The dinucleotide 3',5'-cylic diguanylic acid (c-di-GMP) is believed to act as a second messenger molecule in signal transduction pathways regulating biofilm formation and surface attachment in Vibrio cholerae and other bacteria. Two protein domains have been identified that are capable of catalyzing the biosynthesis and degredation of c-di-GMP and are believed to act in controlling intracellular c-di-GMP concentrations. Some proteins containing a GGDEF (short for the peptide sequence: glycine- glycine- aspartic acid- glutamic acid- phenylalanine) domain can exhibit diguanylate cyclase activity, being able to catalyze the synthesis of c-di-GMP from two GTP (guanosine triphosphate) molecules, and some proteins containing an EAL (short for the peptide sequence: glutamic acid- alanine- leucine) domain can act as phophodiesterases, capable of catalyzing the degradation of c-di-GMP to a linear pGpG molecule. The GGDEF and EAL domains are abundant among V. cholerae proteins and many are linked to sensory or signaling domains. Though some of these proteins have been characterized functionally, the signals they process remain largely unknown. In order to further characterize the function of EAL and GGDEF domain proteins and study the signal transduction pathways they are a part of, a supply of pure standard c-di-GMP is critical. Presented here is the progress towards the synthesis of c-di-GMP. The synthetic approach taken is adapted from the reported method by Hyodo et al, which uses readily available protecting groups for the coupling and cyclization of two protected guanosine nucleotides.