Trypsin substrate analog inhibitor

Eichler J, Houghten RA, Identification of substrate-analog trypsin inhibitors through the screening of synthetic peptide combinatorial libraries, Biochemistry, 32(41) 11035—41, 1993. 

The reason for the exceptional stability of the complex is that pancreatic trypsin inhibitor is a very effective substrate analog. X-ray analyses showed that the inhibitor lies in the active site of the enzyme, positioned such that... 

Enzyme inhibition may be reversible or irreversible with different inhibitors. Irreversible inhibitors usually form covalent bonds and, thus, are not useful for this type of affinity chromatography. Reversible inhibitors work by a variety of mechanisms, but usually competitive inhibitors structurally resemble the peptide substrates and bind the active center. Trichosanthes kirilowii trypsin inhibitor analog (Ala-6-TTI) is a trypsin inhibitor in which... 

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