The protein IF1 is a natural inhibitor of the mitochondrial FoF1-ATPase. Many investigators have been propted to identify the shortest segment of IF1, retaining its native activity, for use in biomedical applications. Here, the activity of the synthetic peptides IF1-(42-58) and IF1-(22-46) is correlated to their structure and conformational plasticity determined by CD and (1H)-NMR spectroscopy. Among all the IF1 segment tested, IF1-(42- 58) exerts the most potent, pH and temperature dependent activity on the FoF1 complex. The results suggest that, due to its flexible structure, it can fold in helical and/or b-spiral arrangements tha fovor the binding to the FoF1 complex, where tha native IF1 binds. IF1-(22-46), instead, as it adopts a rigid a-elical conformation, it inhibits ATP hydrolysis only in the soluble F1 mojety.
Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor protein, IF1
2002
Abstract
The protein IF1 is a natural inhibitor of the mitochondrial FoF1-ATPase. Many investigators have been propted to identify the shortest segment of IF1, retaining its native activity, for use in biomedical applications. Here, the activity of the synthetic peptides IF1-(42-58) and IF1-(22-46) is correlated to their structure and conformational plasticity determined by CD and (1H)-NMR spectroscopy. Among all the IF1 segment tested, IF1-(42- 58) exerts the most potent, pH and temperature dependent activity on the FoF1 complex. The results suggest that, due to its flexible structure, it can fold in helical and/or b-spiral arrangements tha fovor the binding to the FoF1 complex, where tha native IF1 binds. IF1-(22-46), instead, as it adopts a rigid a-elical conformation, it inhibits ATP hydrolysis only in the soluble F1 mojety.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
