Pro-sequence assisted folding and disulfide bond formation of human nerve growth factor
作者： Anke Rattenholl , Margherita Ruoppolo , Angela Flagiello , Maria Monti , Floriana Vinci
关键词: Proteolytic enzymes 、 Neurotrophin 、 Nerve growth factor 、 Cystine knot 、 Enhancer 、 Folding (chemistry) 、 Matrix-assisted laser desorption/ionization 、 Mass spectrometry 、 Biochemistry 、 Chemistry
摘要: Nerve growth factor (NGF) is a member of the neurotrophin family. These factors support neuronal survival and differentiation. Neurotrophins are synthesized as pre-pro-proteins. Whereas pre-sequences mediate secretion, function pro-peptides largely unknown. To test role pro-sequence folding enhancer, recombinant human pro-NGF (rh-pro-NGF) was produced in Escherichia coli. The oxidative refolding rh-pro-NGF rh-NGF studied using electrospray mass spectrometry (ESIMS) time-course analysis. This analysis permitted both identification quantification intermediates present during process. disulfide bonds formed at different times processes were characterized by proteolytic digestion followed matrix assisted laser desorption ionization (MALDIMS) Folding yields kinetics significantly enhanced when compared to vitro mature rh-NGF. results suggest that NGF promotes part.
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