Kumar, Avishek

IIT Gandhinagar

AbstractSurface Patterning For Enhanced Protein StabilityAvishek KumarReduced activity of enzymes upon immobilization is a major challenge for the industrialuse of enzymes. Enzyme-surface interactions and interactions between the immobilizedenzymes are thought of as the main reasons for the reduced activity.In my research work, we study the thermal and structural stability of proteins ona patterned hydrophobic surface in the framework of a hydrophobic-polar (HP) latticemodel. Our results indicate that, while a homogeneous hydrophobic surface denatures theproteins, carefully patterned surfaces can dramatically increase the stability of adsorbedproteins. The size, shape, and the distance between surface patterns play a significantrole in determining the stability of proteins. When the spacing between the patterns islarge, maximum stability is observed when the surface pattern is complementary to theexposed hydrophobic domain of the protein, while at lower spacing, patterns with lowerhydrophobicity stabilize the protein more compared to the complementary pattern.The findings from the paper can be rationalized to design novel enzyme-specific sur-faces for immobilization with current enzymatic activity.(a) (b)Pictorial representation of the proposed idea. Blue represents hydrophilic groups. Orangerepresents hydrophobic groups. In bulk (i.e., water), the native structure of the proteinhas a hydrophobic core surrounded by the polar exterior. (A) Proteins lose their biolog-ical activity on interaction with the homogeneous hydrophobic surface upon adsorption.(B) Proteins retain its biological activity on interaction with the patterned surface uponadsorption.ii

Surface patterning for enhanced protein stability

https://repository.iitgn.ac.in//bitstream/123456789/4694/1/T00420.pdf

Surface patterning for enhanced protein stability

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IIT Gandhinagar