Protein–Ligand Screening by NMR

Claridge, Timothy D. W.

doi:10.1016/b978-0-08-099986-9.00011-7

Cited by 4 publications

(1 citation statement)

References 68 publications

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“…Protons with slower T1 relaxations accumulate saturation in solution, giving rise to higher STD relative intensity, thereby overestimating their proximity to the macromolecule. 36 Angulo et. al.…”

Section: Entrymentioning

confidence: 99%

Saturation Transfer Difference NMR Spectroscopy Using Glycopolymers

muzulu¹,

Basu

2020

Preprint

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<p>We report the use of Saturation Transfer Difference (STD) NMR spectroscopy to observe the interaction of various phenylboronic acids (PBAs) with synthetic glycopolymers presenting galactose and glucose. After optimizing experimental parameters to maximize spin diffusion, the binding of boronic acids to the glycopolymers was examined using STD NMR. Efficient amplification factor build-up curves which were used to generate an epitope map for the boronic acid binding to the glycopolymers. STD-NMR was also used to detect the interaction between indole and a galactosylated glycopolymer, providing an indole-based view of this C-H – π interaction.</p>

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Section: Entrymentioning

confidence: 99%

Saturation Transfer Difference NMR Spectroscopy Using Glycopolymers

muzulu¹,

Basu

2020

Preprint

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Characterization of Grades of HPMCAS Spray Dried Dispersions of Itraconazole Based on Supersaturation Kinetics and Molecular Interactions Impacting Formulation Performance

Adhikari

Polli

2020

Pharm Res

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Small molecule inhibitors of RAS-effector protein interactions derived using an intracellular antibody fragment

et al. 2018

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Targeting specific protein–protein interactions (PPIs) is an attractive concept for drug development, but hard to implement since intracellular antibodies do not penetrate cells and most small-molecule drugs are considered unsuitable for PPI inhibition. A potential solution to these problems is to select intracellular antibody fragments to block PPIs, use these antibody fragments for target validation in disease models and finally derive small molecules overlapping the antibody-binding site. Here, we explore this strategy using an anti-mutant RAS antibody fragment as a competitor in a small-molecule library screen for identifying RAS-binding compounds. The initial hits are optimized by structure-based design, resulting in potent RAS-binding compounds that interact with RAS inside the cells, prevent RAS-effector interactions and inhibit endogenous RAS-dependent signalling. Our results may aid RAS-dependent cancer drug development and demonstrate a general concept for developing small compounds to replace intracellular antibody fragments, enabling rational drug development to target validated PPIs.

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Protein–Ligand Screening by NMR

Cited by 4 publications

References 68 publications

Saturation Transfer Difference NMR Spectroscopy Using Glycopolymers

Saturation Transfer Difference NMR Spectroscopy Using Glycopolymers

Characterization of Grades of HPMCAS Spray Dried Dispersions of Itraconazole Based on Supersaturation Kinetics and Molecular Interactions Impacting Formulation Performance

Small molecule inhibitors of RAS-effector protein interactions derived using an intracellular antibody fragment

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