in the sample [3]. Further investigations with molecular docking methods have shown a high probability of Matrix Metalloproteinase 9 and Neutrophil Elastase inhibition by the S-A1-III. Pivotal role of serpins and their chain-modification prospective allows to consider them as wound-healing agent or potential ingredient of cosmeceuticals.