The structural integrity of human TFF1 under reducing conditions.

ABSTRACT: The trefoil factor family (TFF) comprises three secretory peptides (TFF1, TFF2, TFF3) that regulate diverse physiological processes to maintain gastrointestinal mucosal integrity and homeostasis. The TFF domain is stabilized by six conserved cysteine residues forming three intramolecular disulfide bonds. In this work, we investigated human TFF1 domain stability against increasing concentrations of the reducing agent tris(2-carboxyethyl)phosphine (TCEP). Experiments revealed high resistance of the disulfide bonds within the TFF1 domain to reduction compared to two reference peptides with similar three-disulfide frameworks, namely the bovine pancreatic trypsin inhibitor (BPTI) and the peptide drug linaclotide. Full reduction of TFF1 was only achieved with a large excess of TCEP (150-fold), a

SUBMITTER: Elmaci DN 

PROVIDER: S-EPMC11889601 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature