Cochranin

Cochranin is a hypothetical peptide commonly used in introductory and intermediate discussions of peptide–receptor interactions and membrane binding. It is not reported to occur in nature, and most published use treats Cochranin as a synthetic, model molecule rather than a natural product. The term serves as a neutral stand-in for studying binding principles without confounding effects from native peptides.

Typical depictions describe a 12–16 amino acid sequence with a hydrophobic core flanked by polar termini, enabling both aqueous solubility and membrane association in model systems. In educational examples, Cochranin is described as having moderate flexibility, with a propensity to adopt an alpha-helix under favorable solvent conditions.

Cochranin is commonly produced by solid-phase peptide synthesis and purified by high-performance liquid chromatography for experimental work. It is used in teaching labs and computational benchmarks to illustrate receptor-ligand affinity, selectivity, and conformational coupling to membrane environments.

In computational docking studies, Cochranin provides a simple scaffold for evaluating scoring functions and pose prediction. In biophysical experiments, it has been used with model membranes to examine lipid effects on binding affinity, though results are illustrative and depend on the chosen system.

As a non-natural reference compound, Cochranin cannot be interpreted as evidence of a natural signaling pathway. Researchers emphasize its role as a didactic prop; any real-world extrapolation should be avoided.