Letters in Drug Design & Discovery

G. Perry
University of Texas
San Antonio, TX
Email: lddd@benthamscience.org


Protein Interaction Networks in Metallo Proteins and Docking Approaches of Metallic Compounds with TIMP and MMP in Control of MAPK Pathway

Author(s): Kaladhar Svgk Dowluru, Potladurthi Chandra Sai, Padmanabhuni Venkata Nageswara Rao, Amajala Krishna chaitanya, Duddukuri Govinda Rao, Vadlapudi Varahala Rao, Potladurthi Suresh, Erva Rajeswara Reddy, Sudabattula Vijaya kumar, Divyakolu Vinod Kumar, Gajjala Bhaskar Reddy.


Metalloprotein is a basic term for a proteins that contains a metal ion cofactor, have many functions in cells, such as enzymes, transport and storage proteins, and signal transduction proteins. The balance between MMPs and TIMPs are critical in extracellular matrix (ECM) development, morphogenesis, tissue repair and remodeling through MAPK Pathway. Excess of MMPs and TIMPs shows adverse effects, leading to aging diseases such as Alzheimer’s Disease, Cancer, Asthma, Diabetes 2 Mellitus etc. Human Protein Reference Dataset (HPRD) assessed 10 interactions for TIMP1, 5 interactions for TIMP2, 8 interactions for TIMP3 and 2 interactions for TIMP4. The data also assessed 11 interactions for MMP1 and 11 interactions for MMP2. The data from HPRD and Pathwaylinker has also predicted the interaction of Metalloproteins with aging diseases. In the present experimentation, in silico docking models predicted that Iron and Cobalt are activators for TIMPs and MMPs. These metals can serve as an important reactants with good binding affinity for TIMPs and MMPs. Except TIMP1 and TIMP2, all other TIMPs used in present experimentation have good binding affinities with Cyanocobalamin. Hence Cyanocobalamine can be used in treatment of various diseases such as D2M, Cancer, Alzheimer and Parkinson diseases in low dose for longer period, in control of MAPK pathway.

Keywords: MMP, TIMP, Metallic compounds, Protein-protein interactions, Docking, Anti-aging, Bioinformatics, Metalloproteins, ERK1/2, Pulmonary Disease

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Article Details

Year: 2013
Page: [49 - 55]
Pages: 7
DOI: 10.2174/1570180811309010049