RESUMO
Above-room-temperature polar magnets are of interest due to their practical applications in spintronics. Here we present a strategy to design high-temperature polar magnetic oxides in the corundum-derived A2BB'O6 family, exemplified by the non-centrosymmetric (R3) Ni3TeO6-type Mn(2+)2Fe(3+)Mo(5+)O6, which shows strong ferrimagnetic ordering with TC = 337â K and demonstrates structural polarization without any ions with (n-1)d(10)ns(0), d(0), or stereoactive lone-pair electrons. Density functional theory calculations confirm the experimental results and suggest that the energy of the magnetically ordered structure, based on the Ni3TeO6 prototype, is significantly lower than that of any related structure, and accounts for the spontaneous polarization (68â µC cm(-2)) and non-centrosymmetry confirmed directly by second harmonic generation. These results motivate new directions in the search for practical magnetoelectric/multiferroic materials.
RESUMO
Human serum albumin (HSA) plays a pivotal role in drug release from its delivery vehicles such as cyclodextrins (CDs) by binding to the drugs. Here molecular recognition and binding of a drug mimic (CD1) to HSA have been explored in a microfluidic channel when CD1 is encapsulated in ß-cyclodextrin (ßCD) and heptakis(2,3,6-tri-O-methyl)-ß-cyclodextrin (TRIMEB), respectively, to investigate whether change of the host vehicle modulate the rate of drug binding to the serum protein. Molecular recognition of ßCD encapsulated CD1 by HSA occurs by the conformational selection fit mechanism leading to rapid binding of CD1 to HSA (k1 ~ 700 s-11) when the ßCD/CD1 complex interacts with HSA. In contrary, HSA recognizes CD1 encapsulated in TRIMEB by an induced fit mechanism leading to a significantly slower binding rate (k1 ~ 20.8 s-1) of the drug mimic to the protein. Thus molecular recognition controls the rate of HSA binding by CD1 which in turn modulates the rate of delivery of the drug mimic from its macrocyclic hosts. The remarkable change in the molecular recognition pathway of CD1 by HSA, upon change of the host from ßCD to TRIMEB, originates from significantly different conformational flexibility of the host/drug mimic complexes.