| 1. |
|
|
| 2. |
- Sood, Mohit, et al.
(author)
-
Low temperature (Zn,Sn)O deposition for reducing interface open-circuit voltage deficit to achieve highly efficient Se-free Cu(In,Ga)S2 solar cells
- 2022
-
In: Faraday discussions. - : Royal Society of Chemistry. - 1359-6640 .- 1364-5498. ; 239, s. 328-338
-
Journal article (peer-reviewed)abstract
- Cu(In,Ga)S-2 holds the potential to become a prime candidate for use as the top cell in tandem solar cells owing to its tunable bandgap from 1.55 eV (CuInS2) to 2.50 eV (CuGaS2) and favorable electronic properties. Devices above 14% power conversion efficiency (PCE) can be achieved by replacing the CdS buffer layer with a (Zn,Mg)O or Zn(O,S) buffer layer. However, the maximum achievable PCE of these devices is limited by the necessary high heating temperatures during or after buffer deposition, as this leads to a drop in the quasi-Fermi level splitting (qFLs) and therefore the maximum achievable open-circuit voltage (V-OC). In this work, a low-temperature atomic layer deposited (Zn,Sn)O thin film is explored as a buffer layer to mitigate the drop in the qFLs. The devices made with (Zn,Sn)O buffer layers are characterized by calibrated photoluminescence and current-voltage measurements to analyze the optoelectronic and electrical characteristics. An improvement in the qFLs after buffer deposition is observed for devices prepared with the (Zn,Sn)O buffer deposited at 120 degrees C. Consequently, a device with a V-OC value above 1 V was achieved. A 14% PCE is externally measured and certified for the best solar cell. The results show the necessity of developing a low-temperature buffer deposition process to maintain and translate absorber qFLs to device V-OC.
|
|
| 3. |
- Suryawanshi, Rahul K., et al.
(author)
-
Putative targeting by BX795 causes decrease in protein kinase C protein levels and inhibition of HSV1 infection
- 2022
-
In: Antiviral Research. - : Elsevier. - 0166-3542 .- 1872-9096. ; 208
-
Journal article (peer-reviewed)abstract
- Herpes simplex virus type-1 (HSV1) exploits cellular machinery for its own replicative advantage. Current treatment modalities against HSV1 cause toxicity and drug resistance issues. In the search for alternative forms of treatment, we have uncovered a small molecule, BX795, as a candidate drug with strong antiviral potential owing to its multitargeted mode of action. In this study, we show that in addition to a previously known mechanism of action, BX795 can directly interact with the proviral host factor protein kinase C (PKC) in silico. When administered to HSV1 or mock infected human corneal epithelial (HCE) cells, BX795 significantly reduces the protein level and perinuclear localization of proviral PKC-alpha and PKC-zeta isoforms. This activity closely mimics that of a known PKC inhibitor, Bisindolylmaleimide I (BIM I), which also inhibits viral replication. Taken together our studies demonstrate a previously unknown mechanism by which BX795 exerts its antiviral potential.
|
|
