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Reexamining the diverse functions of arginine in biochemistry.
Gupta, Munishwar Nath; Uversky, Vladimir N.
Afiliação
  • Gupta MN; Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology, Hauz Khas, New Delhi, 110016, India. Electronic address: mn7gupta@gmail.com.
  • Uversky VN; Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Institute for Biological Instrumentation, Institutskaya Str., 7, Pushchino, Moscow Region, 142290, Russia; Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, 33612, USA. Electronic address: vuversky@usf.edu.
Biochem Biophys Res Commun ; 705: 149731, 2024 04 23.
Article em En | MEDLINE | ID: mdl-38432110
ABSTRACT
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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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Arginina Idioma: En Ano de publicação: 2024 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Arginina Idioma: En Ano de publicação: 2024 Tipo de documento: Article