November 28, 2002Journal of the American Chemical Society

Virus−Ligand Interactions: Identification and Characterization of Ligand Binding by NMR Spectroscopy

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Population

Human rhinovirus serotype 2 (HRV2) and an antiviral compound (capsid-binding inhibitor)

Design

Preclinical

Authors

ABAndrew J. BenieNovo Nordisk (Denmark)RMRosita MoserUniversity of Vienna EBEnglbert BäumlPhilipps University of Marburg

Discussion

Member takes

Implication

Enables atomic-level viral ligand mapping without crystallization; leaves open clinical translation from animal models.

Structured PICO

Population

Human rhinovirus serotype 2 (HRV2) and an antiviral compound (capsid-binding inhibitor)

Intervention

Saturation transfer difference (STD) NMR spectroscopy

Outcome

Detection and characterization of ligand binding to viruses and determination of the ligand binding epitope at atomic resolution

STD NMR spectroscopy provides a fast and robust method to assess binding and determine ligand binding epitopes on viral capsids at atomic resolution without the need for crystallization.

Cite This Study

Benie et al. (2002) studied this question.

synapsesocial.com/papers/6a6f6fe88031ec7bb1dbbf59 https://doi.org/10.1021/ja027691e

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Virus−Ligand Interactions: Identification and Characterization of Ligand Binding by NMR Spectroscopy

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Virus−Ligand Interactions: Identification and Characterization of Ligand Binding by NMR Spectroscopy

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider