s performed by AUTODOCK 4.2.

The amino acid residues of ASP297, GLY298, CYS299, TRP303, TYR

syltransferase. The docking results showed that flavon and its derivatives formed hydrogen bonds with TYR3
ligand of L-778, 123, FPP it suggests that flavon and its derivatives will be a selective can interact with rece
roxyflavone into farnesyltransferase was 6.07 kcal/mol.

Farnesyltransferase, Computational Method, Cancer

INTRODUCTION

METODOLOGY

bstance isolated from a wide range of vascular plants, with over 8000 indiavonoids are secondary plant products. They are mainly found in fruits,
ages that have diverse beneficial biochemical antioxidant and anticancer.
bitors are a new class of biologically active anticancer drugs. The exact
class of agents is, however, currently unknown. The drugs inhibit farnesylet proteins, including Ras. It is thought that these agents block Ras activae enzyme farnesyl transferase, ultimately resulting in cell growth arrest. In
syl transferase inhibitors showed great potency against tumor cells; yet in
y was far less than anticipated. Reasons for this disappointing clinical outdrug-development process. In this paper, we outline an algorithm that is
elopment of biologically active anticancer drugs.
rative disorder that is usually treated by chemotherapeutic agents that are
s but also to normal cells. Brain tumor is a tumor which located in brain,
membranes lining the brain (meninges). Brain tumors were the second
male patients by the age of 20-39 years.

Flavon

Geometric Optimization
ab initio

V
Hyperchem v8.01

OBJECTIVES

DOCKING SIMULATION

ones, which are compounds derivatived flavonoid with Farnesyltransfer-

AutoDock 4.2

RESULTS & DISCUSSION

ative Ligand and Flavone Docking Simulation

nd into Farnesyltransferase binding Pocket

Far

kI (nM)
2.29

Residu of Amino Acid

ASP297, GLY298, CYS299,

2
TRP303, TYR361

vone into Farnesyltransferase binding Pocket

35.60

TYR300, TYR361, TRP303

d of Native Ligand and Flavon

Ligand Atom

Distance ()

nd into Farnesyltransferase binding Pocket

H18 at OD2

1.92634

NE1 at O13

2.8414

vone into Farnesyltransferase binding Pocket

H at OH

2.21399

Fig 1. L-778, 123, FPP Into Binding

Pocket of Farnesyltransferase

Fig 2. 6-hydr
Pocket o