No abstract

Rapid improvement of wearable electronics stimulates the demands for the matched functional devices and energy storage devices. Meanwhile, wearable microsystem requires every parts possessing high compressibility to accommodate large-scale mechanical deformations and complex conditions. In this work, a general carbon nanotube-polydimethylsiloxane (CNT-PDMS) sponge electrode is fabricated as the elementary component of the compressible system. CNT-PDMS sponge performs high sensitivity as a piezoresistance sensor, which is capable of detecting stress repeatedly and owns great electrochemical performance as a compressible supercapacitor which maintains stably under compressive strains, respectively. Assembled with the piezoresistance sensor and the compressible supercapacitor, such highly compressible integrated system can power and modulate the low-power electronic devices reliably. More importantly, attached to the epidermal skin or clothes, it can detect human motions, ranging from speech recognition to breathing record, thus showing feasibility in real-time health monitor and human-machine interfaces.

The silent information regulator sirtuin 1 (SIRT1) protein, a highly conserved NAD+-dependent deacetylase belonging to the sirtuin family, is a post-translational regulator that plays a role in modulating inflammation. SIRT1 affects multiple biological processes by deacetylating a variety of proteins including histones and non-histone proteins. Recent studies have revealed intimate links between SIRT1 and inflammation, while alterations to SIRT1 expression and activity have been linked to inflammatory diseases. In this review, we summarize the mechanisms that regulate SIRT1 expression, including upstream activators and suppressors that operate on the transcriptional and post-transcriptional levels. We also summarize factors that influence SIRT1 activity including the NAD+/NADH ratio, SIRT1 binding partners, and post-translational modifications. Furthermore, we underscore the role of SIRT1 in the development of inflammation by commenting on the proteins that are targeted for deacetylation by SIRT1. Finally, we highlight the potential for SIRT1-based therapeutics for inflammatory diseases.