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• W4253163929 abstract "Protein glycation is a post-translational modification (PTM) involving chemical condensation reaction between primary amine groups of proteins and aldehyde or hemiacetal group of aldose sugars such as d-glucose. During glycation reactions, aldehyde or hemiacetal groups of reducing sugars reacts with primary amine groups of organic molecules such as amino acids to form aldimine (Schiff's base) intermediate. The intermediate Schiff's base is highly reactive and highly unstable, which undergoes rapid Amadori rearrangement to form a more stable ketoamine functionality which is also called as Amdori ketoamine. Primary amine groups present in amino acid side chains of proteins are the targets for glycation. The protein glycation may not be sequence-specific but highly dependent on the local environment of the primary amine groups present on the surface of proteins. Protein-linked Lys residues contain primary amine groups, and the surface-exposed Lys residues of proteins are prone to glycation. However, not all primary amine group of Lys residues are amenable to glycation. Surface exposed Lys residues require neighboring groups participation for glycation. Glycation may affect the protein structure and functions and may also cause immunogenicity. Upon glycation, the Amadori ketoamine undergoes degradation to form advanced glycation end products (AGEs). The AGEs may undergo further rearrangements and/or degradation. The AGEs and their related by-products have been shown to be immunogenic in humans. The AGEs and their related by-products are also shown to be toxic to humans. The receptor of AGEs known as receptor of advanced glycation end products (RAGEs) is also a receptor for amyloids. Glycation of serum albumin, hemoglobin, and serum immunoglobulins has been extensively studied. A1C or HbA1C is a glycated form of hemoglobin. Measuring the A1C levels is one of the clinical laboratory test to identify the different stages of diabetes. Protein glycation is implicated in many age-related chronic diseases such as Alzheimer, Parkinson, cardiovascular diseases, peripheral neuropathy, cancer, deafness.Recombinant therapeutic proteins (RTPs) including monoclonal antibodies (mAbs) have been shown to be glycated and their functions may be impacted by glycation. Glycation in the complementarity-determining region (CDRs) of mAbs may impact the antibody–antigen interactions. Glycation in the Fc region may impact antibody effector functions and serum half-life. Glycation in the catalytic domain of enzymes may impact their enzymatic activity. Hence, glycation may become critical quality attribute (CQA) for RTPs and mAbs. Boronate affinity chromatographic method has been extensively used to detect and quantify glycation of purified proteins including RTPs and mAbs. High-resolution mass spectrometry and peptide mapping methods are also being used to identify and to locate the glycation sites of proteins including RTPs and mAbs." @default.
• W4253163929 created "2022-05-12" @default.
• W4253163929 date "2019-03-15" @default.
• W4253163929 modified "2023-10-14" @default.
• W4253163929 title "Glycation of Proteins" @default.
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• W4253163929 doi "https://doi.org/10.1002/9781119053354.ch6" @default.
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