Organized assemblies of capsules of haemoglobin (Hb), in the size range of 0.1 to 0.3 in Langmuir films have been studied at air/water interface below and above the isoelectric point. Spread films of these organizates suggest that there is no expulsion of individual particles or particle assemblies at the interface and the particles are stable. Dynamic surface tension and the associated dilational and shear visco-elasticity in these films suggest that the capsules are highly elastic. Multilayer films of the capsules using Langmuir-Blodgett technique have been fabricated by sequential deposition on solid surfaces. These films have been characterized by circular dichroism spectroscopy (CD), atomic force microscopy (AFM), quartz crystal microbalance (QCM) and Fourier transform infrared with reflection absorption spectroscopy (FTIR-RAS). No appreciable change in the secondary structural features of Hb is seen from CD studies indicating the stability of the protein in these organized assemblies. Sizes of these capsules change near the isoelectric point and large swollen multi-walled capsules are formed. The elastic films of capsules of Hb provide a useful post preparation approach for modification of the surface roughness, porosity, and permeability of pre-assembled polypeptide microcapsules. [Figure not available: see fulltext.] © 2013 Indian Academy of Sciences.
CITATION STYLE
Maheshkumar, J., & Dhathathreyan, A. (2013). Langmuir and Langmuir-Blodgett films of capsules of haemoglobin at air/water and solid/air interfaces. Journal of Chemical Sciences, 125(2), 219–227. https://doi.org/10.1007/s12039-013-0370-5
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