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24 results on '"Wang, Dian-Bing"'

2. ProT‐Diff: A Modularized and Efficient Strategy for De Novo Generation of Antimicrobial Peptide Sequences by Integrating Protein Language and Diffusion Models.

Author

Wang, Xue‐Fei, Tang, Jing‐Ya, Sun, Jing, Dorje, Sonam, Sun, Tian‐Qi, Peng, Bo, Ji, Xu‐Wo, Li, Zhe, Zhang, Xian‐En, and Wang, Dian‐Bing

Subjects
LANGUAGE models, ANTIMICROBIAL peptides, ESCHERICHIA coli, AMINO acid sequence, PROTEIN models, PEPTIDE antibiotics
Abstract

Antimicrobial peptides (AMPs) are a promising solution for treating antibiotic‐resistant pathogens. However, efficient generation of diverse AMPs without prior knowledge of peptide structures or sequence alignments remains a challenge. Here, ProT‐Diff is introduced, a modularized deep generative approach that combines a pretrained protein language model with a diffusion model for the de novo generation of AMPs sequences. ProT‐Diff generates thousands of AMPs with diverse lengths and structures within a few hours. After silico physicochemical screening, 45 peptides are selected for experimental validation. Forty‐four peptides showed antimicrobial activity against both gram‐positive or gram‐negative bacteria. Among broad‐spectrum peptides, AMP_2 exhibited potent antimicrobial activity, low hemolysis, and minimal cytotoxicity. An in vivo assessment demonstrated its effectiveness against a drug‐resistant E. coli strain in acute peritonitis. This study not only introduces a viable and user‐friendly strategy for de novo generation of antimicrobial peptides, but also provides potential antimicrobial drug candidates with excellent activity. It is believed that this study will facilitate the development of other peptide‐based drug candidates in the future, as well as proteins with tailored characteristics. [ABSTRACT FROM AUTHOR]

Published
2024
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14. Molecular Diagnosis of COVID-19: Challenges and Research Needs

Author

Feng, Wei, primary, Newbigging, Ashley M., additional, Le, Connie, additional, Pang, Bo, additional, Peng, Hanyong, additional, Cao, Yiren, additional, Wu, Jinjun, additional, Abbas, Ghulam, additional, Song, Jin, additional, Wang, Dian-Bing, additional, Cui, Mengmeng, additional, Tao, Jeffrey, additional, Tyrrell, D. Lorne, additional, Zhang, Xian-En, additional, Zhang, Hongquan, additional, and Le, X. Chris, additional

Published
2020
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24. Existence of Separate Domains in Lysin PlyG for Recognizing Bacillus anthracisSpores and Vegetative Cells

Author

Yang, Hang, Wang, Dian-Bing, Dong, Qiuhua, Zhang, Zhiping, Cui, Zongqiang, Deng, Jiaoyu, Yu, Junping, Zhang, Xian-en, and Wei, Hongping

Abstract

ABSTRACTAs a potential antimicrobial, the bacteriophage lysin PlyG has been reported to specifically recognize Bacillus anthracisvegetative cells only and to kill B. anthracisvegetative cells and its germinating spores. However, how PlyG interacts with B. anthracisspores remains unclear. Herein, a 60-amino-acid domain in PlyG (residues 106 to 165), located mainly in the previously identified catalytic domain, was found able to specifically recognize B. anthracisspores but not vegetative cells. The exosporium of the spores was found to be the most probable binding target of this domain. This is the first time that a lysin for spore-forming bacteria has been found to have separate domains to recognize spores and vegetative cells, which might help in understanding the coevolution of phages with spore-forming bacteria. Besides providing new biomarkers for developing better assays for identifying B. anthracisspores, the newly found domain may be helpful in developing PlyG as a preventive antibiotic to reduce the threat of anthrax in suspected exposures to B. anthracisspores.

Published
2012
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