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6
result(s) for
"Liang, Bor-Wei"
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Monolithic 3D integration of back-end compatible 2D material FET on Si FinFET
by
Liang, Bor-Wei
,
Li, Lain-Jong
,
Guan, Shi-Xian
in
639/925/357/1018
,
639/925/927/1007
,
Chemistry and Materials Science
2023
The performance enhancement of integrated circuits relying on dimension scaling (i.e., following Moore’s Law) is more and more challenging owing to the physical limit of Si materials. Monolithic three-dimensional (M3D) integration has been considered as a powerful scheme to further boost up the system performance. Two-dimensional (2D) materials such as MoS
2
are potential building blocks for constructing upper-tier transistors owing to their high mobility, atomic thickness, and back-end-of-line (BEOL) compatible processes. The concept to integrate 2D material-based devices with Si field-effect transistor (FET) is technologically important but the compatibility is yet to be experimentally demonstrated. Here, we successfully integrated an n-type monolayer MoS
2
FET on a p-type Si fin-shaped FET with 20 nm fin width via an M3D integration technique to form a complementary inverter. The integration was enabled by deliberately adopting industrially matured techniques, such as chemical mechanical planarization and e-beam evaporation, to ensure its compatibility with the existing 3D integrated circuit process and the semiconductor industry in general. The 2D FET is fabricated using low-temperature sequential processes to avoid the degradation of lower-tier Si devices. The MoS
2
n-FETs and Si p-FinFETs display symmetrical transfer characteristics and the resulting 3D complementary metal-oxide-semiconductor inverter show a voltage transfer characteristic with a maximum gain of ~38. This work clearly proves the integration compatibility of 2D materials with Si-based devices, encouraging the further development of monolithic 3D integrated circuits.
Journal Article
Ferroelectric transistors based on shear-transformation-mediated rhombohedral-stacked molybdenum disulfide
by
Chen, Fu-Xiang
,
Chen, Yi-Chun
,
Hu, Hsiang-Chi
in
639/301/1005/1007
,
639/301/357/1018
,
Computation
2024
To develop low-power, non-volatile computing-in-memory device using ferroelectric transistor technologies, ferroelectric channel materials with scaled thicknesses are required. Two-dimensional semiconductors, such as molybdenum disulfide (MoS
2
), equipped with sliding ferroelectricity could provide an answer. However, achieving switchable electric polarization in epitaxial MoS
2
remains challenging due to the absence of mobile domain boundaries. Here we show that polarity-switchable epitaxial rhombohedral-stacked (3R) MoS
2
can be used as a ferroelectric channel in ferroelectric memory transistors. We show that a shear transformation can spontaneously occur in 3R MoS
2
epilayers, producing heterostructures with stable ferroelectric domains embedded in a highly dislocated and unstable non-ferroelectric matrix. This diffusionless phase transformation process produces mobile screw dislocations that enable collective polarity control of 3R MoS
2
via an electric field. Polarization–electric-field measurements reveal a switching field of 0.036 V nm
−1
for shear-transformed 3R MoS
2
. Our sliding ferroelectric transistors are non-volatile memory units with thicknesses of only two atomic layers and exhibit an average memory window of 7 V with an applied voltage of 10 V, retention times greater than 10
4
seconds and endurance greater than 10
4
cycles.
Rhombohedral-stacked molybdenum disulfide with sliding ferroelectric behaviour can be used to create atomically thin ferroelectric transistors for computing-in-memory device applications.
Journal Article
Homoepitaxy of rhombohedral-stacked MoS2 with room temperature switchable ferroelectricity
by
Yi-Cheng, Chen
,
Chun-Liang, Lin
,
Ting-Hua, Lu
in
Bilayers
,
Chemical potential
,
Chemical synthesis
2022
The discovery of interfacial ferroelectricity in two-dimensional rhombohedral (3R)-stacked semiconductors opens up a new pathway for achieving ultrathin computing-in-memory devices. However, exploring ferroelectricity switching in natural 3R crystals is difficult due to lack of co-existing 3R stacking domains. Here, we present that MoS2 homoepitaxial patterns with 3R polytypic domains can manifest switchable ferroelectricity at room-temperature. Based on the diffusion limited aggregation theory, such MoS2 patterns are formed under the low Mo chemical potential and low temperature with respect to common chemical vapor deposition synthesis. The alternation of 3R polytypes in the MoS2 homoepitaxial patterns, observed by scanning transmission electron microscopy, accounts for ferroelectricity switching. The MoS2 field-effect transistors with 3R polytypic domains exhibit a repeatable counterclockwise hysteresis with gate voltage sweeping, an indication of ferroelectricity switching, and the memory window exceeds those measured for compact-shaped 3R bilayer devices. This work provides a direct growth concept for layered 3R-based ferroelectric memory.
The discovery of potential acetylcholinesterase inhibitors: A combination of pharmacophore modeling, virtual screening, and molecular docking studies
by
Lin, Hsin-Yi
,
Lu, Shin-Hua
,
Liu, Kung-Tien
in
Acetylcholinesterase - chemistry
,
Alzheimer Disease - drug therapy
,
Alzheimer Disease - enzymology
2011
Background
Alzheimer's disease (AD) is the most common cause of dementia characterized by progressive cognitive impairment in the elderly people. The most dramatic abnormalities are those of the cholinergic system. Acetylcholinesterase (AChE) plays a key role in the regulation of the cholinergic system, and hence, inhibition of AChE has emerged as one of the most promising strategies for the treatment of AD.
Methods
In this study, we suggest a workflow for the identification and prioritization of potential compounds targeted against AChE. In order to elucidate the essential structural features for AChE, three-dimensional pharmacophore models were constructed using Discovery Studio 2.5.5 (DS 2.5.5) program based on a set of known AChE inhibitors.
Results
The best five-features pharmacophore model, which includes one hydrogen bond donor and four hydrophobic features, was generated from a training set of 62 compounds that yielded a correlation coefficient of R = 0.851 and a high prediction of fit values for a set of 26 test molecules with a correlation of R
2
= 0.830. Our pharmacophore model also has a high Güner-Henry score and enrichment factor. Virtual screening performed on the NCI database obtained new inhibitors which have the potential to inhibit AChE and to protect neurons from Aβ toxicity. The hit compounds were subsequently subjected to molecular docking and evaluated by consensus scoring function, which resulted in 9 compounds with high pharmacophore fit values and predicted biological activity scores. These compounds showed interactions with important residues at the active site.
Conclusions
The information gained from this study may assist in the discovery of potential AChE inhibitors that are highly selective for its dual binding sites.
Journal Article
Fibronectin modulates the morphology of osteoblast-like cells (MG-63) on nano-grooved substrates
by
Liu, Hsuan-Liang
,
Lai, Juin-Yih
,
Yang, Jung-Yen
in
Actins - analysis
,
Alignment
,
Biocompatible Materials - metabolism
2009
Cell interactions with biomaterials are affected by surface topographic and chemical cues. Although it is well-known that nanometrical grooves/ridges structure modulates cellular spreading, elongation, and alignment, the combinational influence of surface topographic and chemical cues is not well studied. In this study, nano-textured silicon substrata with parallel ridges of 90, 250, or 500 nm wide, separated by grooves with equal width, were fabricated by electron beam lithography and dry etching techniques. Osteoblast-like cells, MG-63, were cultured on the patterned substrata with or without pre-adsorption of fibronectin. The cell morphology was imaged by scanning electron microscopy, and analyzed by image software. We found that FN coating initially modulated cellular spreading, length, and orientation on all types of grooved surfaces. However, after 24 h of culture, the cell morphology was not affected by FN coating on the 250-nm and 500-nm surfaces, while FN decreased cell alignment on the 90-nm surfaces. Our results suggest that surface chemical cues influence the initial cell-substratum contact, while the long-term cellular morphology is dictated by surface topographic cues.
Journal Article
Chemical Chaperone and Inhibitor Discovery: Potential Treatments for Protein Conformational Diseases
by
Hsuan-Liang Liu
,
Chih-Hung Huang
,
Wei-Bor Tsai
in
Health aspects
,
Medical research
,
Medicine, Experimental
2007
Jian-Hua Zhao1, Hsuan-Liang Liu1,2, Hsin-Yi Lin1,2, Chih-Hung Huang1,2, Hsu-Wei Fang1,2, Shiao-Shing Chen3, Yih Ho4, Wei-Bor Tsai5 and Wen-Yih Chen6 1Department of Chemical Engineering and Biotechnology, National Taipei University of Technology, 1 Sec. 3 ZhongXiao E. Rd., Taipei 10608. 2Graduate Institute of Biotechnology, National Taipei University of Technology, 1 Sec. 3 ZhongXiao E. Rd., Taipei, Taiwan 10608. 3Institute of Environmental Engineering and Management, National Taipei University of Technology, 1 Sec. 3 ZhongXiao E. Rd., Taipei, Taiwan 10608. 4School of Pharmacy, Taipei Medical University, 250 Wu-Hsing St., Taipei, Taiwan 110. 5Department of Chemical Engineering, National Taiwan University, 1 Sec. 4 Roosevelt Rd., Taipei, Taiwan 106. 6Department of Chemical and Materials Engineering, National Central University, 300 Jhongda Rd., Jhongli City, Taoyuan County, Taiwan 32001. Abstract: Protein misfolding and aggregation cause a large number of neurodegenerative diseases in humans due to (i) gain of function as observed in Alzheimer's disease, Huntington's disease, Parkinson's disease, and Prion's disease or (ii) loss of function as observed in cystic fi brosis and α1-antitrypsin defi ciency. These misfolded proteins could either lead to the formation of harmful amyloids that become toxic for the cells or to be recognized and prematurely degraded by the protein quality control system. An increasing number of studies has indicated that some low-molecular-weight compounds named as chemical chaperones can reverse the mislocalization and/or aggregation of proteins associated with human conformational diseases. These small molecules are thought to non-selectively stabilize proteins and facilitate their folding. In this review, we summarize the probable mechanisms of protein conformational diseases in humans and the use of chemical chaperones and inhibitors as potential therapeutic agents against these diseases. Furthermore, recent advanced experimental and theoretical approaches underlying the detailed mechanisms of protein conformational changes and current structure-based drug designs towards protein conformational diseases are also discussed. It is believed that a better understanding of the mechanisms of conformational changes as well as the biological functions of these proteins will lead to the development and design of potential interfering compounds against amyloid formation associated with protein conformational diseases.
Journal Article