interfaces group
publications members

Imprinting Langmuir monolayers and thin polymer films for protein recognition (done in collaboration with Prof. D.W. Britt, Utah State University)

Schematic of protein induced template formation in fluid films vs. an otherwise identical immobilized control film (from X.-Z. Du, V. Hlady and D. W. Britt: Langmuir monolayer approaches to protein recognition through molecular imprinting, Biosensors and Bioelectronics, 20 (10) (2005) 2053-2060.)

Schematic of protein imprinting in Langmuir monolayers.  The native PEG:SME:DOMA monolayer at the air/water interface (A) interacts with the protein to form imprints (B) that are complementary in shape and charge to the protein.  The monolayer is locked into place when transferred to a hydrophobic support (C), followed by removal of the template protein and rebinding studies (D). (from N. W. Turner, B. E. Wright, V. Hlady, and D. W. Britt: Formation of protein molecular imprints within Langmuir monolayers: A quartz crystal microbalance study, J. Colloid Interface Sci., 308 (2007) 71–80.)

Schematic representation of conformational protein molecular imprinting on a gold QCM crystal:  (A) The template isoform of the protein (black) and APBA (grey) are mixed together to form a complex (B).  Upon polymerisation this complex is trapped within a poly(APBA) matrix which is adsorbed onto a surface (C).  The template protein is extracted (D) to leave an imprint.  When challenged with the template isoform or an alternative isoform of the same protein the imprint favours the template (E).  The greater the difference between the protein structure used in the imprinting step and that used for rebinding, the less likely it is to bind (F). N.W. Turner, X. Liu, S.A. Piletsky, V. Hlady, and D.W. Britt, Recognition of conformational changes in beta-lactoglobulin by molecularly imprinted thin films. Biomacromolecules, 8(9) (2007) 2781-7.