Chemistry Reference
In-Depth Information
In 2008 we investigated pharmacokinetic and pharmacodynamic predictions of
novel potential HIV-1 integrase inhibitors [19].
In 2008 we published the second volume of our Enciclopedia: Current Methods in
Medicinal Chemistry and Biological Physics [20].
In 2008 we also published an Invited Mini Review on Current Topics in
Computer-aided Drug Design [21].
In 2009 we reported computer-aided drug design of novel Phospholipase A
2
(PLA
2
) inhibitor candidates for treatment of snakebites. We did the PLA
2
BthTX-I
structure prediction based on homology modeling as well as a virtual screening in
a large database yielding a set of potential bioactive inhibitors. Molecular
interaction fields indicated important binding effects. We proposed a theoretically
nontoxic, drug-like, and potential novel BthTX-1 inhibitor. Our calculations were
used to design novel phospholipase inhibitors for future treatment of snakebite
victims as well as other human diseases in which PLA
2
enzymes are involved [22,
540].
In 2010 we reported computer-aided drug design and ADMET predictions for
identification and evaluation of novel potential farnesyltransferase inhibitors in
cancer therapy [541]. Ras protein is a cell component that controls growth and
multiplication whereas an abnormal form of the signaling Ras is present in almost
30% of cancers. Methods capable of neutralizing Ras are useful in the fight
against cancer. We used molecular dynamics, density functional theory, virtual
screening, ADMET predictions and molecular interaction field studies to design,
analyze and propose novel potential inhibitors of Farnesyltransferase. Some
proposals indicate theoretically interesting pharmacotherapeutic profiles, when
compared to the very active and most cited FTase inhibitors. This yields
alternative scaffolds to design future potential FTase inhibitors in the fight against
cancer [23].
In 2010 we published our topic Recent Developments in Medicinal Chemistry,
2010, Vol 1 [24].
We reported in 2010 our invited contribution stoichiometry of amino acids driven
protein folding? [25].
