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Instability of monoclonal myeloma protein may be identified as susceptibility to penetration and binding by newly synthesized Congo red derivatives

机译:单克隆骨髓瘤蛋白的不稳定性可能被认为是新合成的刚果红衍生物易于渗透和结合的原因

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Monoclonal myeloma proteins often have anabnormal, unstable structure, and tend to aggregate with fatal clinical consequences. A method for early clinical identification of this aggregation tendency is impatiently awaited. This work proposes the use of supramolecular dyes as specific ligands to reveal protein instability. Disclosure of excessive polypeptide chain flexibility in unstable monoclonal proteins, leading to increased susceptibility to penetration by foreign compounds, appeared possible when new supramolecular Congo red-derived dyes with different protein-binding capabilities were used for complexation. Two basic protein instability levels, local and global, were differentiated by comparing the extent of protein loading with dye and the subsequent electrophoretic migration rate of the complexes. A simple electrophoretic test is proposed for assessment of the instability of monoclonal proteins in clinical conditions. (C) 2004 Elsevier SAS. All rights reserved.
机译:单克隆骨髓瘤蛋白通常具有异常,不稳定的结构,并倾向于聚集在一起,产生致命的临床后果。不耐烦地等待着一种早期临床鉴定这种聚集趋势的方法。这项工作建议使用超分子染料作为特定的配体,以揭示蛋白质的不稳定性。当使用具有不同蛋白质结合能力的新型超分子刚果红衍生染料进行络合时,可能会发现不稳定的单克隆蛋白质中过多的多肽链柔性会导致外来化合物渗透的敏感性增加。通过比较蛋白质在染料中的上样程度和随后的复合物电泳迁移率,可以区分出两个基本的蛋白质不稳定性水平,即局部的和全局的。提出了一种简单的电泳测试来评估单克隆蛋白在临床条件下的不稳定性。 (C)2004 Elsevier SAS。版权所有。

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