The following Tendemistat description is based on scoop, koning et al. (2003)[1] and Vertesy et al. (1984)[2] :
Tendemistat is a 74 amino acid protein produced by Streptomyces tendae. Though it has been suggested to perform a regulatory role in its natural producer[3], its native purpose remains unclear. However, tendamistat was found to be a potent inhibitor of alpha-amylase. Tendamistat was specifically found to affect mammalian enzymes, and has shown no effect on alpha-amylases from other sources such as plants and bacteria. Tendamistat (green) forms a tight stoichiometric 1:1 complex with alpha-amylase (orange), a crystal structure of the complex was determined to a 2.5 A resolution [4] .
A few crystal structures have been determined for tendamistat, the latest being determined to a 0.93 A resolution [5] . The binding of tendamistat to alpha-amylase leads to the steric blockage of the active site of the enzyme.
Structurally tendamistat belongs to the scoop class of all beta proteins, since it is exclusivly formed of beta sheets . Former research have concidered tendamistat as a therapoic agent for diabetes mellitus due to its ability to block alpha amylase activity. However, tendamistat was found to be immunogenic, and therefore could not be used as a cure on its own. Currently tendamistat is mainly interesting as a scaffold for designed new peptide inhibitors of alpha-amylase [6], and as a general model for biophysical studies on protein folding.
