The technique of electrospray ionisation mass spectrometry has been used to study the hydrogen/deuterium exchange of bisMSH-DTPA, a derivative of α-melanocyte stimulating hormone (MSH) in which two complete MSH peptide chains are covalently bound to a single molecule of diethylenetriamine pentaacetic acid (DTPA). The results show different levels of exchange between the metal-chelated and the unchelated peptide. We suggest that the unchelated peptide is able to form a hydrogen-bonded structure between the carboxyl groups of DTPA and the amino nitrogen of the N'-terminal serine of MSH.
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