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首页> 外文期刊>Journal of Molecular Biology >Pro-sequence assisted folding and disulfide bond formation of human nervegrowth factor
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Pro-sequence assisted folding and disulfide bond formation of human nervegrowth factor

机译：前序列辅助人神经生长因子的折叠和二硫键形成

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摘要

Nerve growth factor (NGF) is a member of the neurotrophin family. These growth factors support neuronal survival and differentiation. Neurotrophins are synthesized as pre-pro-proteins. Whereas the pre-sequences mediate secretion, the function of the pro-peptides is largely unknown. To test the role of the pro-sequence as a folding enhancer, recombinant human pro-NGF (rh-pro-NGF) was produced in Escherichia coli. The oxidative refolding of rh-pro-NGF and rh-NGF was studied using electrospray mass spectrometry (ESIMS) time-course analysis. This analysis permitted both the identification and quantification of intermediates present during the process. The disulfide bonds formed at different times of the refolding processes were characterized by proteolytic digestion followed by matrix assisted laser desorption ionization mass spectrometry (MALDIMS) analysis. Folding yields and kinetics of rh-pro-NGF were significantly enhanced when compared to the in vitro refolding of mature rh-NGF. These results suggest that the pro-sequence of NGF promotes folding of the mature part.
机译：神经生长因子（NGF）是神经营养蛋白家族的成员。这些生长因子支持神经元存活和分化。神经营养蛋白被合成为前原蛋白。尽管前序列介导分泌，但是前肽的功能在很大程度上是未知的。为了测试前序列作为折叠增强子的作用，在大肠杆菌中生产了重组人pro-NGF（rh-pro-NGF）。使用电喷雾质谱（ESIMS）时程分析研究了rh-pro-NGF和rh-NGF的氧化重折叠。该分析允许对过程中存在的中间体进行鉴定和定量。通过蛋白水解消化，然后通过基质辅助激光解吸电离质谱（MALDIMS）分析来表征在重折叠过程的不同时间形成的二硫键。与成熟的rh-NGF的体外重折叠相比，rh-pro-NGF的折叠产量和动力学得到显着提高。这些结果表明NGF的前序列促进成熟部分的折叠。

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