Trefoil Factor-1 (TFF1), also known as pS2, is a small peptide that belongs to the trefoil factor family (TFF) of proteins. These proteins are characterized by the presence of one or more trefoil domains, which are compact, stable structures that play a crucial role in mucosal protection and repair. TFF1 is predominantly expressed in the epithelial cells of the stomach and is involved in maintaining the integrity of the gastrointestinal mucosa.
TFF1 is a highly conserved protein that mediates mucosal repair by stimulating cell migration, inhibiting apoptosis, and promoting the barrier function of mucus . It forms a homodimer via a disulfide linkage, which is essential for its wound healing activity . TFF1 is also known to stabilize the mucous gel layer that covers the gastrointestinal mucosa, providing a physical barrier against various noxious agents .
The recombinant form of TFF1 (Human Recombinant, His Tag) is produced using genetic engineering techniques. The gene encoding TFF1 is synthesized and expressed in host cells such as Escherichia coli or Brevibacillus choshinensis . The recombinant protein is then purified using affinity chromatography, typically involving a His tag, which allows for efficient purification.
Recombinant TFF1 has significant potential in therapeutic applications, particularly in the treatment of gastric damage and wound healing . Studies have shown that recombinant TFF1 produced by Brevibacillus choshinensis exhibits better wound healing capabilities compared to that produced by Escherichia coli . This enhanced activity is attributed to the glycosylation of the recombinant protein, which may contribute to its improved functionality .