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Single crystals of Diglycine Picrate (DGLP) were grown by slow evaporation technique and the vibrational spectral analysis is carried out using FT Raman and FT-IR spectroscopy, supported by Density Functional Theoretical (DFT) computations to derive equilibrium geometry, vibrational wavenumbers and first hyperpolarizability. The vibrational spectra confirm the existence of NH3(+) in DGLP. The influence of Twisted Intramolecular Charge Transfer (TICT) caused by the strong ionic ground state hydrogen bonding between charged species making DGLP crystal to have the non-centrosymmetric structure has been discussed. The Natural Bond Orbital (NBO) analysis confirms the occurrence of strong intermolecular N-H⋯O hydrogen bond. The HOMO-LUMO energy gap and the first order hyperpolarizability were calculated and it supports the nonlinear optical activity of the Diglycine Picrate crystal., (Copyright © 2014 Elsevier B.V. All rights reserved.)

Fabrication of protein adhesive and resistant surfaces based on chitosan/polystyrene sulfonate (CHI/PSS) multilayer membranes is presented. Adsorption behavior of bovine serum albumin (BSA) and lysozyme to CHI/PSS multilayer was studied by simple adsorption method and under pressure driven (ultrafiltration) conditions. The protein incorporated membranes were characterized by FT-IR, UV-vis, SEM and AFM. The loading of proteins to the multilayer was found to be dependent on the nature of protein, pH, number of bilayers, methods of adsorption and time of adsorption. Simple adsorption resulted in BSA adhesive layers with some conformational changes at higher number of bilayers. Ultrafiltration leads to protein repellence at higher number of bilayers which is attributed to the presence of irremovable water. Lysozyme adsorption/sorption varied with pH. Surface coverage dominates at pH close to pI and at pH 5 under ultraflitration condition where as simple adsorption resulted in protein repellence at pI. The secondary structure of adsorbed lysozyme is preserved for a wide pH range (5-11). Desorption study of lysozyme adsorbed membranes at pH 8.8 was carried out to understand the adsorption/sorption of protein. Diffusion of the sorbed lysozyme from the inner layers to the surface is found to take place at lower concentrations of NaCl., (Copyright © 2012 Elsevier B.V. All rights reserved.)