Research
About MetAP2

Methionine aminopeptidase type II (MetAP2) is an enzyme in the metallopeptidase class that removes the initiator methionine residue from newly-formed protein chains. Methionine removal is important in the regulation of a number of cellular processes - protein turnover, protein targeting, and cell proliferation. MetAP2 activity is an essential cellular activity.

In 1997, MetAP2 was identified as the cellular target of fumagillin class molecules. The small molecule fumagillol derivatives – TNP-470, PPI-2458 and CKD-732 – were all shown to inhibit cell growth, which led various groups to conclude that MetAP2 participates in the regulation of cell proliferation.  All three compounds – TNP-470, PPI-2458 and CKD-732 – were evaluated pre-clinically and clinically for use in oncology based on their anti-proliferative activity. Two of the three small molecule compounds have also been evaluated pre-clinically for anti-obesity activity.

SynDevRx novel fumagillol-polymer conjugates were designed to provide best-in-class MetAP2 inhibition and improved therapeutic options for the treatment of cancer and metabolic-related diseases.