Cadmium sulphide (CdS) nanoparticles were grown by the reaction of sodium sulphide (Na₂S) with Langmuir-Blodgett (LB) films of cadmium salts ofn-octadecylsuccinic acid (ODSU) and with LB films of ODSU in mixtures of octadecylamine and octadecyl alcohol. The results indicate that heterogeneous nucleation and aggregation in the pure ODSU LB films due to processes like Ostwald ripening are destabilized by the presence of the long-chain amine and alcohol in mixed systems. CdS nanoparticles in the LB films were monitored by UV-visible absorption spectra, which allow an estimation of the size of the particles. The morphology, size and nature of the nanocrystallites formed depend on whether the sulphidation was done on the pure film or in the mixed films. It is seen that particles of size around 1.6 nm were formed in ODSU/octadecylalcohol and ODSU/ octadecylamine mixed LB films while in pure ODSU films the size was about 2.7 nm. These films showed typical needle-shaped structures, as observed by the optical microscopic technique. Mean size and morphology were confirmed by transmission and scanning electron microscopy, while selective area electron diffraction patterns showed six-fold symmetry and indicated that the CdS crystals grow epitaxially with respect to the monolayer. Further, the crystallisation enhanced in the mixed LB films showed a characteristic zinc oxide (Wurtzite) structure compared with the pure ODSU matrix.

Spreading behaviour of the dimeric surfactant polyethylene-glycoldistearate (PEGDS) monolayer at air/water interface has been studied using surface pressure-area (π-A) isotherms as a function of temperature. The isotherms show a plateau suggesting a transition between a liquid expanded (LE) and a condensed state. The condensed state possibly arises due to nucleation and growth of multilayers from the monolayer. Isobaric measurements of bothA-T and π-T at constant area show transitions atT = 295 K. These plots suggest a melting followed by formation of condensed microcrystallites. Structure optimization carried out using various angles of orientation of the alkyl tails with respect to the backbone in PEGDS reveals tilt transitions of the tails in different states which can be related to the packing behaviour seen in the isotherms. Optical microscopy has been used to confirm the structures in these states.

Copper sulphide clusters were prepared in Langmuir-Blodgett films of copper complexes of amphiphilic Schiff bases-3,4-dimethoxy-N-benzylidene hexadeylamine (I) and 3,4-dimethoxy-N-benzylidene-4’-(hexadecylamino) benzylamine (II) The clusters obtained were analysed using UV-Vis spectroscopy and optical microscopy. Brewster angle microscopic studies on monolayers ofI andII at air/water interface showed formation of needle-like domains which seem to cluster faster inI than inII. Atomic force microscopy (AFM) studies also showed fairly uniform sized clusters inII whereas in the case ofI they seem to show varying sizes. From the results it is concluded that π-elongation in the polar head groups leads to controlled cluster sizes in compoundII as compared to those in compoundI.

Cadmium complex ofn-octadecyl succinic acid (ODSA) in Langmuir films at air/water interface has been studied using surface pressure-molecular area (π - A) and surface potential-molecular area (ΔV - A) isotherms. The metal complex formed, transferred as LB film onto solid substrates, was analysed using FT-IR and was subjected to sulphidation reaction. Antisymmetric and symmetric carboxylate stretching vibrations have been used to determine the nature of the ODSA/cation complexes. CdS formed after sulphidation of the cadmium complex (ODSACd) showed possible single-electron phenomenon indicating the nanosized nature of clusters formed. Atomic Force Microscopy (AFM) measurements carried out confirmed the size of these CdS clusters.

Binding energies of the interaction of collagen like triple helical peptides with a series of polyphenols, viz. gallic acid, catechin, epigallocatechingallate and pentagalloylglucose have been computed using molecular modelling approaches. A correlation of calculated binding energies with the interfacial molecular volumes involved in the interaction is observed. Calculated interface surface areas for the binding of polyphenols with collagen-like triple helical peptides vary in the range of 60–210 Ų and hydrogen bond lengths vary in the range of 2.7–3.4 Å. Interfacial molecular volumes can be calculated from the solvent inaccessible surface areas and hydrogen bond lengths involved in the binding of polyphenols to collagen. Molecular aggregation of collagen in the presence of some polyphenols and chromium (III) salts has been probed experimentally in monolayer systems. The monolayer arrangement of collagen seems to be influenced by the presence of small molecules like formaldehyde, gluteraldehyde, tannic acid and chromium (III) salts. A fractal structure is observed on account of two-dimensional aggregation of collagen induced by tanning species. Atomic force microscopy has been employed to probe the topographic images of two-dimensional aggregation of collagen induced by chromium (III) salts. A case is made that long-range ordering of collagen by molecular species involved in its stabilisation is influenced by molecular geometries involved in its interaction with small molecules.

Cobalt oxides were prepared by three different methods: (1) by reacting cobalt nitrate with oxalic acid, (2) co-precipitating cobalt nitrate with sodium carbonate, and (3) using sodium dodecyl sulphate as organic surfactant. All three samples were characterized before and after calcination by solvent extraction and the resulting products examined by IR spectroscopy. In the case of method 3, the removal of surfactant was followed by TGA studies. Products from all three methods were identified by XRD. Peaks in low angle XRD indicate the porous nature of the oxides. The morphology of the pores was studied by transmission electron microscopy. Some irregular pore structures were obtained for samples from methods 1 and 2, with an average size of 4–6 nm. Only the product from method 3 using SDS as template showed ordered structure and optimum size, and Brunauer-Emmet-Teller surface areas of the as-prepared, as well as the treated samples, exhibited H3 type hysteresis. The samples from the three methods were used as catalysts in the oxidation reaction of cyclohexane under mild conditions and the catalytic efficiency of the cobalt oxide was comparable with mesoporous cobalt oxides.

Curcumin is a widely used therapeutic agent with a wide spectrum of biological and physiological applications like wound healing and interacts with the skin protein, collagen. This work reports the effect of curcumin on various physico-chemical properties of collagen. The results suggest that significant changes in viscosity and surface tension occur on collagen interacting with curcumin. Secondary structure analysis using circular dichroism shows that curcumin does not alter the triple helical structure of collagen. Increasing concentration of curcumin resulted in aggregation of the protein. Further, curcumin imparts high level of thermal stability to collagen with shrinkage temperature of collagen increasing from 60 to 90°C.

The effect of additives like curcumin and surfactants on the self-assembly of collagen from a simple 2-dimensional system of Langmuir films of the protein at air/solution interface has been attempted in this study using quartz crystal microbalance (QCM) and dynamic surface tensiometer. Though pure curcumin is not surface active, a synergistic effect of collagen with curcumin seems to lead to enhanced surface activity in the protein. In general, the presence of additives, increases the surface activity of collagen even for the lowest concentration and the largest change in surface activity is seen for collagen with sodium dodecyl sulfate (SDS). The results suggest interplay between the unexposed hydrophobic groups, and the opening out and solvation of the more charged or polar groups at the surface leading to aggregation followed by self-assembly. Modulation of aggregation at interface in collagen due to these additives may be an approach that could be explored for possible applications in bio-materials and for delivery of protein-drug complexes.