Abstract
In this paper, we describe a rapid procedure to characterise the products generated in the presence of mercuric salts following removal of the acetamidomethyl (Acm)-protecting group from cysteine residues of synthetic polypeptides prepared by solid-phase peptide synthesis (SPPS) methods. In particular, electrospray ionisation mass spectrometry (ESI-MS) procedures have been employed to characterise the mercuro-polypeptide products related to the ribosomal L36 protein isolated from the bacterium Thermus thermophilus. The results demonstrate that very stable mercuro-polypeptide complexes can form under standard conditions of deprotection involving Hg 2+ salts in the presence of a reductant such as β-mercaptoethanol. Metal ion exchange effects involving other divalent metal ions, such as Co 2+ or Zn 2+, can also be monitored by similar procedures, thus permitting the relative affinity and selectivity for metal ion–polypeptide interactions to be qualitatively assessed. Since the Thermus thermophilus ribosomal L36 protein contains a putative zinc finger binding CCCH motif, these procedures enable the formation of metal-ion complexes of synthetic polypeptides related to this structural motif to be directly examined.
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