Trefoil peptides: from structure to function

Cell Mol Life Sci. 1997 Dec;53(11-12):888-903. doi: 10.1007/s000180050108.


The unique structure in which six cysteine residues in a sequence of 38 or 39 amino acid residues form three disulphide bonds in a 1-5, 2-4 and 3-6 configuration constitutes the basic elements of a trefoil domain. Today three mammalian trefoil factors (TFF1, TFF2 and TFF3) containing one or two trefoil domains are known. Trefoil factors are usually associated with the mucin layer of the gastrointestinal tract. Early studies on trefoil factors concentrated on structure elucidation and sites of expression in health and disease, whereas studies over the last 3-5 years have focused on the mechanism of action and the search for specific receptors. This review summarises our present knowledge of trefoil peptide structures, their sites of expression, and their protection and repair functions, with a focus on the mechanism by which these peptides exert their biological function.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cysteine / chemistry
  • Digestive System Physiological Phenomena*
  • Growth Substances*
  • Humans
  • Intercellular Signaling Peptides and Proteins
  • Intestinal Mucosa / physiology
  • Mice
  • Mice, Transgenic
  • Models, Molecular
  • Molecular Sequence Data
  • Mucins*
  • Muscle Proteins*
  • Neuropeptides*
  • Peptides*
  • Proteins*
  • Rats
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Structure-Activity Relationship
  • Terminology as Topic
  • Trefoil Factor-1
  • Trefoil Factor-2
  • Trefoil Factor-3
  • Tumor Suppressor Proteins


  • Growth Substances
  • Intercellular Signaling Peptides and Proteins
  • Mucins
  • Muscle Proteins
  • Neuropeptides
  • Peptides
  • Proteins
  • TFF1 protein, human
  • TFF2 protein, human
  • TFF3 protein, rat
  • Tff2 protein, rat
  • Trefoil Factor-1
  • Trefoil Factor-2
  • Trefoil Factor-3
  • Tumor Suppressor Proteins
  • pancreatic spasmolytic polypeptide
  • Cysteine