Department of Medical Laboratory Sciences, College of Applied Medical Sciences, University of Hail, Hail, Saudi Arabia.
Department of Biochemistry, S.S. Faculty of Science, Mohammad Ali Jauhar University, Rampur, India.
Cell Biochem Funct. 2022 Jul;40(5):526-534. doi: 10.1002/cbf.3722. Epub 2022 Jun 16.
Glycation is vital in terms of its damaging effect on macromolecules resulting in the formation of end products, which are highly reactive and cross-linked irreversible structures, known as advanced glycation end products (AGEs). The continuous accumulation of AGEs is associated with severe diabetes and its associated ailments. Saccharides with their reducing ends can glycate amino acid side chains of proteins, among them glucose is well-known for its potent glycating capability. However, other reducing sugars can be more reactive glycating agents than glucose. The D-ribose is a pentose sugar-containing an active aldehyde group in its open form and is responsible for affecting the biological processes of the cellular system. D-ribose, a key component of many biological molecules, is more reactive than most reducing sugars. Protein glycation by reducing monosaccharides such as D-ribose promotes the accelerated formation of AGEs that could lead to cellular impairments and dysfunctions. Also, under a physiological cellular state, the bioavailability rate of D-ribose is much higher than that of glucose in diabetes, which makes this species much more active in protein glycation as compared with D-glucose. Due to the abnormal level of D-ribose in the biological system, the glycation of proteins with D-ribose needs to be analyzed and addressed carefully. In the present study, human immunoglobulin G (IgG) was isolated and purified via affinity column chromatography. D-ribose at 10 and 100 mM concentrations was used as glycating agent, for 1-12 days of incubation at 37°C. The postglycation changes in IgG molecule were characterized by UV-visible and fluorescence spectroscopy, nitroblue tetrazolium assay, and various other physicochemical analyses for the confirmation of D-ribose mediated IgG glycation.
糖基化在其对大分子的破坏性影响方面至关重要，导致终产物的形成，这些终产物是高度反应性和交联的不可逆结构，称为晚期糖基化终产物（AGEs）。AGEs 的不断积累与严重的糖尿病及其相关疾病有关。具有还原末端的糖可以糖化蛋白质的氨基酸侧链，其中葡萄糖以其强大的糖化能力而闻名。然而，其他还原糖可能比葡萄糖更具反应性的糖化剂。D-核糖是一种戊糖，在其开链形式中含有一个活性醛基，负责影响细胞系统的生物过程。D-核糖是许多生物分子的关键组成部分，比大多数还原糖更具反应性。还原单糖如 D-核糖对蛋白质的糖化作用促进了 AGEs 的加速形成，这可能导致细胞损伤和功能障碍。此外，在生理细胞状态下，D-核糖的生物利用度速率在糖尿病中比葡萄糖高得多，这使得该物质在蛋白质糖化方面比 D-葡萄糖更活跃。由于生物系统中 D-核糖的异常水平，需要仔细分析和解决 D-核糖与蛋白质的糖化。在本研究中，通过亲和柱色谱法分离和纯化人免疫球蛋白 G（IgG）。使用 10 和 100 mM 浓度的 D-核糖作为糖化剂，在 37°C 下孵育 1-12 天。通过紫外可见和荧光光谱、硝基蓝四唑测定以及各种其他物理化学分析来表征 IgG 分子在糖基化后的变化，以确认 D-核糖介导的 IgG 糖基化。
