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. 2020 Aug 3;21(15):5544.
doi: 10.3390/ijms21155544.

Dairy-Inspired Coatings for Bone Implants from Whey Protein Isolate-Derived Self-Assembled Fibrils

Rebecca Rabe  1 , Ute Hempel  2 , Laurine Martocq  3 , Julia K Keppler  1   4 , Jenny Aveyard  5 , Timothy E L Douglas  3   6
Affiliations

Dairy-Inspired Coatings for Bone Implants from Whey Protein Isolate-Derived Self-Assembled Fibrils

Rebecca Rabe et al. Int J Mol Sci. .

Abstract

To improve the integration of a biomaterial with surrounding tissue, its surface properties may be modified by adsorption of biomacromolecules, e.g., fibrils. Whey protein isolate (WPI), a dairy industry by-product, supports osteoblastic cell growth. WPI's main component, β-lactoglobulin, forms fibrils in acidic solutions. In this study, aiming to develop coatings for biomaterials for bone contact, substrates were coated with WPI fibrils obtained at pH 2 or 3.5. Importantly, WPI fibrils coatings withstood autoclave sterilization and appeared to promote spreading and differentiation of human bone marrow stromal cells (hBMSC). In the future, WPI fibrils coatings could facilitate immobilization of biomolecules with growth stimulating or antimicrobial properties.

Keywords: bone; coating; fibril; stem cell; whey protein isolate.

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Conflict of interest statement

The authors declare no conflict of interest. The funders had no role in the design of the study; in the collection, analyses, or interpretation of data; in the writing of the manuscript, or in the decision to publish the results.

Figures

Figure 1
Figure 1
(a) Process of fibrils formation at pH 2 in solution; at pH 2, β-lactoglobulin denatures and hydrolyses at 90 °C. Specific peptides self-associate into the amyloid aggregates, which can consist of approximately three intertwined protofibrils. At pH 3.5, acid hydrolysis is reduced; therefore, non-hydrolyzed β-lactoglobulin assembles into worm-like aggregates, which are not amyloid but amyloid-like, and of different shape and morphology. (b) Fibrillar yield in solutions of different pH and (c) adsorption of whey protein isolate (WPI) fibrils on glass substrates.
Figure 2
Figure 2
(a) Contact angle (CA) measurements of uncoated and fibrillar coated samples with solution at pH 2 and pH 3.5 and SEM images of fibrillar coatings obtained at (b) pH 2 and (c) pH 3.5 (scale bar: 1 μm).
Figure 3
Figure 3
(a) Morphology of human bone marrow stromal cells (hBMSC) on (a) glass, (b) fibrillar coating (pH = 2), (c) fibrillar coating (pH = 3.5), 2 h after plating, and (d–f) TNAP staining at day 11 after plating, respectively. (g) TNAP activity on different substrates (day 11) and metabolic activity results at (h) day 2 and (i) day 4 after plating.
See this image and copyright information in PMC

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