Abstract:
:Botulinum toxin type A can temporarily inhibit muscle contraction. Currently, physicians administer this toxin as a bio-drug in treatment of some muscle contraction disorders. TAT-BoNT/A(1-448) is a functional recombinant protein derived from botulinum toxin light chain. Unlike the full length botulinum toxin, TAT-BoNT/A(1-448) is a self-permeable molecule which can pass through bio-surfaces so can be used as a topical therapeutic agent without injection. To maintain the functionality of TAT-BoNT/A(1-448), it is necessary to restore its normal folding upon expression and purification. In this study, we have investigated and optimized expression conditions for this novel recombinant protein. Under denaturing condition (1 mM IPTG, at 37°C), the chimeric protein was produced as inclusion body and required to be purified using denaturing agents (e.g. urea). Yet, lower incubation temperature (18°C) and less IPTG concentration (0.5 mM) induce a protein under native condition. In such condition, about 60% of the chimeric protein was expressed in soluble form.
journal_name
Bioengineeredjournal_title
Bioengineeredauthors
Saffarian P,Peerayeh SN,Amani J,Ebrahimi F,Sedighianrad H,Halabian R,Imani Fooladi AAdoi
10.1080/21655979.2016.1201252subject
Has Abstractpub_date
2016-11-01 00:00:00pages
478-483issue
6eissn
2165-5979issn
2165-5987journal_volume
7pub_type
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