A novel bifunctional protein PNU7 in CaCO polymorph formation: Vaterite stabilization and surface energy minimization.

Int J Biol Macromol

Ministry of Education Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, PR China; Department of Biotechnology and Biomedicine, Yangtze Delta Region Institute of Tsinghua University, Jiaxing, Zhejiang Province 314006, PR China; Zhejiang Provincial Key Laboratory of Applied Enzymology, Yangtze Delta Region Institute of Tsinghua University, 705 Yatai Road, Jiaxing 314006, PR China; Taizhou innovation center, Yangtze Delta Region Institute of Tsinghua University, Zhejiang 318000, PR China. Electronic address:

Published: December 2022

CaCO, which occurs in three crystalline anhydrous polymorphs named calcite, aragonite, and vaterite, is always found in mineralized skeletons or growing shells of many marine organisms. However, understanding how these organisms achieve this control has been a significant challenge in biomineralization. In this work, we proposed a novel vaterite stabilizer acidic matrix protein PNU7 that existed in both prism and nacre of Pinctada fucata, and identified its functional domain DDDDDDHDDVEETED. Our experiments reveal that PNU7 triggers a stable large vaterite formation with Mg deficiency even under low Ca. Increasing PNU7 in the calcium carbonate crystallization system with Mg leads to a significant shrinking in crystal size and rising in nucleation quantity. Moreover, it converts an atomically rough dome-like shape to a smooth sphere on unsiliconized glass. These effects rescind after removing the asp-rich region at the C-terminus. We also find that decreasing pnu7 mRNA in vivo leads to nacreous inner surface growth substantially lessened. Thus, PNU7 may not only supply vaterite in shell formation but also involve the nacreous regulation via surface energy minimization.

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http://dx.doi.org/10.1016/j.ijbiomac.2022.10.059DOI Listing

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