更新于：2024-11-01

醇溶蛋白

更新于：2024-11-01

基本信息

别名-

简介-

关联

项与醇溶蛋白相关的药物

AG-017

靶点

醇溶蛋白

作用机制

醇溶蛋白刺激剂 [+2]

在研机构

Precigen, Inc.

原研机构

Precigen ActoBio, Inc.

在研适应症

乳糜泻

非在研适应症-

最高研发阶段临床1期

首次获批国家/地区-

首次获批日期1800-01-20

Kuma030

靶点

醇溶蛋白

作用机制

醇溶蛋白抑制剂

在研机构

University of Washington

原研机构

University of Washington

在研适应症

乳糜泻

非在研适应症-

最高研发阶段临床前

首次获批国家/地区-

首次获批日期1800-01-20

100 项与醇溶蛋白相关的临床结果

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100 项与醇溶蛋白相关的转化医学

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0 项与醇溶蛋白相关的专利（医药）

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681

项与醇溶蛋白相关的文献（医药）

2025-02-01·Food Chemistry

Effect of high-molecular-weight glutenin subunit deletion on gluten functionality and Chinese southern-type steamed bread quality

Article

作者: Jiang, Hao ; Wang, Pei ; Jiang, Dong ; Yang, Tao ; Zhou, Qin

High-molecular-weight glutenin subunit (HMW-GS) is key factor in gluten strength and end-use quality. However, the contribution of individual HMW-GS on dough strength and Chinese southern-type steamed bread (CSTSB) quality remained unknown. In this study, we investigated the effects of individual HMW-GS deletion on CSTSB quality. The HMW-GS deletion led to significant reductions in glutenin/gliadin ratios, disulfide bond content, and SDS-unextractable polymeric protein formation. Additionally, HMW-GS deletion resulted in decreased gluten protein chain length, molecular weight, and particle size, contributing to increased thermal instability and reduced crosslinking. The HMW-GS deletion weakened dough strength but improved CSTSB performance, particularly in Dx2d and Dy12d. In-silico analysis further revealed strong interactions between Bx7 and Dx2, primarily driven by desolvation energy, highlighting their crucial role in stabilizing gluten protein interactions.

2024-07-26·ACS Sensors

Parylene Double-Layer Coated Screen-Printed Carbon Electrode for Label-Free and Reagentless Capacitive Aptasensing of Gliadin

Article

作者: Chen, Hsien-Yeh ; Lee, Chin-Yun ; Hsieh, Bo-Chuan ; Tsai, Chun-Ning

Celiac patients are required to strictly adhere to a gluten-free diet because even trace amounts of gluten can damage their small intestine and leading to serious complications. Despite increased awareness, gluten can still be present in products due to cross-contamination or hidden ingredients, making regular monitoring essential. With the goal of guaranteeing food safety for consuming labeled gluten-free products, a capacitive aptasensor was constructed to target gliadin, the main allergic gluten protein for celiac disease. The success of capacitive aptasensing was primarily realized by coating a Parylene double-layer (1000 nm Parylene C at the bottom with 400 nm Parylene AM on top) on the electrode surface to ensure both high insulation quality and abundant reactive amino functionalities. Under the optimal concentration of aptamer (5 μM) used for immobilization, a strong linear relationship exists between the amount of gliadin (0.01-1.0 mg/mL) and the corresponding ΔC response (total capacitance decrease during a 20 min monitoring period after sample introduction), with an R² of 0.9843. The detection limit is 0.007 mg/mL (S/N > 5), equivalent to 0.014 mg/mL (14 ppm) of gluten content. Spike recovery tests identified this system is free from interferences in corn and cassava flour matrices. The analytical results of 24 commercial wheat flour samples correlated well with a gliadin ELISA assay (R² = 0.9754). The proposed label-free and reagentless capacitive aptasensor offers advantages of simplicity, cost-effectiveness, ease of production, and speediness, making it a promising tool for verifying products labeled as gluten-free (gluten content <20 ppm).

2024-07-01·Food Chemistry

Formation, structural characteristics and specific peptide identification of gluten amyloid fibrils

Article

作者: Ren, Feiyue ; Li, Ren ; Liu, Jie ; Feng, Yulin ; Wang, Jing ; Zhang, Huijuan

This research investigates the formation of amyloid fibrils using enzymatically hydrolyzed peptides from gluten, including its components glutenin and gliadin. After completing the fibrillation incubation, the gluten group demonstrated the most significant average particle size (908.67 nm) and conversion ratio (57.64 %), with a 19.21 % increase in thioflavin T fluorescence intensity due to self-assembly. The results indicated increased levels of β-sheet structures after fibrillation. The gliadin group exhibited the highest zeta potential (∼13 mV) and surface hydrophobicity (H₀ = 809.70). Around 71.15 % of predicted amyloidogenic regions within gliadin peptides showed heightened hydrophobicity. These findings emphasize the collaborative influence of both glutenin and gliadin in the formation of gluten fibrils, influenced by hydrogen bonding, hydrophobic, and electrostatic interactions. They also highlight the crucial role played by gliadin with amyloidogenic fragments such as ILQQIL and SLVLQTL, aiming to provide a theoretical basis for understanding the utilization of gluten proteins.