Users Online: 867
Home Print this page Email this page
Home About us Editorial board Search Browse articles Submit article Ahead of Print Instructions Subscribe Contacts Login 
Year : 2016  |  Volume : 5  |  Issue : 1  |  Page : 170

Chitosan-myristate nanogel as an artificial chaperone protects neuroserpin from misfolding

1 Department of Biochemistry, Payam Noor University, Tehran, Iran
2 Department of Clinical Biochemistry, Tarbiat Modares University, Tehran, Iran
3 Young Researchers and Elite Club, Tehran Medical Sciences Branch, Islamic Azad University, Tehran, Iran

Correspondence Address:
Dr. Afshin Mohsenifar
Department of Clinical Biochemistry, Tarbiat Modares University, Tehran
Login to access the Email id

Source of Support: Payame Noor University, I.R. of IRAN, Conflict of Interest: None

DOI: 10.4103/2277-9175.190942

Rights and Permissions

Background: Molecular chaperon-like activity for protein refolding was studied using nanogel chitosan-myristic acid (CMA) and the protein neuroserpin (NS), a member of the serine proteinase inhibitor superfamily (serpin). Materials and Methods: Recombinant his-tag fusion NS was expressed in Escherichia coli. For confirmation of refolding of the purified NS, structural analysis was performed by circular dichroism and spectrofluorometric along with its inhibitory activity, which was assayed by single-chain tissue plasminogen activator. For evaluating NS aggregation during preparation, the samples were separated on a 7.5% (w/v) nondenaturing polyacrylamide gel electrophoresis. MA and chitosan covalently join together by the formation of amide linkages through the 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide-mediated reaction. The morphology and size of the prepared CM nanogel were characterized by transmission electron microscopy and scanning electron microscopy. Results: Heating at different temperatures (25°C, 37°C, 45°C, 65°C, 80°C) results in a further rise in β-structures accompanied by a fall of helices and no significant change in random coils. Structural changes in NS in the presence of CMA nanogel were less than that in the absence of CMA nanogel. Mater nanogel effectively prevented aggregation of NS during temperature induced protein refolding by the addition of cyclodextrins. The nanogel activity resembled the host-guest chaperon activity. Conclusion: These conditions, called conformational disorders, include Alzheimer's, Parkinson's, Huntington's disease, the transmissible spongiform encephalopathies, prion diseases, and dementia. Nanogels can be useful in recovery of the structural normality of proteins in these diseases.

Print this article     Email this article
 Next article
 Previous article
 Table of Contents

 Similar in PUBMED
   Search Pubmed for
   Search in Google Scholar for
 Related articles
 Citation Manager
 Access Statistics
 Reader Comments
 Email Alert *
 Add to My List *
 * Requires registration (Free)

 Article Access Statistics
    PDF Downloaded235    
    Comments [Add]    
    Cited by others 1    

Recommend this journal