Crystal Structure and Interaction of Phycocyanin with β-Secretase: A Putative Therapy for Alzheimer's Disease

ISSN: 1996-3181 (Online)
ISSN: 1871-5273 (Print)


Volume 13, 10 Issues, 2014


Download PDF Flyer




CNS & Neurological Disorders - Drug Targets

Formerly: Current Drug Targets - CNS & Neurological Disorders

Aims & ScopeAbstracted/Indexed in

Ranking and Category:
  • 51st of 261 in Pharmacology & Pharmacy
  • 78th of 252 in Neurosciences

Submit Abstracts Online Submit Manuscripts Online

Editor-in-Chief:
Stephen D. Skaper
Department of Pharmaceutical and Pharmacological Sciences
University of Padova
Padova
Italy


View Full Editorial Board

Subscribe Purchase Articles Order Reprints

Current: 3.769
5 - Year: 3.923

Crystal Structure and Interaction of Phycocyanin with β-Secretase: A Putative Therapy for Alzheimer's Disease

Author(s): Niraj Kumar Singh, Syed S. Hasan, Jitendra Kumar, Isha Raj, Amrin A. Pathan, Asha Parmar, Shazi Shakil, Samudrala Gourinath and Datta Madamwar

Affiliation: (Datta Madamwar) BRD School of Biosciences, Sardar Patel Maidan, Vadtal Road, Satellite Campus, Post Box No. 39, Sardar Patel University, Vallabh Vidyanagar-388 120, Gujarat, India.

Abstract

Alzheimer’s disease (AD) represents a neurological disorder, which is caused by enzymatic degradation of an amyloid precursor protein into short peptide fragments that undergo association to form insoluble plaques. Preliminary studies suggest that cyanobacterial extracts, especially the light-harvesting protein phycocyanin, may provide a means to control the progression of the disease. However, the molecular mechanism of disease control remains elusive. In the present study, intact hexameric phycocyanin was isolated and crystallized from the cyanobacterium Leptolyngbya sp. N62DM, and the structure was solved to a resolution of 2.6 A. Molecular docking studies show that the phycocyanin αβ- dimer interacts with the enzyme β-secretase, which catalyzes the proteolysis of the amyloid precursor protein to form plaques. The molecular docking studies suggest that the interaction between phycocyanin and β-secretase is energetically more favorable than previously reported inhibitor-β-secretase interactions. Transgenic Caenorhabditis elegans worms, with a genotype to serve as an AD-model, were significantly protected by phycocyanin. Therefore, the present study provides a novel structure-based molecular mechanism of phycocyanin-mediated therapy against AD.

Keywords: Alzheimer's, amyloid precursor protein, β-secretase, cyanobacteria, phycocyanin.

Purchase Online Rights and Permissions

Article Details

Volume: 13
Issue Number: 4
First Page: 691
Last Page: 698
Page Count: 8
DOI: 10.2174/1871527313666140228114456
Advertisement

Related Journals




Webmaster Contact: urooj@benthamscience.org Copyright © 2014 Bentham Science