Interactions between bovine serum albumin and Langmuir films composed of charged and uncharged poly(N-isopropylacrylamide) block copolymers.
The thermoresponsive poly(N-isopropylacrylamide) (PNIPAAM) and NIPAAM block copolymer derivatives are attractive for drug delivery applications as they contract reversibly at lower critical solution temperatures (LCST) close to physiological conditions. In order to investigate biomaterial-protein compatibility, we have studied the interaction between PNIPAAM copolymer films spread at the air-water surface and bovine serum albumin (BSA) injected below the precompressed polymer films, using the Langmuir technique coupled with Brewster angle microscopy (BAM). A PNIPAAM homopolymer was applied together with a number of PNIPAAM-based di- and triblock copolymers, to assess effects of e.g., charge and hydrophobicity on protein-polymer interactions. The nature and strength of protein-polymer interaction was found to be tunable, ranging from complex formation (PNIPAAM homopolymer) to mixed monolayers and electrostatic cross-linking, according to the nature of the co-monomer. Results show that intercalation versus adsorption can be controlled through polymer composition.
Ugelstad Laboratory, Department of Chemical Engineering, Norwegian University of Science and Technology (NTNU), N-7491 Trondheim, Norway.
Sondre
S
Volden
Marit-Helen G
MH
Ese
Kaizheng
K
Zhu
Masahiro
M
Yasuda
Bo
B
Nyström
Wilhelm R
WR
Glomm
D000178:Acrylamides / Q000737:chemistry*; D000180:Acrylic Resins; D000818:Animals; D002417:Cattle; D057927:Hydrophobic and Hydrophilic Interactions; D011108:Polymers / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry*
D000178:Acrylamides; D000180:Acrylic Resins; D011108:Polymers; C052970:poly-N-isopropylacrylamide; D012710:Serum Albumin, Bovine