The NMR signature of maltose-based glycation in full-length proteins

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The NMR signature of maltose-based glycation in full-length proteins

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NMR assignment:

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Side-chains:

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Structure from NMR restraints:

Ab initio:

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Rosetta-NMR (Robetta)

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GeNMR

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Amber

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Torsion angles from chemical shifts:

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TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

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Proshift

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Camcoil

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12-21-2023, 03:08 PM

nmrlearner

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The NMR signature of maltose-based glycation in full-length proteins

The NMR signature of maltose-based glycation in full-length proteins

Abstract

Reducing sugars can spontaneously react with free amines in protein side chains leading to posttranslational modifications (PTMs) called glycation. In contrast to glycosylation, glycation is a non-enzymatic modification with consequences on the overall charge, solubility, aggregation susceptibility and functionality of a protein. Glycation is a critical quality attribute of therapeutic monoclonal antibodies. In addition to glucose, also disaccharides like maltose can form glycation products. We present here a detailed NMR analysis of the Amadori product formed between proteins and maltose. For better comparison, data collection was done under denaturing conditions using 7Â*M urea-d4 in D2O. The here presented correlation patterns serve as a signature and can be used to identify maltose-based glycation in any protein that can be denatured. In addition to the model protein BSA, which can be readily glycated, we present data of the biotherapeutic abatacept containing maltose in its formulation buffer. With this contribution, we demonstrate that NMR spectroscopy is an independent method for detecting maltose-based glycation, that is suited for cross-validation with other methods.

Source: Journal of Biomolecular NMR

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