Qingfang Deng

Dr. Qingfang Deng

orcid

Research Focus & Metrics

Academic Career Length

4Years (2023-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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9 February 2026 in Foods
Verified
Journal Article
Open access
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QDQingfang Deng
Qingfang Deng
YHYuanyuan Huang
Yuanyuan Huang
WXWen Xie
Wen Xie
JLJiawen Li
Jiawen Li
TTTing Tang
Ting Tang
XZXin Zhou
Xin Zhou
Background/Objectives: Mori fructus polysaccharides are key bioactive components with diverse activities, but structural characterization of homogeneous fractions remains limited, hindering insights into structure–activity relationships. This study addresses this gap by isolating and characterizing a homogeneous polysaccharide (MFP-III) from M. fructus. Methods: MFP-III, representing the final gel-filtration homogeneous fraction, was purified using defined procedures: DEAE-52 cellulose chromatography followed by Sephadex G-100 gel filtration. Purity and homogeneity were validated by high-performance liquid chromatography (HPLC). Structural characteristics were analyzed via HPLC, GC-MS, FTIR, and NMR spectroscopy. Meanwhile, hypoglycemic activity of MFP-III was evaluated. Results: MFP-III (94.2 ± 2.6%) has a molecular weight of approximately 6.83 kDa, primarily composed of rhamnose, arabinose, galactose, glucose, mannose, and galacturonic acid. Its backbone structure is presumed to be →2,4)-α-L-Rhap-(1 → 4)-α-D-GalpA-(1→, with branching units potentially attached to O-4. MFP-III demonstrated significant inhibitory activity against α-glucosidase (IC50 = 1.56 mg/mL) and α-amylase (IC50 = 2.07 mg/mL), stronger than acarbose at equivalent concentrations. Conclusions: The findings provide preliminary insights into the hypoglycemic structure–activity relationship of MFP-III, providing data support for the development of blood glucose-lowering natural inhibitors, and offering a theoretical foundation for advancing the application of polysaccharides from other sources.

21 June 2023 in Preprints.org
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Preprint
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FMFengwei MA
Fengwei MA
QWQihua Wen
Qihua Wen
QDQingfang Deng
Qingfang Deng
YLYihao Lu
Yihao Lu
BZBuyan Zhang
Buyan Zhang
SXSU XU
SU XU
Selenium (Se) is an essential trace element for human beings and Se supplementation is of great significance. In this paper, high selenized Gastrodia elata Blume Polysaccharides (SeGEP) were obtained through pre-sulfation before conducting the selenylation modification process, which owned a maximum Se content reach to 2.29%. UV, FT-IR, NMR, SEM, EDX, HPLC, size-exclusion chromatography and periodate oxidation analysis showed that the seleninic group had been successfully introduced into GEP with the substitution position at C-6 of glucose. Immunostimulating assays were conducted in vitro and in vivo on RAW 264.7 cells and cyclophosphamide (CTX)-induced mice model, respectively. The results showed that Se-GEP enhanced RAW264.7 cells proliferation, cell phagocytosis, and secretion of nitric oxide (NO) and interleukin (IL)-1β factors. In addition, Se-GEP enhanced the immunologic activity of CTX-treated mice by increasing the spleen and thymus indices, enhancing the phagocytic function, and activating both Th1 and Th2 lymphocytes. The current outcome also suggested that Se-GEP with covalently bonding Se group possessing increased safety and has a potential dietary selenium nutrient for improving human immunity.

1 April 2026 in Antioxidants
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Journal Article
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QDQingfang Deng
Qingfang Deng
BJBaitong Jing
Baitong Jing
RCRuhai Chen
Ruhai Chen
YCYang Cao
Yang Cao
XZXiaomei Zhou
Xiaomei Zhou
XZXin Zhou
Xin Zhou
Alcohol-associated liver disease (ALD) is a prevalent chronic liver disease worldwide, with unclear pathogenesis and limited effective treatments. Mori Fructus polysaccharide (MFP-1) exhibits good therapeutic potential for ALD, but its mechanism remains unclear. This study aims to elucidate how MFP-1 mitigates ALD. An integrated multi-omics approach, encompassing quantitative proteomics, metabolomics, and lipidomics, was employed to systematically characterize the hepatic response to MFP-1 in ALD. MFP-1 coordinates metabolic reprogramming by regulating fatty acid synthesis and β-oxidation. It also enhances branched-chain amino acid catabolism via the 2-oxocarboxylic acid pathway, optimizing energy generation and amino acid utilization. MFP-1 protects against ALD by simultaneously targeting multiple metabolic vulnerabilities. These findings elucidate the mechanistic basis of MFP-1’s hepatoprotective effects and highlight its potential for improving ALD.