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Hello, my name is Adrian Whitty.
I'm an associate
professor of chemistry
in the Department of Chemistry
at Boston University.
But before I came to
BU five years ago,
I worked in industry in drug
discovery for about 15 years.
And so my research programs
at Boston University
are very much guided by
what I learned about how
to develop drugs in
an industrial setting.
What I want to talk about
today is the problem
of how to develop small molecule
inhibitors against a very
challenging class of
drug targets, called
protein-protein interactions.
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So, I'm going to start by talking
about why one would even want
to inhibit protein-protein
interactions, in the first place.
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On this slide, we see an analysis
that was published by Hopkins
and Groom, about 10 years ago,
in which they have analyzed all
of the proteins that make
up the human proteome,
and attempted to determine
what fraction of those fall
into the classes of protein
families that we know we are
able to discover small
molecule inhibitors for,
using contemporary drug
discovery technology.
And, what this slide shows is
that, it's estimated that about 10%
of the gene products
in the human genome
are biologically
compelling as drug targets.
They're involved in
diseases, and, therefore,
potentially drugs
targeting those proteins
could be beneficial
in disease states.
What Hopkins and Groom determined
is that, only a fraction
of those biologically
compelling drug targets
fall into families that we know
how to find inhibitors four.
And the majority parts of other
protein families, where there is
no current precedent for
identifying small molecule
inhibitors that can act as drugs.
And a large fraction of these
disease modifying genes,
that are not part of conventionally
druggable gene families,
are protein-protein interactions.
