Dataset Information

Noncovalent CH-π and π-π Interactions in Phosphoramidite Palladium(II) Complexes with Strong Conformational Preference.

ABSTRACT: The weak noncovalent interactions and flexibility of ligands play a key role in enantioselective metal-catalyzed reactions. In transition metal complexes and their catalytic applications, the experimental assessment and the design of key interactions is as difficult as the prediction of the enantioselectivities, especially for flexible, privileged ligands such as chiral phosphoramidites. Therefore, the interligand interactions in cis-Pd^II L₂ Cl₂ phosphoramidite complexes were investigated by NMR spectroscopy and computations. We were able to induce a strong conformational preference by breaking the symmetry of the C₂ -symmetric side chain of one of the ligands, and shift the equilibrium between hetero- and homocomplexes towards heterocomplexes because of interligand interactions in the cis-complexes. The modulation of aryl substituents was exploited, along with the solvent effect. The combined CH-π and π-π interactions reveal design patterns for binding and folding of chiral ligands and catalysts.

SUBMITTER: Zabka M

PROVIDER: S-EPMC9298319 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature

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Noncovalent CH-π and π-π Interactions in Phosphoramidite Palladium(II) Complexes with Strong Conformational Preference.

Žabka Matej M Naviri Lavakumar L Gschwind Ruth M RM

Angewandte Chemie (International ed. in English) 20211103 49

The weak noncovalent interactions and flexibility of ligands play a key role in enantioselective metal-catalyzed reactions. In transition metal complexes and their catalytic applications, the experimental assessment and the design of key interactions is as difficult as the prediction of the enantioselectivities, especially for flexible, privileged ligands such as chiral phosphoramidites. Therefore, the interligand interactions in cis-PdII L2 Cl2 phosphoramidite c ...[more]

PMID: 34585835

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Project description:Glycan-binding proteins, or lectins, recognize distinct structural elements of polysaccharides, to mediate myriad biological functions. Targeting glycan-binding proteins involved in human disease has been challenging due to an incomplete understanding of the molecular mechanisms that govern protein-glycan interactions. Bioinformatics and structural studies of glycan-binding proteins indicate that aromatic residues with the potential for CH-π interactions are prevalent in glycan-binding sites. However, the contributions of these CH-π interactions to glycan binding and their relevance in downstream function remain unclear. An emblematic lectin, human galectin-3, recognizes lactose and N-acetyllactosamine-containing glycans by positioning the electropositive face of a galactose residue over the tryptophan 181 (W181) indole forming a CH-π interaction. We generated a suite of galectin-3 W181 variants to assess the importance of these CH-π interactions to glycan binding and function. As determined experimentally and further validated with computational modeling, variants with smaller or less electron-rich aromatic side chains (W181Y, W181F, W181H) or sterically similar but nonaromatic residues (W181M, W181R) showed poor or undetectable binding to lactose and attenuated ability to bind mucins or agglutinate red blood cells. The latter functions depend on multivalent binding, highlighting that weakened CH-π interactions cannot be overcome by avidity. Two galectin-3 variants with disrupted hydrogen bonding interactions (H158A and E184A) showed similarly impaired lactose binding. Molecular simulations demonstrate that all variants have decreased binding orientation stability relative to native galectin-3. Thus, W181 collaborates with the endogenous hydrogen bonding network to enhance binding affinity for lactose, and abrogation of these CH-π interactions is as deleterious as eliminating key hydrogen bonding interactions. These findings underscore the critical roles of CH-π interactions in carbohydrate binding and lectin function and will aid the development of novel lectin inhibitors.

Dataset Information

Noncovalent CH-π and π-π Interactions in Phosphoramidite Palladium(II) Complexes with Strong Conformational Preference.

Publications

Noncovalent CH-π and π-π Interactions in Phosphoramidite Palladium(II) Complexes with Strong Conformational Preference.

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