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Publications
 
 
 Comparative Modeling of Human Siglec-8 Membrane Protein  

Shagunbansali1, Sreenivas.enaganti1, Saritha.devaraju1, Harikrishna.N1, Vijay.H1, Vamsee.K1, 
Laxman.R1, Ramesh.S1


Corresponding author: Sreenivas Enaganti 
Asteracelabs Pvt. ltd, Nallakunta, Windsorplaza,208 IInd floor,Hyderabad,500024 , India 
E-mail : sreenivas.bioinfo@gmail.com
International Journal of Advances in Pharmaceutical Sciences (2010) 410-414

Abstract
Many cells are present in our body and play different role. But some cells only involved in the inflammatory process.Siglec-8 is a member of the CD33 Sialicacid binding Ig-like lectins membrane proteins that constitute a distinct subset of the Ig super- family and are characterized by their sequence similarities and abilities to bind sialic acids in glycoproteins and glycolipids . Siglec-8 found predominantly on human eosinophils. Siglec is also present in the airway passages.so they involved in the asthma. Thus, it is a potential chemotherapeutic target for asthma treatment. Structure of this enzyme in Homosapiens has not yet been elucidated. We used the structural template of N-Terminal Domains of Native Siglec-5 from Homosapiens for modeling of siglec-8 structure by using Modeller.Thus we analyses and propose the usefulness
 
Keywords : Asthma; Siglec-8; Homo sapiens; Modeler; Homology Modeling
 
 
 
 Structure-Guided Modeling of Arachidonate 15-Lipoxygenase B from H.Sapiens 

Deepika.G*,Nagamani.C,JayasreeYadav.V,Suneetha.B,Srikanth.Anukula Sreenivas.Enaganti*


Corresponding author: Sreenivas Enaganti
Asteracelabs Pvt. ltd, Nallakunta, Windsorplaza,208 IInd floor,Hyderabad,500024 , India
E-mail : sreenivas.bioinfo@gmail.com
International Journal of Advances in Pharmaceutical Sciences (In Press: (AR-AP-2010-3-242))

Abstract
15-Lipoxygenase is a highly regulated lipid–peroxidating enzyme whose expression and arachidonic acid metabolites are implicated in several important inflammatory conditions. In this scenario, we had performed modeling of arachidonate 15-lipoxygenase B, an enzyme involved in Leucotriene biosynthesis. We wish to contribute to the structural knowledge of arachidonate 15-lipoxygenase B from Homo sapiens. In this pursuit, 3D model of arachidonate 15-lipoxygenase B has been established by homology modeling, choosing the Revised structure of rabbit reticulocyte 15S-lipoxygenase with PDB code 2P0M and Crystal structure of Delta 413-417:GS LOX with PDB code 3FG1 as templates by the MODELLAR9v7 program. The model was extensively validated using protein structure checking tools: PROCHECK, WHAT IF and ProSA. The developed model was analyzed through domain analysis for the presence of various domains. Secondary structural conformations for the developed model were determined using PDBSUM. This study suggests use of this 3D structure as a target of new drugs that act on multidrug resistant varieties of Homo sapiens.

Keywords : Arachidonate 15-lipoxygenase B, Modeller9V7
 
 
 
 A NAT Protein Model as Tuerbculosis Target for screening Alkaloids by using In silico Approaches 

Sreenivas Enaganti1*, Saumita Acharyya Nandi1, Sivaprasad Mudili2, Dr.Surekharani,
Maddukuri1, B.Rajasekhara Reddy1, Shirisha Sugavasi3, Rahul.B1, Arun jyothi.B4


Corresponding author: Sreenivas Enaganti
Asteracelabs Pvt. ltd, Nallakunta, Windsorplaza,208 IInd floor,Hyderabad,500024 , India
E-mail : sreenivas.bioinfo@gmail.com
JOURNAL OF PHARMACY RESEARCH (In Press: JPR_11_909)

Abstract
Mycolic acids represent a major component of the unique cell wall of Mycobacteria.
Mycolic acid biosynthesis is inhibited by isoniazid, a key frontline anti-tubercular drug that is inactivated by mycobacterial arylamine N-acetyltransferase (NAT). ). It was well established thatNAT is critical to normal mycolic acid synthesis and hence other derivative cell wall components and represents a novel drug target for antituberculosis therapy. An increasing incidence of deaths due to tuberculosis and the known drawbacks of the current existing drugs including the emergence of multi drug-resistant strains have led to a renewed interest in the discovery of new anti-tubercular agents with novel modes of actions. The recent researches focused on natural products have shown a useful way to obtain a potentially rich source of drug candidates,where alkaloids have been found more effective. Homology model of NAT has been constructed using the X-ray structures (Protein Data Bank (PDB) ID: 2VFB & 1GX3) as templates by using MODELLER 9v7 software. The resulting model assessed by PROCHECK, ProSA and RMSD that showed the final refined model is reliable, has 0.17Å as RMSD and has (-7.37) as Z-scores.Further Docking studies carried out with 25 Alkaloid compounds by using Molegro Virtual Docker. Out of 25 docked complexes we got four best alkaloid compounds. The model could prove useful in further functional characterization of this protein.

Keywords : Homology modeling, Docking, Mycobacterium tuberculosis, N-acetyltransferase (NAT), Alkaloids.
 
 
 
 Structural analysis and binding properties of modeled surfactant protein-A

Sivaprasad Mudili1, Surekharani Maddukuri2, Salma Sulthana3,A.Pradeep Kumar2,Ramesh.S2,Saumita AcharyyaNandi2 B.Rajasekhara Reddy 4,Deepika.G2,Sreenivas.Enaganti2


MANUSCRIPT NUMBER: IJABB-04 International Journal of Advanced Biotechnology and Bioinformatics (IJABB).Corresponding author: Sreenivas Enaganti
Asteracelabs Pvt. ltd, Nallakunta, Windsorplaza,208 IInd floor,Hyderabad,500024 , India
E-mail : sreenivas.bioinfo@gmail.com
1Department Hyderabad, 500 007, India 2Asterace Labs, Windsorplaza 208, Nallakunta, Hyderabad, 500024, India of Ocular biochemistry, National Institute of Nutrition, Jamai Osmania,
 
Surfactant protein A (SP-A) constitutes an important part of the innate immune defense in the lung. The three-dimensional (3D) model of the human surfactant protein-A (hSP-A) has been constructed based on the crystal structure of Rat norvegicus 1R13 protein (Protein Data Bank ID: 1R13) using MODELLER 9.9 software. Under the process of homology modeling 2 models were generated, and the model having the lowest modeler objective function value was chosen for further assessment. The generated model assessed and validated using PROCHECK, ProSA and RMSD that showed the final refined model is reliable, with 0.59 Å as RMSD and has -6.11 as Z-scores. Furthermore, with the generated model, we carried out binding studies with simple carbohydrate and lipid ligands using the Molegro Virtual Docker. Docking studies with these ligands into the active site of hSP-A indicate that maltose and Dipalmitoylphosphatidylcholine are more preferred ligands than others, with the binding scores of -93.8850 & -103.774 respectively. Docking studies revealed that Arg58, Arg63, Glu144, Lys34, Ser 98, Asp99, Glu33 and Ile59 of receptor are important determinant residues as they have strong hydrogen bonding contacts with both carbohydrate and lipid 1compounds. This is in good agreement with the experimental results. Results of the current study will provide a deep insight about the structure and function of Surfactant Protein-A and how these interactions influence the binding and neutralization of pulmonary pathogens.

Keywords : Surfactant Protein-A (SPA), Homology Modeling, Docking, Rattus norvegicus,Lipids, Carbohydrates.
 
 
 
 Insilico evaluation of Anti-inflammatory activity of Natural compounds against Modeled COX2  

MANUSCRIPT NUMBER (JPR_12_395 Journal of Pharmacy Research )

Sruthi.H.V1, Megha Kanniganti1 ,Salma Sulthana2, Nanda Kumar yellapu3, A.Pradeep Kumar1, Rajasekhara Reddy4,N.V.Naidu5,Sravani Saragandla1, Saumita AcharyyaNandi1,Sreenivas.Enaganti 1*

Corresponding author: Sreenivas Enaganti
Asteracelabs Pvt. ltd, Nallakunta, Windsorplaza,208 IInd floor,Hyderabad,500024 , India
E-mail : sreenivas.bioinfo@gmail.com
1Department Hyderabad, 500 007, India 2Asterace Labs, Windsorplaza 208, Nallakunta, Hyderabad, 500024, India of Ocular biochemistry, National Institute of Nutrition, Jamai Osmania,

Prostaglandins, a subset of the eicosanoid family of signaling molecules, are chemical messengers of inflammation and pain. Eicosanoids, the oxygenated metabolites of arachidonic acid formed via the eicosanoid pathway play a dominant role in inflammation. Among these prostaglandins, specifically from prostaglandin synthase 2 or Cyclooxygenase -2 formed via COX-2 pathway are known to mediate inflammation. COX 2 enzymatic activities is the major pharmacological target of widely used Nonsteroidal anti-inflammatory drugs (NSAIDs). Blocking this enzyme impedes the production of the chemical messengers (prostaglandins) that cause pain and swelling from inflammation. The potential mechanisms for the chemo preventive effect of non steroidal anti-inflammatory drugs may occur through specific inhibition of Cox 2 enzymes. But the drawbacks of current existing NSAID drugs and the emergence of gastrointestinal side effects have led to a renewed interest in the discovery of new anti- inflammation agents with novel mode of actions. The recent research is focused on the use of Insilco methods to study the binding activity of some natural compounds with anti- inflammatory properties to COX-2. The natural compounds involved in the present work were all natural products possessing anti-inflammatory properties. Homology model of COX2 has been constructed using X-ray structure (PDB ID: 1PXX) as template by using MODELLER 9.9 software. Docking studies were carried out using GOLD software to determine whether these natural compounds can act as COX-2 inhibitors. The results indicated that out of 32, four natural compounds could be potentially rich source of drug candidates & may act as preferential inhibitors of COX-2.

Keywords : Prostaglandins, Eicosanoids, NSAIDs, Cyclooxygenase -2, GOLD.