Two enzymes act upon the nascent polypeptide chain to realize this modification. How these enzymes function in concert and interact with the translating polypeptide chain is one question we seek to answer. Through increased understanding of this aspect of protein myristylation, we plan to identify targets for drug inhibition. Our lab integrates organic synthesis, biochemistry, and molecular biology as a continuum into the discipline of medicinal chemistry. We use organic synthesis to explore the chemico-enzymatic potentials of the selected enzymes, prepare peptide substrates for in vitro assays, and develop target peptidomimetics.
Biochemistry provides a means to purify and characterize the enzymes.
Molecular biology allows us to obtain a reliable source of enzymes for different biological assays and to test hypotheses using mutated enzymes. The variety of techniques in biology and chemistry that we use to advantage in our lab are reflective of the current state of technology in academia and the biotechnology and pharmaceutical industries. Our perspective is one of medicinal chemistry, where models of intermolecular interactions or compounds recognized must yield sufficient information to be useful for drug design and discovery. Peseckis, S.M., I. Deichaite and M.D. Resh. A New Role for Long Chain Fatty Acid Acylation of Proteins.