publication . Article . 2017

Development of surface-engineered PLGA nanoparticulate-delivery system of Tet-1-conjugated nattokinase enzyme for inhibition of Aβ 40 plaques in Alzheimer’s disease

Bhatt, Prakash Chandra; Verma, Amita; Al-Abbasi, Fahad A; Anwar, Firoz; Kumar, Vikas; Panda, Bibhu Prasad;
Open Access
  • Published: 01 Dec 2017 Journal: International Journal of Nanomedicine, volume Volume 12, pages 8,749-8,768 (eissn: 1178-2013, Copyright policy)
  • Publisher: Dove Medical Press Ltd.
Abstract
According to the World Health Organization, globally there are around 18 million patients suffering from Alzheimer’s disease (AD), and this number is expected to double by 2025. The pathophysiology of AD includes selective deposition of Aβ peptide in the mitochondria of cells, which inhibits uptake of glucose by neurons and key enzyme functions. Current drug treatments for AD are unable to rectify the underlying pathology of the disease; they only provide short-term symptomatic relief, so there is a need for the development of newer treatment regimes. The antiamyloid activity, antifibrinolytic activity, and antithrombotic activity of nattokinase holds potential ...
Subjects
free text keywords: Conjugated system, Delivery system, Enzyme, chemistry.chemical_classification, chemistry, PLGA, chemistry.chemical_compound, Nattokinase, Biochemistry, Materials science, Original Research, Aβ40, Alzheimer’s disease, surface modification, TEM, Tet1 peptide
Related Organizations
39 references, page 1 of 3

2013 Alzheimer’s disease facts and figures. Alzheimers Dement. 2013; 9 (2): 208-245 [PubMed]

Cummings, JL. Alzheimer’s disease. N Engl J Med. 2004; 351: 56-67 [PubMed]

Mucke, L. Alzheimer’s disease. Nature. 2009; 461: 895-897 [PubMed]

McDonald, B, Esiri, MM, Morris, J. Aluminium and Alzheimer’s disease. Age Ageing. 1993; 22: 392-393 [PubMed]

Vemuri, P, Lesnick, TG, Przybelski, SA. Age, Vascular Health, and Alzheimer’s disease Biomarkers in an Elderly Sample. Ann Neurol. 2017 [OpenAIRE]

Lu, JX, Qiang, W, Yau, WM, Schwieters, CD, Meredith, SC, Tycko, R. Molecular structure of β-amyloid fibrils in Alzheimer’s disease brain tissue. Cell. 2013; 154: 1257-1268 [OpenAIRE] [PubMed]

Fändrich, M. On the structural definition of amyloid fibrils and other polypeptide aggregates. Cell Mol Life Sci. 2007; 64: 2066-2078 [OpenAIRE] [PubMed]

Serpell, LC. Alzheimer’s amyloid fibrils: structure and assembly. Biochim Biophys Acta. 2000; 1502: 16-30 [OpenAIRE] [PubMed]

Liang, X, Zhang, L, Zhong, J, Huan, L. Secretory expression of a heterologous nattokinase in Lactococcus lactis. Appl Microbiol Biotechnol. 2007; 75: 95-101 [PubMed]

Dubey, R, Kumar, J, Agrawala, D, Char, T, Pusp, P. Isolation, production, purification, assay and characterization of fibrinolytic enzymes (nattokinase, streptokinase and urokinase) from bacterial sources. Afr J Biotechnol. 2011; 10: 1408-1420

Cho, YH, Song, JY, Kim, KM. Production of nattokinase by batch and fed-batch culture of Bacillus subtilis. N Biotechnol. 2010; 27: 341-346 [PubMed]

Hsu, RL, Lee, KT, Wang, JH, Lee, LY, Chen, RP. Amyloid-degrading ability of nattokinase from Bacillus subtilis natto. J Agric Food Chem. 2009; 57: 503-508 [PubMed]

Wang, C, Du, M, Zheng, D, Kong, F, Zu, G, Feng, Y. Purification and characterization of nattokinase from Bacillus subtilis natto B-12. J Agric Food Chem. 2009; 57: 9722-9729 [PubMed]

Akiyama, H, Barger, S, Barnum, S. Inflammation and Alzheimer’s disease. Neurobiol Aging. 2000; 21: 383-421 [OpenAIRE] [PubMed]

Manish, M, Bhatnagar, R, Singh, S. Preparation and characterization of PLGA encapsulated protective antigen domain 4 nanoformulation. Methods Mol Biol. 2016; 1404: 669-681 [PubMed]

39 references, page 1 of 3
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publication . Article . 2017

Development of surface-engineered PLGA nanoparticulate-delivery system of Tet-1-conjugated nattokinase enzyme for inhibition of Aβ 40 plaques in Alzheimer’s disease

Bhatt, Prakash Chandra; Verma, Amita; Al-Abbasi, Fahad A; Anwar, Firoz; Kumar, Vikas; Panda, Bibhu Prasad;