The effect of pH on recombinant C-terminal domain of Botulinum Neurotoxin type E (rBoNT/E-HCC) | ||
| Molecular Biology Research Communications | ||
| مقاله 1، دوره 2، شماره 4، اسفند 2013، صفحه 123-132 اصل مقاله (191.78 K) | ||
| نوع مقاله: Original article | ||
| شناسه دیجیتال (DOI): 10.22099/mbrc.2013.1820 | ||
| نویسندگان | ||
| Seyed Jafar Mousavy* 1؛ Mosayeb Rostamian1؛ Firouz Ebrahimi1؛ Mohammad Reza Dayer2 | ||
| 1Department of Biology, Faculty of Basic Sciences, Imam Hussein University, Tehran, Iran. | ||
| 2Department of Biology, Faculty of Science, Shahid Chamran University of Ahvaz, Ahvaz, Iran. | ||
| چکیده | ||
| Recombinant proteins are tending to be the most favorable vaccine-candidates against botulism. Recombinant Carboxy-terminal of botulinum neurotoxin serotype E (rBoNT/E-HCC) has been introduced as an efficient vaccine against botulism type E. In this report, we made an effort to investigate the effect of different pH on protein structure to assess if rBoNT/E-HCC could be used as a vaccine for oral administration. Initially, rBoNT/E-HCC was expressed and purified. Structural changes of rBoNT/E-HCC at several pH conditions were studied by various techniques including circular dichroism (CD), fluorescence, aggregation and UV-Vis spectroscopy. The results showed the more compact and more stable structure for rBoNT/E-HCC at acidic pH, and loosely folded structure at alkaline pH. Our finding as the first step of rBoNT/E-HCC evaluation, hopefully introduce it as a suitable vaccine candidate for oral administration. | ||
| کلیدواژهها | ||
| Botulinum Neurotoxin Type E؛ pH؛ Fluorescence؛ Circular Dichroism؛ Aggregation | ||
| مراجع | ||
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