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tant for the binding of both agonists and antagonists.6
Hence, 5-HT, Gramine (both agonists), Ketanserin
and Spiperone (both antagonists) have no affinity for
D155A, D155N and D155Q mutant receptors. More re-
cent work has suggested that the binding interaction of
the basic nitrogen may be more complex than originally
thought, since there may be an additional interaction of
the protonated amine with a Ser159, also on Helix 3.7
Mutating this serine again affected the binding of some
agonists such as 5-HT, whilst others such as lysergic acid
were not affected.
Figure 3.
affinity for 5-HT2A receptors (Ki 5-HT2A >5000 nM).
The amide linkage in 4 restricts rotation of the pheneth-
yl side chain and it is possible that the phenyl group is
prevented from reaching a suitable position for binding.
Although the basic nitrogen in 5-HT2 receptor antago-
nists has been identified as being important for the bind-
ing of agonists and antagonists of the receptor, it has
also been implicated in a number of undesirable side ef-
fects associated with compounds of this class. These in-
clude affinity for dopamine receptors and the IKr
potassium channel, a voltage gated ion channel involved
in control of the heart rhythm. Regulatory agencies are
increasingly concerned about cardiovascular events fol-
lowing the chronic dosing of drugs, and require strin-
gent tests to confirm their safety. The atypical
antipsychotic sertindole, a compound with dual 5-HT2/
D2 affinity, was withdrawn from the market due to the
prolongation of the corrected QT interval, a conse-
quence of its affinity for the IKr channel.8 Designing
5-HT2A ligands with little or no affinity for the IKr
channel would therefore be beneficial. However, potent
IKr channel blockers such as Dofetilide and Terfenadine
(Fig. 2) clearly show that the pharmacophore for bind-
ing at IKr is similar to the one for binding at the 5-
HT2A receptor. Recent work that involved building a
predictive pharmacaphore model for the IKr potassium
channel concluded that the following features were
important for binding: ‘one positive ionisable feature,
two aromatic rings and one hydrophobic group.’9
From unpublished work in our own laboratories, and
known 5-HT2A ligands such as EMD-281014, we knew
that piperazine amides and sulfonamides,11 such as 3,
provide high affinity antagonists analogous to the
piperidine sulfones represented by 2. Consequently,
we chose to synthesise compound 5, again non-basic,
but without the conformational restriction of the amide
4 and where the hydroxyl group can serve either as a
mimic of the protonated amine or in its own right as
a hydrogen bond donor/acceptor that might interact
with Ser159. Gratifyingly, we found that 5 had greater
affinity for the 5-HT2A receptor (Ki 5-HT2A 190 nM)
than the amide 4. The present paper describes the
development of this lead into a novel series of non-
basic piperidine sulfonamides and amides to give high
affinity, selective ligands, thus disproving the generally
accepted view that a basic nitrogen is crucial for bind-
ing at the 5-HT2A receptor.
The 4-hydroxypiperidine 5 was synthesised by addition
of the requisite Grignard reagent to N-BOC piperidone
to give 6, followed by deprotection, and sulfonylation of
the resulting trifluoroacetate salt (Scheme 1). Treating 5
We have previously shown that in the sulfonylpiperidine
series of 5-HT2A antagonists (2), reducing the basicity of
the piperidine nitrogen together with appropriate aro-
matic substitution can lead to significantly reduced bind-
ing to the IKr channel.10 We investigated the interaction
of the basic nitrogen further by synthesising the amide 4
(Fig. 3) which, although lacking a basic nitrogen that
can interact with the charged Asp155, does have an
amide which could perhaps interact as a hydrogen bond
acceptor with Ser159. The amide 4, however, had no
Scheme 1. Reagents: (i) 2,4-difluorophenethyl bromide, Mg, THF; (ii)
TFA, Et3N, 4-F-phenylsulfonyl chloride, CH2Cl2; (iii) DAST, CH2Cl2.
Figure 2. IKr channel blockers.