Key result
In vitro digestion of ANF analogs showed that rANF5-23-NH2 had a half-life of 0.5 min for initial hydrolysis at the Cys7-Phe8 bond, whereas rANF7-23-NH2 remained intact at this bond (t1/2 = 16 min).
Removal of the first six residues from the N-terminus of ANF analogs may improve stability against endopeptidase-mediated core hydrolysis.
The use of high-performance liquid chromatography and fast atom bombardment mass spectrometry are shown to be an efficient combination for investigating protease-mediated digestion of synthetic analogs of the peptide hormone ANF (atrial natriuretic factor). As examples of the reported methodology, rANF5-23-NH2 and rANF7-23-NH2 were digested with the endopeptidase thermolysin. These truncated analogs were selected to investigate metabolism within the disulfide-linked core of ANF, particularly at the Cys7-Phe8 bond. While this position was the site of initial hydrolysis for rANF5-23-NH2 (t1/2 = 0.5 min), the Cys7-Phe8 bond remained intact for all observed degradation products of rANF7-23-NH2 (t1/2 = 16 min). These findings suggest that improved stability towards endopeptidase-mediated core hydrolysis may be conferred to analogs of ANF by removal of the first six residues from the N-terminus.
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Chen et al. (1989) studied this question. rANF5-23-NH2 and rANF7-23-NH2 was evaluated on protease-mediated digestion (t1/2). In vitro digestion of ANF analogs showed that rANF5-23-NH2 had a half-life of 0.5 min for initial hydrolysis at the Cys7-Phe8 bond, whereas rANF7-23-NH2 remained intact at this bond (t1/2 = 16 min).
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