Reexamining the diverse functions of arginine in biochemistry

被引:1
|
作者
Gupta, Munishwar Nath [1 ,5 ]
Uversky, Vladimir N. [2 ,3 ,4 ]
机构
[1] Indian Inst Technol, Dept Biochem Engn & Biotechnol, New Delhi 110016, India
[2] Russian Acad Sci, Inst Biol Instrumentat, Pushchino Sci Ctr Biol Res, Inst Skaya Str 7, Pushchino 142290, Moscow Region, Russia
[3] Univ S Florida, Morsani Coll Med, Dept Mol Med, Tampa, FL 33612 USA
[4] Univ S Florida, Morsani Coll Med, USF Hlth Byrd Alzheimers Res Inst, Tampa, FL 33612 USA
[5] 508-Block 3,Mayur Vihar Phase 1 Extens, Delhi 110091, India
关键词
Arginine clusters; Chaperones; Cryoprotectants; Drug excipients; Intrinsically disordered proteins; Liquid-liquid phase separation; Osmolytes; Protein aggregation; Protein chromatography; INTRINSICALLY DISORDERED PROTEINS; LIQUID PHASE-SEPARATION; HEXANUCLEOTIDE REPEAT; PROPOSED MECHANISM; AMINO-ACIDS; MEAN FORCE; AGGREGATION; STABILITY; CHARGE; STABILIZATION;
D O I
10.1016/j.bbrc.2024.149731
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
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页数:8
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