General method to stabilize mesophilic proteins in hyperthermal water.

ABSTRACT: The stability of protein structures and biological functions at normal temperature is closely linked with the universal aqueous environment of organisms. Preserving bioactivities of proteins in hyperthermia water would expand their functional capabilities beyond those in native environments. However, only a limited number of proteins derived from hyperthermophiles are thermostable at elevated temperatures. Triggered by this, here we describe a general method to stabilize mesophilic proteins in hyperthermia water. The mesophilic proteins, protected by amphiphilic polymers with multiple binding sites, maintain their secondary and tertiary structures after incubation even in boiling water. This approach, outside the conventional environment for bioactivities of mesophilic proteins, provides a general strategy to dramatically increase the T_m (melting temperature) of mesophilic proteins without any changes to amino sequences of the native proteins. Current work offers a new insight with protein stability engineering for potential application, including vaccine storage and enzyme engineering.

SUBMITTER: Xin X 

PROVIDER: S-EPMC8169989 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature