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This paper presents the synthesis of iron(III)-aluminum(III) mixed oxide with some of its physicochemical characteristics and fluoride adsorption behavior thereon. Results showed that the optimum initial pH for fluoride adsorption is 4.0-10.0, and the equilibrium time required is 1.5 h. The isotherm data follow the order Redlich-Peterson g Langmuir > Freundlich > Temkin. The Langmuir monolayer adsorption capacity of the adsorbent is determined to be 17.73 mg/g, which is higher than that of either of the pure oxides. The enthalpy change (∆H°) and entropy change (∆S°) for the adsorption reaction are +29.31 kJ/mol and +116.75 J mol -1 K -1 , respectively. The adsorption is endothermic in nature. The kinetics follows a pseudo-second-order rate equation, and the reaction rate is a multistage-controlled diffusion process. The activation energy for this adsorption reaction is 6.35 kJ/mol.

Wound healing is a common physiological process which consists of a sequence of molecular and cellular events that occur following the onset of a tissue lesion in order to reconstitute barrier between body and external environment. The inherent properties of hydrogels allow the damaged tissue to heal by supporting a hydrated environment which has long been explored in wound management to aid in autolytic debridement. However, chronic non-healing wounds require added therapeutic features that can be achieved by incorporation of biomolecules and supporting cells to promote faster and better healing outcomes. In recent decades, numerous hydrogels have been developed and modified to match the time scale for distinct stages of wound healing. This review will discuss the effects of various types of hydrogels on wound pathophysiology, as well as the ideal characteristics of hydrogels for wound healing, crosslinking mechanism, fabrication techniques and design considerations of hydrogel engineering. Finally, several challenges related to adopting hydrogels to promote wound healing and future perspectives are discussed.

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Noncovalent interactions in soybean agglutinin (SBA) were studied on an electrospray ionization (ESI) time-of-flight mass spectrometer constructed recently at the University of Manitoba. The high m/z range and high sensitivity of the instrument together with mild ESI interface conditions turned out to be ideal for detecting this noncovalently bonded tetrameric protein (MW approximately 116,000 Da) in low charge states (z = 23 to 27). By altering the acetonitrile content of the SBA solutions it was shown that the observed SBA tetramers are due to structurally specific noncovalent associations in solution. Octamers and dodecamers (MW approximately 350,000 Da) were also detected. Information on the quaternary structure of the tetramers was obtained by analyzing the fragment-ion spectrum resulting from the collision-induced dissociation of the tetramer ions.

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