Dynamic Enhancement for Dual Active Bridge Converter with a Deadbeat Current Controller.

This paper investigates the deadbeat current controllers for isolated bidirectional dual-active-bridge dc-dc converter (IBDC), including the peak current mode (PCM) and middle current mode (MCM). The controller uses an enhanced single phase shift (ESPS) modulation method by exploiting pulse width as an extra control variable in addition to phase shift ratio. The control variables for PCM controllers are derived in detail and the two different current controllers are compared. A double-closed-loop control method is then employed, which could directly control the high-frequency inductor current and eliminate the transient DC current bias of the transformer. Furthermore, load feedforward was introduced to further enhance the dynamic of the converter. With the proposed control method, the settling time could be reduced within several PWM cycles during load disturbance without transient DC current bias. A 5 kW IBDC converter prototype was built and the settling time of 6 PWM cycles during load change with voltage regulation mode was achieved, which verifies the superior dynamic performance of the control method.

Isolation, physicochemical, and structure-function relationship of the hydrophobic variant of Fc-fusion proteins that bind to TNF-α receptor, HS002 and HS002A.

HS002 is the recombinant human tumor necrosis factor-α receptor Ⅱ: IgG Fc fusion protein licensed in China to treat rheumatism and psoriasis. The aim of this study was to isolate and characterize the hydrophobic freeze-dried powder injection (HS002) and ampoule injection (HS002A) variants derived from proteins of the same sequence and then to explore the structure-function relationship. Extensive physicochemical and structural testing was performed during a side-by-side comparison of the monomer peak and variant. Then the TNF-α-related binding activity, cell biological activity and affinity with FcRn were analyzed. Finally, a transformation study of the hydrophobic variant was performed under serum-like redox conditions. This research revealed that HS002A has similar physicochemical and structure-function relationship profiles to those of HS002. The hydrophobic variant exhibited the presence of new incorrect disulfide bridging. At the same time, this novel disulfide scrambled species structure-function relationship was found to be the molecular basis for reduced TNF-α binding and cell biological activities. In addition, incorrect disulfide bridging was found to be reversible under serum-like redox conditions, restoring TNF-α binding and cell biological activities to almost normal levels, all of which indicate that the variant is probably irrelevant to clinical efficacy once the drug enters the bloodstream.