C687: Lecture 5

Molecular Modeling Examples and a Tour of the CAVE

March 8, 1999


This Lecture consists of three parts. The class will be divided into three groups and rotate through each part.

1:30-2:00 2:00-2:30 2:30-3:00
Group 1 CAVE Tour
Lindley Hall
Modeling Examples
Room A701
StereoView Room,
Graphics Output
Room A400
Group 2 Modeling Examples
Room A400
CAVE Tour
Lindley Hall
StereoView Room,
Graphics Output
Room A400
Group 3 Modeling Examples
Room A400
StereoView Room,
Graphics Output
Room A400
CAVE Tour
Lindley Hall

CAVE Tour

A tour of the
CAVE will be hosted by the VR/VE group in Lindley Hall room 135. The tour will cover the latest developments of the Reciprocal Net project & XMView, and constrained navigation about a peptide helix.

Examples of Molecular Modeling

The following example is shown in the text Molecular Modeling: Basic Principles and Applications, by Holtje & Folkers, VCH: New York, 1997.


28 different serotoninergic 5-HT2a receptor antagonists were modeled to define the pharmacophore. These antagonists can be divided into four structural subsets:

Compound Representative
in Figure 1
Color in
Figure 1
tricyclic compounds clothiapine red
4-(phenylketo)-piperidines altanserin aqua
irindalone compounds irindalone green
butyrophenone derivatives spiperone purple

FIGURE 1: Representative Serotoninergic 5-HT2a Receptor Antagonists


Confomational searches were performed for each ligand, and low-energy conformers that represent binding configurations were selected. This study utilized the "Active Analog Approach", in which conformationally constrained molecules were matched with diverse regions of highly flexible congeners Also, from comparisons of the structures of the 28 ligands, it was evident that the pharmacophore most likely included two planar or heterocyclic ring systems connected by an aliphatic or alicyclic chain with a protonable nitrogen. These structural elements of conformers were superimposed to aid in the selection of the consensus binding configurations.

FIGURE 2: Conformational Similarities of Structural Elements Derived from the Conformational Searches. Comparable structural elements of the four main groups of antagonists are color-coded and the stepwise superpositioning procedure followed is indicated. Clothiapine, irindalone, altanserin, and spiperone are shown from left to right.


Molecular Electrostatic Potentials using AM1-derived charges (AM1 is a semi-empirical quantum mechanical method) showed two slightly different electrostatic pharmacophores among the four representatives (Figure 3). In one of the two models, all of the protons at the pharmacophorically important cationic tertiary nitrogens are pointing in the same direction. In the other model, this is not the case. Assuming that this cationic protonated nitrogen involved ina hydrogen bond or electrostatic interaction with the receptor binding site, the first pharmacophore would clearly be favored.

FIGURE 3: Isopotential contours of clothiapine (upper left), altanserin (upper right), irindalone (lower left), and spiperone (lower right). blue = -1.0 kcal/mol, red = +1.0 kcal/mol, yellow = 0 kcal/mol


The hydrophilic and hydrophobic Molecular Interaction Fields (MIFs) of the antagonists show several common sites for hydrogen bonds and hydrophobic contacts.

FIGURE 4: Hydrophilic Molecular Interaction Field GRID contours fo the same molecules as shown in FIGURE 3 derived from an aliphatic hydroxyl probe. Energy contoured at -4.0 kcal/mol.

FIGURE 5: Hydrophobic Molecular Interaction Field GRID contours fo the same molecules as shown in FIGURE 3 derived from an aliphatic methyl probe. Energy contoured at -1.4 kcal/mol.


Superimposing common molecular interaction field contours resulted in the identification of the consensus pharmacophore (Figure 6).

FIGURE 6: The Concensus Pharmacophore. purple = hydrophobic area, green = electron-deficient aromatic system, red = electronegative heteroatoms, pink = protonated nitrogen, blue = large planar ring system


Based on the concensus pharmacophore, a receptor map can be constructed to approximate the receptor binding site (Figure 7).

FIGURE 7: Receptor Map. Positions A, B, C, D, and F depict hydrophobic contacts. Position E is an ionic interaction


The interaction of the receptor map with the pharmacophoric conformation of each antagonist can be calculated and compared to the experimental binding affinities. (Figure 8). Theory and Experiment Agree Very Well! This receptor map and the Concensus Pharmacophore can now be used to develop new antagonists with more potency!

FIGURE 8: Calculated Interaction Energies and Experimental Binding Affinitites


In-Class Assignment

You are given the amino acid sequence of a new protein, and the chemical structure of 2 ligands that bind to the protein, and the chemical structure of 1 similar ligand that does NOT bind to the protein.

Outline all of the molecular modeling experiments needed to model this system.


StereoView Room


Graphics Output


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Last updated: 01/23/2001