Proteolinen

Proteolinen is a coined term used in some proteomics contexts to refer to short peptide fragments generated by the proteolytic cleavage of larger protein precursors. These peptides—often called bioactive peptides in the literature—can act as signaling molecules with roles in endocrine, nervous, and immune systems.

Generation and structure: Proteolinen are produced by proteases (e.g., convertases, exopeptidases) that cleave precursor proteins such as prohormones, proproteins, or larger structural proteins. They may undergo post-translational modifications such as C-terminal amidation or disulfide bond formation, which can influence activity and receptor binding. Most proteolinen are short, typically a few amino acids to a few tens of residues, and their activity depends on sequence and structure.

Functions and examples: They can function as hormones, neurotransmitters, or antimicrobial peptides. Classical examples include peptides derived from larger precursors like angiotensin from angiotensinogen, bradykinin from kininogen, or opioid peptides from proopiomelanocortin; these illustrate how processing yields active fragments with specific receptors.

Detection and research: Proteolinen are studied through peptidomics and mass spectrometry; challenges include instability and rapid degradation. They may act locally or circulate systemically, and their levels can reflect physiological or pathological states.

In summary: The term proteolinen describes a broad class of short bioactive peptides produced by proteolysis of larger proteins, with diverse roles in biology and potential medical applications.