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Reexamining the diverse functions of arginine in biochemistry
Biochemical and Biophysical Research Communications ( IF 2.5 ) Pub Date : 2024-02-27 , DOI: 10.1016/j.bbrc.2024.149731
Munishwar Nath Gupta , Vladimir N. Uversky

Arginine in a free-state and as part of peptides and proteins shows distinct tendency to form clusters. In free-form, it has been found useful in cryoprotection, as a drug excipient for both solid and liquid formulations, as an aggregation suppressor, and an eluent in protein chromatography. In many cases, the mechanisms by which arginine acts in all these applications is either debatable or at least continues to attract interest. It is quite possible that arginine clusters may be involved in many such applications. Furthermore, it is possible that such clusters are likely to behave as intrinsically disordered polypeptides. These considerations may help in understanding the roles of arginine in diverse applications and may even lead to better strategies for using arginine in different situations.

中文翻译:

重新审视精氨酸在生物化学中的多种功能

游离状态的精氨酸以及作为肽和蛋白质的一部分显示出形成簇的明显倾向。人们发现,游离形式的它可用于冷冻保护、作为固体和液体制剂的药物赋形剂、作为聚集抑制剂以及蛋白质色谱中的洗脱液。在许多情况下,精氨酸在所有这些应用中的作用机制要么是有争议的,要么至少继续引起人们的兴趣。精氨酸簇很可能参与许多此类应用。此外,此类簇可能表现为本质上无序的多肽。这些考虑因素可能有助于理解精氨酸在不同应用中的作用,甚至可能导致在不同情况下使用精氨酸的更好策略。
更新日期:2024-02-27
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