Attempts Towards the Bucky-amino Acid Acylation of the Phospho-cytidine-phospho-adenosine (pdCpA) Subunit

T. Amanda Strom, Andrew R Barron


Abstract: The irreversible adsorption of fullerene (C60) substituted amino acids to the hydrophobic resin bead surface during solid phase peptide synthesis leads to low yields. Due to challenge in preparing sufficient C60-substituted phenylalanine (Bucky amino acid, Baa) an alternative route to fullerene-substituted peptides was investigated. The first step is the synthesis of the amino acylated phospho-cytidine-phospho-adenosine subunit (pdCpA-Baa) prior to enzymatically ligating it to a truncated tRNA. However, despite the successful synthesis of the cyanomethyl ester, Fmoc-Baa-OCH2CN (1) no reaction is observed between the hydrophilic pdCpA and hydrophobic Baa even in the presence of cationic surfactant or in DMF solution. As an alternative method a N,N’-diisopropylcarbodiimide coupling route was investigated, which despite the presence of an appropriate m/z in the MALDI-MS did not lead to an isolable product. The successful coupling of a hydrophobic perfluorophenyl ester (Fmoc-Gly-OPfp) to pdCpA suggest that it is steric bulk rather than miscibility that precludes the Baa coupling.


Acylation, Bucky amino acid, C60, phospho-cytidine-phospho-adenosine, fullerene

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