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co-instillation of P. aeruginosa in a lung infection model in mice and therefore pro-
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vides a promising drug candidate[149].
a
The proposed natural ligand of PA-IIL is the Lewis
[Fucα(1-4)]GlcNAc, which shows a dissociation constant of 210
trisaccharide, Galβ(1-3)
nM [137]. To
reduce the structural complexity of the trisaccharide, glycomimetics based on
either Fuc alone or the Fucα(1-4)GlcNAc disaccharide were designed and synthesized
(Figure5.11)[150–160].
The crystal structure of PA-IIL in complex with sulfonamide 6a (Figure5.11) provides insight into binding details. A hydrogen bond of the sulfonamide with the carboxylate of Asp96 and lipophilic contacts with the protein surface represent the most
1515.4 Pseudomonas aeruginosa Virulence Factors (PA-IL and PA-IIL)
0
Lewis
8 (REF. 156)
10 (REF. 158)
6a X = OMe, Y = H (REF. 153)
6b X = H, Y = Me (REF. 154)
9 (REF. 157)
7 (REF. 154)
11 (REF. 159)
12 (REF. 160)
Figure5.11 Representative structures of PA-IIL antagonists (6-11) and bifunctional
glycodendrimer (12).
5 Antiadhesive Carbohydrates and Glycomimetics
152
important contacts in this glycomimetic/lectin interaction[153]. Further structural
optimization on the sulfonamide moiety resulted in two nanomolar glycomimetics
(6b and 7, Figure5.11) with excellent receptor-binding kinetics and thermodynamic
profiles[154]. Both 6b and 7 efficiently blocked biofilm formation of P. aeruginosa
in vitro and showed good oral bioavailability and pharmacokinetic properties
in vivo [155]. The α--fucoside 8 bearing an isoxazol sulfonamide (Figure 5.11)
a
showed a potency comparable to Lewis
a
, such as derivative 9 (Figure5.11) [157], also reached binding affinity in
Lewis
[156]. Additionally, partial structures of
nanomolar range. ITC experiment with 9 revealed that increased entropy costs upon
binding are probably related to increased flexibility of Fucα(1-4)GlcNAc compared to
a
, which, however, is overcompensated by an enthalpy gain resulting from an
Lewis
extended hydrogen network. Finally, oligovalent ligands bearing Fucα(1-4)GlcNAc
(→ 10, Figure5.11)[158] or -Fuc (→ 11, Figure5.11)[159] exhibit increased binding
activity toward PA-IIL; however, this effect is modest on a per saccharide basis.
Notably, heterobifunctional ligands presenting both -Gal and -Fuc in an oligovalent set-up (→ 12, Figure5.11)[160] showed efficacy in surgically stressed mice.
Whereas 60% of the control group died within 48 hours after acute infection with
P. aeruginosa, 100% of mice treated with 12 survived.
5.4.3 Conclusions and Perspectives
Studies on monovalent glycomimetics have revealed a series of high-affinity PA-IL
and PA-IIL antagonists with low toxicity, good metabolic stability, and oral bioavailability. A notable feature of some candidates is their inhibitory potency against biofilm formation without affecting bacterial viability. Therefore, development of
resistance toward these antibiofilm agents is unlikely, in contrast to traditional bactericidal or bacteriostatic antibiotics. Additionally, combining elements of both
PA-IL and PA-IIL antagonists in one molecule represents a new, therapeutically
valuable compound class for fighting P. aeruginosa infections. Future developments
could include evaluation of antiadhesive therapeutics in a monotherapy treatment
against biofilm-associated infections as well as their synergistic effects with antibiotics for eradication of bacteria outside biofilms[141, 142].
5.5 General Aspects
Two topics, namely resistance and affinity of carbohydrates, are of general importance and are therefore not presented in each chapter separately but in a general
form in this last chapter.
Resistance. Drug resistance reduces the effectiveness of a medication, such as an
antimicrobial or an antiviral, in treating a disease. The alarming increase in drugresistant bacteria makes a search for novel anti-infective drugs mandatory[161].
It is well established that adhesion of enteric, oral, and respiratory bacteria is
the initial step required for colonization and the subsequent development of
References
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disease. An attractive possibility to reduce these contacts is to provide agents that
interfere with the ability of bacteria to adhere to tissues of their hosts. The validity
of this approach has been demonstrated in experiments performed in a wide variety of animals, from mice to monkeys, and also in humans[10]. Because antiadhesive agents are not bactericidal, the propagation and spread of resistant strains
are much less likely to occur after exposure to bactericidal agents, such as antibiotics. Inhibitor of adhesins, like FimH, PapG, or PA, involved in the first contact
between bacteria and host cells[162]. Also, blockers of viral entry receptors like
DC-SIGN are, therefore, regarded as a new means to fight infectious diseases.
Affinity of carbohydrate–lectin interactions. The interactions of carbohydrates
with proteins are mainly mediated by the directional hydrogen bond contacts of
hydroxyl groups. Thus, lectins have evolved to recognize the spatial arrangement
of these functional groups on carbohydrate scaffolds. In a typically shallow and
solvent-exposed lectin-binding pocket, highly mobile water molecules can easily
assume all relevant interactions and functionally replace the carbohydrate ligand.
In view of this, it is not self-evident why carbohydrate ligands bind to proteins
with any measurable affinity at all. To compensate for the unfavorable consequences of highly polar interactions in solvent-exposed binding sites, carbohydrates and lectins utilize a set of physicochemical mechanisms to mitigate these
unfavorable properties (cooperative desolvation and modulation of local dielectric properties)[163–165] or leverage other effects (hydrophobic CH–π interactions and preorganization)[166, 167] to enhance their binding affinity. However,
due to competition with an omnipresent solvent, the resulting interactions typically remain weak on a monovalent level as experienced in case of DC-SIGN,
PapG, or PA antagonists. High avidity in a biological context is achieved by
expanding the monovalent contact to an oligo- or multivalent level [168]. In
nature, interaction of multiple carbohydrate epitopes, e.g. on a glycoprotein, with
a surface displaying an equally high number of receptors potentiates the weak
monovalent interaction and gives thermodynamically complex systems with high
overall avidity. Inspired by nature, medicinal carbohydrate chemistry applies
comparable approaches to convert low-affinity natural carbohydrates or mediumaffinity glycomimetics into high-affinity, therapeutically valuable compounds.
153
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