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Your search keyword '"Peng, Chune"' showing total 21 results
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21 results on '"Peng, Chune"'

7. Development of Glycosylation-Modified D PPA-1 Compounds as Innovative PD-1/PD-L1 Blockers: Design, Synthesis, and Biological Evaluation.

Author

Deng, Peng, Dong, Xiaodan, Wu, Ziyuan, Hou, Xixi, Mao, Longfei, Guo, Jingjing, Zhao, Wenshan, Peng, Chune, Zhang, Zhe, and Peng, Lizeng

Subjects
PROGRAMMED cell death 1 receptors, PROGRAMMED death-ligand 1, IMMUNE checkpoint proteins, PEPTIDES, GLYCOPEPTIDES, T cells, GENE enhancers
Abstract

In the context of peptide drug development, glycosylation plays a pivotal role. Accordingly, L-type peptides were synthesized predicated upon the PD-1/PD-L1 blocker DPPA-1. Subsequent glycosylation resulted in the production of two distinct glycopeptides, D-glu-LPPA-1 and D-gal-LPPA-1, by using D-glucose (D-glu) and D-galactose (D-gal), respectively, during glycosylation. Both glycopeptides significantly inhibited the interaction between PD-1 and PD-L1, and the measured half maximal inhibitory concentrations (IC50s) were 75.5 μM and 101.9 μM for D-glu-LPPA-1 and D-gal-LPPA-1, respectively. Furthermore, D-gal-LPPA-1 displayed a pronounced ability to restore T-cell functionality. In an MC38 tumor-bearing mouse model, D-gal-LPPA-1 demonstrated a significant inhibitory effect. Notably, D-gal-LPPA-1 substantially augmented the abundance and functionality of CD8+ T cells in the tumor microenvironment. Additionally, in the lymph nodes and spleens, D-gal-LPPA-1 significantly increased the proportion of CD8+ T cells secreting interferon-gamma (IFN-γ). These strong findings position D-gal-LPPA-1 as a potent enhancer of the antitumor immune response in MC38 tumor-bearing mice, underscoring its potential as a formidable PD-1/PD-L1 blocking agent. [ABSTRACT FROM AUTHOR]

Published
2024
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20. Preparation and properties of (Bi1/2Na1/2)TiO3–Ba(Ti,Zr)O3 lead-free piezoelectric ceramics

Author

Peng, Chune, Li, Jing-Feng, and Gong, Wen

Subjects
*CERAMICS, *POWDER metallurgy, *PIEZOELECTRICITY, *PEROVSKITE
Abstract

Abstract: Lead-free piezoelectric ceramics based on bismuth sodium titanate (Bi1/2Na1/2)TiO3 (BNT)–barium zirconate titanate Ba(Ti,Zr)O3 (BZT) were prepared by using a modified sintering process. The BNT–BZT ceramics sintered at 1180 °C for 3 h in air showed perovskite structure with high densities around 5.32–5.82 g/cm3 (~97% as relative density). Focusing on the morphotropic phase boundary (MPB) of BNT–BZT system, the ferroelectric, dielectric and piezoelectric properties of the BNT–BZT ceramics were studied. In the case of (Bi1/2Na1/2)TiO3–xBa(Ti0.942Zr0.058)O3 solid solution ceramics, the maximum of piezoelectric constant d 33 (147 pC/N) was obtained for the ceramic with 9% BZT, which has a tetragonal phase near the MPB region. The BNT–BZT system was expected to be a new and promising candidate for lead-free piezoelectric ceramics. [Copyright &y& Elsevier]

Published
2005
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21. Identification and functional analysis of phosphorylation residues of the ArabidopsisBOTRYTIS-INDUCED KINASE1

Author

Xu, Jinhua, Wei, Xiaochao, Yan, Limin, Liu, Dan, Ma, Yuanyuan, Guo, Yu, Peng, Chune, Zhou, Honggang, Yang, Cheng, Lou, Zhiyong, and Shui, Wenqing

Abstract

ArabidopsisBOTRYTIS-INDUCED KINASE1 (BIK1) is a receptor-like cytoplasmic kinase acting early in multiple signaling pathways important for plant growth and innate immunity. It is known to form a signaling complex with a cell-surface receptor FLS2 and a co-receptor kinase BAK1 to transduce signals upon perception of pathogen-associated molecular patterns (PAMPs). Although site-specific phosphorylation is speculated to mediate the activation and function of BIK1, few studies have been devoted to complete profiling of BIK1 phosphorylation residues. Here, we identified nineteen in vitroautophosphorylation sites of BIK1 including three phosphotyrosine sites, thereby proving BIK1 is a dual-specificity kinase for the first time. The kinase activity of BIK1 substitution mutants were explicitly assessed using quantitative mass spectrometry (MS). Thr-237, Thr-242 and Tyr-250 were found to most significantly affect BIK1 activity in autophosphorylation and phosphorylation of BAK1 in vitro. A structural model of BIK1 was built to further illustrate the molecular functions of specific phosphorylation residues. We also mapped new sites of FLS2 phosphorylation by BIK1, which are different from those by BAK1. These in vitroresults could provide new hypotheses for more in-depth in vivostudies leading to deeper understanding of how phosphorylation contributes to BIK1 activation and mediates downstream signaling specificity.

Published
2013
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