Protein nanopatterns templated on diblock copolymer surfaces and cell interactions

We have created patterns of proteins on the surfaces of microphase separated diblock copolymer films.


Poly(styrene-b-isoprene) creates a lamellar morphology. We found that bovine serum albumin (BSA) adsorbed preferentially on the poly(styrene) phase so that it was templated on the diblock copolymer surface. See: Liu, D., Wang, T., & Keddie, J. L. (2009). Protein Nanopatterning on Self-Organized Poly(styrene-b-isoprene) Thin Film Templates. Langmuir, 25(8), 4526-4534.

Patterns of proteins on surfaces affect the attachment and spreading of biological cells. Therefore, protein nanopatterns have applications in tissue engineering. We have found that Chinese Hamster Ovary (CHO) cells adhere and grow at higher densities on self-assembled, ring-like fibronectin protein nanopatterns (below, left), than on homogeneous fibronectin surfaces (right).

A likely explanation for this result is an increased clustering of proteins (integrins) with which the cells bind. To read more, see: Dan Liu, Che Azurahanim Che Abdullah, Richard P. Sear and Joseph L. Keddie, “Cell adhesion on nanopatterned fibronectin substrates.” Soft Matter (2010) 6(21), 5408-5416.

Ring-like protein pattern
Ring-like protein pattern
AFM image
This AFM image (2 mm x 2 mm in area) shows the two phases at a diblock copolymer film surface. One phase is poly(styrene), and the other phase is polyisoprene, which is a softer polymer. We have found that proteins preferentially adsorb on the poly(styre

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The Soft Matter Group
University of Surrey