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Nazem H, Mohsenifar A, Majdi S. Chitosan-myristate nanogel as an artificial chaperone protects neuroserpin from misfolding. Adv Biomed Res. 2016;5:170doi: 10.4103/2277-9175.190942.
Nazem, H., Mohsenifar, A., & Majdi, S. (2016). Chitosan-myristate nanogel as an artificial chaperone protects neuroserpin from misfolding. Advanced biomedical research, 5170. https://doi.org/10.4103/2277-9175.190942
Nazem, Habib, et al. "Chitosan-myristate nanogel as an artificial chaperone protects neuroserpin from misfolding." Advanced biomedical research vol. 5 (2016): 170. doi: https://doi.org/10.4103/2277-9175.190942
Nazem H, Mohsenifar A, Majdi S. Chitosan-myristate nanogel as an artificial chaperone protects neuroserpin from misfolding. Adv Biomed Res. 2016 Oct 26;5:170. doi: 10.4103/2277-9175.190942. eCollection 2016. PMID: 27995109; PMCID: PMC5137230.
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Adv Biomed Res. 2016 Oct 26;5:170. doi: 10.4103/2277-9175.190942. eCollection 2016.

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

Advanced biomedical research

Habib Nazem, Afshin Mohsenifar, Sahar Majdi

Affiliations

  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.

PMID: 27995109 PMCID: PMC5137230 DOI: 10.4103/2277-9175.190942

Abstract

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

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.

Keywords: Cyclodextrin; misfolding; nanogel (chitosan-myristic acid); neuroserpin

Conflict of interest statement

Conflicts of Interest: None declared.

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