Synthesis of robust underwater glues from common proteins via unfolding-aggregating strategy

Yongchun Liu, Ke Li, Juanhua Tian, Aiting Gao, Lihua Tian, Hao Su, Shuting Miao, Fei Tao, Hao Ren, Qingmin Yang, Jing Cao and Peng Yang ()
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Yongchun Liu: Shaanxi Normal University
Ke Li: Xi’an Medical University
Juanhua Tian: The Second Affiliated Hospital of Xi’an Jiaotong University
Aiting Gao: Shaanxi Normal University
Lihua Tian: Shaanxi Normal University
Hao Su: Shaanxi Normal University
Shuting Miao: Shaanxi Normal University
Fei Tao: Shaanxi Normal University
Hao Ren: Shaanxi Normal University
Qingmin Yang: Shaanxi Normal University
Jing Cao: Northwestern Polytechnical University
Peng Yang: Shaanxi Normal University

Nature Communications, 2023, vol. 14, issue 1, 1-15

Abstract: Abstract Underwater adhesive proteins secreted by organisms greatly inspires the development of underwater glue. However, except for specific proteins such as mussel adhesive protein, barnacle cement proteins, curli protein and their related recombinant proteins, it is believed that abundant common proteins cannot be converted into underwater glue. Here, we demonstrate that unfolded common proteins exhibit high affinity to surfaces and strong internal cohesion via amyloid-like aggregation in water. Using bovine serum albumin (BSA) as a model protein, we obtain a stable unfolded protein by cleaving the disulfide bonds and maintaining the unfolded state by means of stabilizing agents such as trifluoroethanol (TFE) and urea. The diffusion of stabilizing agents into water exposes the hydrophobic residues of an unfolded protein and initiates aggregation of the unfolded protein into a solid block. A robust and stable underwater glue can thus be prepared from tens of common proteins. This strategy deciphers a general code in common proteins to construct robust underwater glue from abundant biomass.

Date: 2023
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DOI: 10.1038/s41467-023-40856-z

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