Synthesis of Adenosine 5'- (Aminoalkyl phosphonates and phosphinates) Analogues of Aminoacyl Adenylates

Translation of the genetic code and protein synthesis from amino acids takes place in the ribosome’s where tRNAs act as key intermediates. Correct translation of genetic information into the specific amino acids is dependent on aminoacyl-tRNA ́s. The synthesis of these is catalyzed by aminoacyl-tRNA synthetase. The aminoacylation reaction, the so-called charging of tRNA is carried out in two steps. The first step is the formation of aminoacyl adenylates (I) by a specific reaction involving amino acids, adenosine triphosphate, and an aminoacyl-tRNA synthetase. The amino acids are thus activated, and subsequently transferred to their corresponding tRNA through a highly specific reaction catalyzed by the same enzymes. It is known that Aminoalkyl adenylates (II) are inhibitors of these enzymes and are thought to occupy the binding sites for the aminoacyl adenylates. A drawback is that Aminoalkyl adenylates are sensitive to biological degradation. Adenosine 5’-(aminoalkyl phosphonates or phosphinates) (III) can prove valuable as stable inhibitors of amino acid activation and as substrates for studies of enzyme – substrate interaction.