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dc.contributor.authorJain, G.
dc.contributor.authorPendola, M.
dc.contributor.authorHuang, Y.
dc.contributor.authorJuan Colas, J.
dc.contributor.authorGebauer, Denis
dc.contributor.authorJohnson, S.
dc.contributor.authorEvans, J.
dc.date.accessioned2018-05-18T08:00:46Z
dc.date.available2018-05-18T08:00:46Z
dc.date.created2018-05-18T00:23:23Z
dc.date.issued2017
dc.identifier.citationJain, G. and Pendola, M. and Huang, Y. and Juan Colas, J. and Gebauer, D. and Johnson, S. and Evans, J. 2017. Functional Prioritization and Hydrogel Regulation Phenomena Created by a Combinatorial Pearl-Associated Two-Protein Biomineralization Model System. Biochemistry. 56 (28): pp. 3607-3618.
dc.identifier.urihttp://hdl.handle.net/20.500.11937/68096
dc.identifier.doi10.1021/acs.biochem.7b00313
dc.description.abstract

In the nacre or aragonitic layer of an oyster pearl, there exists a 12-member proteome that regulates both the early stages of nucleation and nanoscale-to-mesoscale assembly of nacre tablets and calcitic crystals from mineral nanoparticle precursors. Several approaches to understanding protein-associated mechanisms of pearl nacre formation have been developed, yet we still lack insight into how protein ensembles or proteomes manage nucleation and crystal growth. To provide additional insights, we have created a proportionally defined combinatorial model consisting of two pearl nacre-associated proteins, PFMG1 and PFMG2 (shell oyster pearl nacre, Pinctada fucata) whose individual in vitro mineralization functionalities are distinct from one another. Using scanning electron microscopy, atomic force microscopy, Ca(II) potentiometric titrations, and quartz crystal microbalance with dissipation monitoring quantitative analyses, we find that at 1:1 molar ratios, rPFMG2 and rPFMG1 co-aggregate in specific molecular ratios to form hybrid hydrogels that affect both the early and later stages of in vitro calcium carbonate nucleation. Within these hybrid hydrogels, rPFMG2 plays a role in defining protein co-aggregation and hydrogel dimension, whereas rPFMG1 defines participation in nonclassical nucleation processes; both proteins exhibit synergy with regard to surface and subsurface modifications to existing crystals. The interactions between both proteins are enhanced by Ca(II) ions and may involve Ca(II)-induced conformational events within the EF-hand rPFMG1 protein, as well as putative interactions between the EF-hand domain of rPFMG1 and the calponin-like domain of rPFMG2. Thus, the pearl-associated PFMG1 and PFMG2 proteins interact and exhibit mineralization functionalities in specific ways, which may be relevant for pearl formation.

dc.publisherAmerican Chemical Society
dc.titleFunctional Prioritization and Hydrogel Regulation Phenomena Created by a Combinatorial Pearl-Associated Two-Protein Biomineralization Model System
dc.typeJournal Article
dcterms.source.volume56
dcterms.source.number28
dcterms.source.startPage3607
dcterms.source.endPage3618
dcterms.source.issn0006-2960
dcterms.source.titleBiochemistry
curtin.departmentSchool of Molecular and Life Sciences (MLS)
curtin.accessStatusFulltext not available


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