COMPUTER-ASSISTED DRUG DESIGN OF DONEPEZIL ANALOGUES FOR ALZHEIMER’S DISEASE

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COMPUTER-ASSISTED DRUG DESIGN OF DONEPEZIL ANALOGUES FOR ALZHEIMER’S DISEASE Sai Lakshmi.Palla*1, N.Dugnath*2, Manoj Kumar Mahto*3 *1,2,3 N.

Duganath, Department of Pharmaceutical Chemistry, Oil Technological Research Institute, Jawaharlal Nehru Technological University, Anantapur, Andhra Pradesh, India515001.

ABSTRACT Alzheimer's disease is a progressive disorder that causes brain cells to degenerate and die. Alzheimer’s disease is characterized by loss of neurons and synapses in the cerebral cortex and certain sub cortical regions. Alzheimer's disease is the most common cause of dementia a continuous decline in thinking, behavioral and social skills that disrupts a person's ability to function independently. Donepezil inhibit the acetylcholinesterase which degrades the acetylcholine transmitter. Computer Assisted Drug designing is used for the introduction of new therapeutic analogues of Donepezil. Energy minimization for analogues is done by using hyperchem software. Docking of the protein-ligand complex was done by using GOLD software. Present study includes new lead identification for Alzheimer’s disease, inhibiting the function of Acetyl cholinesterase protein, molecular docking studies. Binding affinity calculations by using molecular docking studies including computer aided drug design followed by molecular mechanics based binding affinity calculations. Keywords: Donepezil, Acetylcholinesterase, Binding affinity, Molecular docking, Molecular mechanics.

I.

INTRODUCTION

Bioinformatics is a management information system for molecular biology. Applications of Bioinformatics involve sequence analysis, molecular evolution, genome mapping database query tools and comparison, gene identification, structure prediction, drug designing and drug target identification. Computerassisted drug design (CADD), also called computer-assisted molecular design (CAMD) and represents more recent applications of computers as tools in the drug design process. In most current applications of CADD, attempts are made to find a ligand (the putative drug) that will interact favorably with a receptor that represents the target site. Binding of Ligand to the receptor may include hydrophobic, electrostatic, and hydrogen-bonding interactions. Ligand based drug design is applicable when the structure of the receptor site is unknown, but when a series of compounds have been identified that exert the activity of interest. Receptor based drug design1 incorporates several molecular modeling techniques, one of which is docking. Docking allows scoring based on force fields, which include both Vander Waals and electrostatic interactions. These results illustrate the potential for docking programs to search objectively for ligand than are complementary to receptor sites, thereby assisting researchers in identifying potential drugs than may be considerably different from existing drugs. The term molecular mechanics refer to the use of Newtonian mechanics to model molecular systems. Molecular mechanics have properties like each atom is stimulated as a single particle, each particle is assigned a radius, polarizability and constant net charge. MM+ is designed to reproduce the equilibrium covalent geometry of molecules as precisely as possible. AMBER is a family of force fields for molecular dynamics. The standard AMBER force field is parameterized to small organic constituents of proteins and nucleic acids. Energy minimization2 methods can precisely locate minimum energy conformations by mathematically “homing in” on the energy function minima.

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Fig.-1: Hypothetical energy surface The goal of energy minimization is to find a route from an initial conformation to the nearest minimum energy conformation using the smallest number of calculations possible. Molecular dynamics3 is carried out to anneal the system to obtain a lower energy minimum. They calculate the future positions and velocities of atoms based upon their current values. Protein-ligand docking4 is done by modelling the interaction between protein and ligand, if the geometry of the pair is complementary and involves favorable biochemical interactions, the ligand will potentially bind the protein invitro or in vivo. The QSAR equation is a linear model, which relates variations in biological activity to variations in the values of computed properties for a series of molecules. Alzheimer's disease (AD) 6 is a brain disease that slowly destroys memory and thinking skills and, eventually, the ability to carry out the simplest tasks. Dementia is generally defined as the ‘loss of intellectual abilities (medically called cognitive function) like loss of thinking, remembering, and reasoning skills that interferes with a person's daily life and activities.

Fig.-2: Healthy brain and Alzheimer’s advanced Two pathological characteristics are observed in AD patients at autopsy: extracellular plaques and intracellular tangles in the hippocampus, cerebral cortex, and other areas of the brain essential for cognitive function.5 the key event leading to AD appears to be the formation of a peptide known as amyloidal beta which clusters into amyloidal plaques on the blood vessels and on the outside surface of neurons of the brain which ultimately leads to the killing of neurons.

Fig.-3: Amyloidal plaques www.irjmets.com

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Currently there are more than 100 clinical trials being conducted in Alzheimer’s and dementia. The government requires that all new medicines undergo rigorous testing in the laboratory, first in animals and then in human volunteers, before they can be prescribed by doctor or sold in pharmacies. Once the required clinical trials are completed, companies submit an application to the FDA, the government agency responsible for the safety of foods and drugs sold in U.S. together with an independent panel of medical advisors, the FDA reviews the scientific data and determines whether the drug is safe and effective for people with Alzheimer’s. NMDA7 antagonist, is prescribed to treat moderate to severe Alzheimer’s disease. Acetyl cholinesterase8 is an enzyme that degrades the neurotransmitter acetylcholine , producing choline and an acetate group. Donepezil9 enhances cholinergic transmission by reducing the enzymatic degradation of acetylcholine. Donepezil is 1200 times more selective for acetyl cholinesterase rather than butyl cholinesterase. Donepezil gives a short-term improvement in cognitive function but does not appear to alter the underlying disease process. Bioinformatics was an emerging field with the potential to significantly improve how drugs are found, brought to clinical trials and eventually released to the marketplace. The main aim of doing CADD: •

CADD enable comparative study of the analogues and help us in analyzing relative superiority of the analogues to the initial drug itself.

Computer-assisted molecular design (CAMD) represents more recent applications of computers as tools in the drug design process.

Extensive literature studies were undertaken to scrutinize methods involved in computer aided drug designing.

National and international journal, news and conference reviews also patents available on drug designing of Alzheimer’s were searched from available web sites.

II.

METHODOLOGY

The present study was to design and identify the potent novel acetyl cholinesterase inhibitors in the treatment of Alzheimer’s disease using Insilco tools and techniques.

Based on above scheme select the disease to that select target protein and collect the protein reports from PDB. Compute protein energy minimization. Select the lead moiety and design the ligands/analogs for lead moiety. Compute energy minimization and note down molecular properties. Dock the ligand analogs and minimized protein. From that we can determine the binding affinity of analogs. www.irjmets.com

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MODELING AND ANALYSIS

The software’s used for design of drug analogs are Hyperchem and GOLD( Genetic Optimization for ligand Docking). Hyperchem is a molecular modeler and editor and a powerful computational technique. Hyperchem used to build and display molecules, optimizing the structure of molecules and studying the dynamic behavior of molecules.

Fig.-4: HyperChem software for design of drug analogs Computational molecular docking is a research technique for predicting whether one molecule will bind to another, usually a protein. Protein -protein, protein-DNA and protein-ligand docking prediction is all performed by using Hyperchem software.

Fig.-5: Docking study with HyperChem GOLD used in virtual screening, lead optimization, and identifying the correct binding mode of active molecules. GOLD uses genetic sequence to provide docking of flexible ligand and a protein with hydroxy groups. This makes GOLD is the good choice when the binding pocket contains amino acids that form hydrogen bonds with the ligand. GOLD offers a scoring functions: GOLD score, Chem Score and User defined Score. The solutions are known to have 70-80% accuracy when tested on complexes extracted from PDB.

Fig.-6: GOLD- Protein Ligand Docking Software www.irjmets.com

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Following steps are involved in Donepezil analog study: 1.Determining the analogs and energy optimization a) b) c) d) e) f)

Force field Selection(AMBER) Analog Selection(Donepezil) Single Point Energy Calculation(energy or spin density) Geometry Optimization(energy of analogs optimized) Molecular Mechanics Optimization(Polak-Ribiere) Measuring Intramolecular parameters(bond length, bond angle, torsion angle)

2. Dynamic calculations a) Molecular dynamic calculations 3. Optimization of Solvents a) b) c) d) e) f)

Adding periodic box(simulate behavior of molecules in aqueous solution) Molecular Mechanics force field(AMBER) Optimization by selecting only the Hydrogens Optimization by selecting only water molecules Optimization by selecting active region(modified hydrophobic region)of ligand Optimization for the ligand molecule in its solvated state

4. Optimization in various force fields(bond length, bond angle, torsion angles) 5. Optimization of protein-ligand complexes(target for donepezil is acetyl cholinesterase having enzyme code 1EVE) 6. Docking a) Preparing input for Docking b) Docking(using GOLD software)

IV.

RESULTS AND DISCUSSION

Donepezil Ligand R-CH3 is replaced with different ligands like R-NH2, R-CH2CH3, R-OH, R-Cl and R-H. Energy minimization of different ligand moieties are given in the table. Table-1 Ligand-R-CH3

Single point

Energy

Gradient

Converge

1816.160 kcal/mol

1092.113kcal/A0mol

Yes

Geometry optimization

31.81 kcal/mol

0.000931 kcal/A0mol

Yes

Single point

Energy

Gradient

Converge

1687.42 kcal/mol

1096.983kcal/A0mol

Yes

31.24 kcal/mol

0.000849 kcal/A0mol

Yes

Fig No 7 Ligand-R-NH2

Geometry optimization Fig No 8

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Single point

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Energy

Gradient

Converge

1812.94 kcal/mol

1060.493 kcal/A0mol

Yes

Geometry optimization

32.965kcal/mol

0.001000kcal/A0mol

Yes

Single point

Energy

Gradient

Converge

Fig No 9 Ligand-R-OH

kcal/A0mol

1736.90 kcal/mol

1108.02

Yes

Geometry optimization

31.182 kcal/mol

0.000940 kcal/A0mol

Yes

Single point

Energy

Gradient

Converge

Fig No 10 Ligand-R-Cl

kcal/A0mol

1851.67 kcal/mol

1125.52

Yes

Geometry optimization

32.00 kcal/mol

0.000968 kcal/A0mol

Yes

Single point

Energy

Gradient

Converge

1642.78 kcal/mol

116.74 kcal/A0mol

Yes

29.45 kcal/mol

0.000993kcal/A0mol

Yes

Fig No 11 Ligand-R-H

Geometry optimization Fig No 12

Table-2: Ligand in periodic box: Ligand-R-CH3

Selected atoms

Hydrog ens

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Geometry optimization Steepest descent(500)

Polakribier(2000cycles)

Energy

Gradient

Conver ge

Energy

Gradien t

Conver ge

8836.19kcal /mol

0.76kcal/A0 mol

No

-1073.36

0.00098 8 kcal/A0 mol

Yes

kcal/mol

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Whole molecul e

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1073.36kcal /mol

0.000988 kcal/A0mol

1073.36kcal /mol

0.000988 kcal/A0mol

No

No

www.irjmets.com 1073.36kcal /mol

0.00098 8

1073.36kcal /mol

0.00098 8 kcal/A0 mol

Yes

kcal/A0 mol Yes

Table-3 Ligand-R-NH2

Selected atoms

Hydrog ens

Geometry optimization Steepest descent(500)

Polakribier(2000cycles)

Energy

Gradient

Conver ge

Energy

Gradient

Converge

7092.24kcal /mol

1.251kcal/A0 mol

No

8861.4 8

0.166

Yes

kcal/A0 mol

kcal/m ol

Fig No:14 Ligands

8864.81kcal /mol

0.064

No

kcal/A0mol

8878.3 5 kcal/m ol

Whole molecul e

-8878.35

0.001000

kcal/mol

kcal/A0mol

No

8878.3 5 kcal/m ol

Selected atoms Ligand-RCH2CH3

Hydrog ens

0.00100 0

Yes

kcal/A0 mol 0.00100 0

Yes

kcal/A0 mol

Geometry optimization Steepest descent(500)

Polakribier(2000cycles)

Energy

Gradient

Conver ge

Energy

Gradient

Conver ge

6800.60kcal/ mol

0.815kcal/A0 mol

No

8474.6 7

0.038

Yes

kcal/A0m ol

kcal/m ol Ligands Fig No: 15

8474.83kcal/ mol

0.015 kcal/A0mol

No

8476.1 19

0.000992

Yes

kcal/A0m ol

kcal/m www.irjmets.com

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Whole molecul e

-8476.12

0.000992

kcal/mol

kcal/A0mol

No

8476.1 2

0.000992

Yes

kcal/A0m ol

kcal/m ol Table-5 Ligand-R-OH

Selected atoms

Hydroge ns

Geometry optimization Steepest descent(500)

Polakribier(2000cycles)

Energy

Gradient

Conver ge

Energy

Gradient

Conver ge

11558.16kcal/ mol

2.167kcal/A0 mol

No

1440.3 69

0.0495

Yes

kcal/A0 mol

kcal/m ol

Fig No: 16 Ligands

1440.725kcal/ mol

0.0164

No

kcal/A0mol

14402. 02 kcal/m ol

Whole molecul e

-1440.016

0.000988

kcal/mol

kcal/A0mol

No

1440.0 16 kcal/m ol

0.00098 8

Yes

kcal/A0 mol 0.00098 8

Yes

kcal/A0 mol

Table-6 Ligand-R-Cl

Selected atoms

Hydroge ns Fig No:17

Geometry optimization Steepest descent(500)

Polakribier(2000cycles)

Energy

Gradient

Conver ge

Energy

Gradient

Conver ge

8744.14kcal/ mol

2.0871kcal/A0 mol

No

10736. 17

0.127

Yes

kcal/A0 mol

kcal/m ol Ligands

10738.41kcal/ mol

0.029 kcal/A0mol

No

1077.1 42 kcal/m

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0.00097 4

Yes

kcal/A0 mol

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Whole molecul e

-1077.142

0.000974

kcal/mol

kcal/A0mol

No

1077.1 42 kcal/m ol

0.00097 4

Yes

kcal/A0 mol

Table-7 Ligand-R-H

Fig No: 18

Selected atoms

Geometry optimization Steepest descent(500)

Hydroge ns

Polakribier(2000cycles)

Energy

Gradient

Conver ge

Energy

Gradient

Conver ge

14198.96kcal/ mol

2.233kcal/A0 mol

No

174.00 34

0.19170 7

Yes

kcal/m ol Ligands

17450.26kcal/ mol

0.0384

No

1759.6 79

kcal/A0mol

kcal/A0 mol 0.0069

Yes

kcal/A0 mol

kcal/m ol Whole molecul e

-1759.689

0.0069

kcal/mol

kcal/A0mol

No

1759.6 89 kcal/m ol

0.00097 8

Yes

kcal/A0 mol

Table-8: Solvated Ligand Donepezil Ligand R-NH2

R-NH2

Force field MM+

Force field Amber-99

Energy

23.77 kcal/A0mol

44.434kcal/A0mol

Gradient

0.000899kcal/A0mol

0.000949 kcal/A0mol

Converge

Yes(766 points)

Yes(642 points)

cycles 1684

cycles

1399

Fig No: 19 Table-9 Donepezil R-CH2CH3

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R-CH2CH3

Force field MM+

Force field Amber-99

Energy

25.98 kcal/A0mol

42.119 kcal/A0mol

Gradient

0.002044 kcal/A0mol

0.000975kcal/A0mol

Converge

Yes(855 1905points)

Yes(709 points)

cycles

cycles

1545

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Fig No:20 Table-10 Donepezil R-OH

R-OH

Force field MM+

Force field Amber-99

Energy

21.44 kcal/mol

42.83 kcal/mol

Gradient

0.000821 kcal/A0mol

0.000985 kcal/A0mol

Converge

Yes(651 points)

Yes(608 1301points)

cycles

1651

cycles

Fig No:21 Table-11 Donepezil R-Cl

R-Cl

Force field MM+

Force field Amber-99

Energy

22.89 kcal/A0mol

8.20 kcal/A0mol

Gradient

0.006264 kcal/A0mol

0.020493kcal/A0mol

Converge

Yes(855 4281points)

Yes(1456 cycles 3212 points)

cycles

Fig No: 22 Table-12 Donepezil R-H

R-H

Force field MM+

Force field Amber-99

Energy

20.93 kcal/A0mol

6.26 kcal/A0mol

Gradient

0.007079 kcal/A0mol

0.000961 kcal/A0mol

Converge

Yes(855 cycles 2106 points)

Yes(794 points)

cycles 1727

Fig No:23 Table-13: Binding Energy calculation: S.no

Ligand

X1(energy of ligand in medium of air)

X2(energy of solvated ligand)

X=X1+(-X2)

1

-CH3

31.81

42.80

-10.99

2

-NH2

31.24

44.34

-13.1

3

-CH2CH3

32.97

42.119

-9.149

4

-OH

31.18

42.83

-11.648

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5

-Cl

32.00

39.33

-7.33

6

-H

29.45

28.78

0.67

Table-14: Protein with modified ligand Donepezil R-CH3

Geometry optimization (polak) Energy

Gradient

Converge

Whole protein

-13698.32 kcal/mol

0.734 kcal/A0mol

Yes

Ligand

-14.91 kcal/mol

0.000994 kcal/A0mol

Yes

Donepezil R-NH2

Geometry optimization (polak)

Fig No:24

Energy

Gradient

Converge

Whole protein

-5056.50 kcal/mol

0.22043 kcal/A0mol

Yes

Ligand

-13.32 kcal/mol

0.00092 kcal/A0mol

Yes

Donepezil R-CH2CH3

Geometry optimization (polak)

Fig No:25

Energy

Gradient

Converge

Whole protein

6124.43kcal/mol

0.3114 kcal/A0mol

Yes

Ligand

-15.11 kcal/mol

0.000998 kcal/A0mol

Yes

Donepezil R-OH

Geometry optimization (polak)

Fig No:26

Energy

Gradient

Converge

Fig No:27 www.irjmets.com

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Whole protein

-6533.18 kcal/mol

0.32 kcal/A0mol

Yes

Ligand

-12.86 kcal/mol

0.000995 kcal/A0mol

Yes

Donepezil R-Cl

Geometry optimization (Polak) Energy

Gradient

Converge

Whole protein

-5056.68 kcal/mol

0.22kcal/A0mol

Yes

Ligand

-13.73kcal/mol

0.000924 kcal/A0mol

Yes

Donepezil R-H

Geometry optimization (Polak)

Fig No:28

Energy

Gradient

Converge

Whole protein

-4625.62kcal/mol

0.335 kcal/A0mol

Yes

Ligand

-12.36 kcal/mol

0.000863 kcal/A0mol

Yes

Fig No:29

Protein for Docking

Fig.-30: Acetyl Cholinesterase Protein Table-15 Energy

Gradient

Converged

-1556 kcal/mol

0.000952 kcal/A0mol

Yes

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Table-16: Ligand for Docking Ligand

Energy

Gradient

Converge

R-NH2

35.06 kcal/mol

0.000952 kcal/A0mol

Yes (955 2086points)

cycles

R-CH3

38.60kcal/mol

0.000997 kcal/A0mol

Yes (183 410points)

cycles

R-CH2CH3

37.97 kcal/mol

0.000807 kcal/A0mol

Yes (135 cycles 314 points)

R-OH

34.30 kcal/mol

0.000960 kcal/A0mol

Yes (807 cycles 1712 points)

R-Cl

38.35 kcal/mol

0.000984 kcal/A0mol

Yes (37 points)

R-H

33.98 kcal/mol

0.000957 kcal/A0mol

Yes (968 points)

cycles

84

cycles 2106

Table-17 S. No

Ligands

Fitness

S(hb-ext)

S(vdw-ext)

S(hb-int)

S(vdw-int)

1

-CH3

60.68

0.28

52.43

0.00

-11.69

2

-NH2

65.47

4.63

48.90

0.00

-6.41

3

-CH2CH3

69.11

0.00

54.53

0.00

-5.86

4

-OH

52.62

4.10

47.12

0.00

-6.27

5

-C1

61.11

5.55

46.26

0.00

-8.05

6

-H

49.54

0.01

50.72

0.00

-20.21

Table-18 S.no

Ligand

Y1

(-)Y2

Y=Y1+Y2

1

-CH3

-14.91

(-)60.68

-75.59

2

-NH2

-13.32

(-)65.4575

-78.7775

3

-CH2CH3

-15.11

(-)64.99375

-80.10375

4

-OH

-12.86

(-)62.62

-75.48

5

-C1

-13.73

(-)61.1075

-74.8375

6

-H

-12.36

(-)49.54

-61.876

Y1=Protein intra dock Y2=Docking energy Table-19 S.no

Ligand

Y

X

Z=Y-X

1

-CH3

-75.59

-10.99

-64.6

2

-NH2

-78.7775

-13.1

-65.6775

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3

-CH2CH3

-80.10375

-9.149

-70.95475

4

-OH

-75.48

-11.648

-63.832

5

-C1

-74.8375

-7.33

-67.5075

6

-H

-61.876

0.67

-62.546

Table-26 Relative binding free energy S.no

Molecules

Relative binding free energy

1

-NH2

-1.07

2

-CH2CH3

-6.35475

3

-OH

0.768

4

-C1

2.054

5

-H

-2.9075

Through rational based drug design approach, new analogs are designed by replacing pharmacophore groups (which are having tendency to bond with target protein) in ligand. Docking is performed with the optimized analogs and protein and binding energy was calculated for each analog. The analog with R group –CH2CH3 in Donepezil having lowest binding free energy -6.35475 will have maximum binding affinity.

V.

CONCLUSION

Based on energy minimization, force field calculations and protein ligand docking studies of structurally similar analogs of Donepezil indicates that molecular mechanics methods gave suitable analogs. Molecular mechanics-based methods for calculation of relative binding affinities can be used before synthesis and biochemical testing of new analogs. The drug Donepezil with substituent R= -CH2CH3 is identified as the most suitable analog in the present study and needs to be further evaluated in laboratory.

VI. [1]

[2] [3]

[4] [5] [6] [7] [8] [9]

REFERENCES

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