This study demonstrates the fabrication and characterization of chicken egg albumen-based bio-memristors. By introducing egg albumen as an insulator to fabricate memristor devices comprising a metal/insulator/metal sandwich structure, significant bipolar resistive switching behavior can be observed. The 1/f noise characteristics of the albumen devices were measured, and results suggested that their memory behavior results from the formation and rupture of conductive filaments. Oxygen diffusion and electrochemical redox reaction of metal ions under a sufficiently large electric field are the principal physical mechanisms of the formation and rupture of conductive filaments; these mechanisms were observed by analysis of the time-of-flight secondary ion mass spectrometry (TOF-SIMS) and resistance–temperature (R–T) measurement results. The switching property of the devices remarkably improved by heat-denaturation of proteins; reliable switching endurance of over 500 cycles accompanied by an on/off current ratio (Ion/off) of higher than 103 were also observed. Both resistance states could be maintained for a suitably long time (>104 s). Taking the results together, the present study reveals for the first time that chicken egg albumen is a promising material for nonvolatile memory applications.

Articular cartilage imaging of the knee on a 3.0 T MR scanner shows increased SNR and CNR efficiencies compared to a 1.5 T scanner, where SSFP-based techniques show the highest increase in SNR and CNR efficiency. There was no difference between average cartilage thickness measurements performed at the 1.5 T and 3.0 T scanners or between the three different sequences.

MF and SHG microscopy provides three-dimensional structural analysis of keratoconus ex vivo. It may provide important morphologic information for the investigation of the pathogenesis of keratoconus and may have potential in a clinical setting as an in vivo diagnostic and monitoring system for advancing keratoconus.

Collagen shrinkage associated with denaturation from thermal treatment has a number of important clinical applications. However, individualized treatment is hindered by the lack of reliable noninvasive methods to monitor the process of collagen denaturation. We investigate the serial changes of collagen denaturation from thermal treatment of rat tail tendons at 58 degrees C by use of second harmonic generation (SHG) microscopy. We find that rat tail tendon shrinks progressively from 0 to 9 min of thermal treatment, and remains unchanged in length upon further thermal treatment. The SHG intensity also decreases from 0 to 9 min of thermal treatment and becomes barely detectable from further thermal treatment. Collagen shrinkage and the SHG intensity are well correlated in a linear model. In addition, SHG imaging reveals a tiger-tail-like pattern of collagen denaturation. The bands of denatured collagen progressively widen from increased thermal treatment and completely replace the adjacent bands of normal collagen after 9 min of thermal treatment. Our results show that collagen denaturation in rat tail tendon from thermal treatment is inhomogeneous, and that SHG intensity can be used to predict the degree of thermally induced collagen shrinkage. With additional development, this approach has the potential to be used in biomedical applications.

(99m)Tc HSA with serial scanning for up to 24 hours is reliable and useful for imaging PLE. Sites of protein loss may also be demonstrated. This imaging method is convenient, easy to perform, and yields results within 24 hours.