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探索核糖体S1蛋白来源肽的淀粉样变性以开发新型抗菌肽。

Exploring Amyloidogenicity of Peptides From Ribosomal S1 Protein to Develop Novel AMPs.

作者信息

Galzitskaya Oxana V

机构信息

Laboratory of Bioinformatics and Proteomics, Institute of Protein Research, Russian Academy of Sciences, Pushchino, Russia.

Laboratory of the Structure and Function of Muscle Proteins, Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Russia.

出版信息

Front Mol Biosci. 2021 Aug 19;8:705069. doi: 10.3389/fmolb.2021.705069. eCollection 2021.

DOI:10.3389/fmolb.2021.705069
PMID:34490350
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8416663/
Abstract

Antimicrobial peptides (AMPs) and similar compounds are potential candidates for combating antibiotic-resistant bacteria. The hypothesis of directed co-aggregation of the target protein and an amyloidogenic peptide acting as an antimicrobial peptide was successfully tested for peptides synthesized on the basis of ribosomal S1 protein in the bacterial culture of . Co-aggregation of the target protein and amyloidogenic peptide was also tested for the pathogenic ribosomal S1 protein from . Almost all peptides that we selected as AMPs, prone to aggregation and formation of fibrils, based on the amino acid sequence of ribosomal S1 protein from formed amyloid fibrils. We have demonstrated that amyloidogenic peptides are not only toxic to their target cells, but also some of them have antimicrobial activity. Controlling the aggregation of vital bacterial proteins can become one of the new directions of research and form the basis for the search and development of targeted antibacterial drugs.

摘要

抗菌肽(AMPs)及类似化合物是对抗抗生素耐药细菌的潜在候选物。在细菌培养物中,基于核糖体S1蛋白合成的肽成功验证了靶蛋白与作为抗菌肽的淀粉样生成肽定向共聚集的假说。还对来自[具体来源]的致病性核糖体S1蛋白进行了靶蛋白与淀粉样生成肽的共聚集测试。基于来自[具体来源]的核糖体S1蛋白的氨基酸序列,我们选择的几乎所有易于聚集并形成原纤维的作为AMPs的肽都形成了淀粉样原纤维。我们已经证明,淀粉样生成肽不仅对其靶细胞有毒,而且其中一些还具有抗菌活性。控制重要细菌蛋白的聚集可能成为新的研究方向之一,并为靶向抗菌药物的研发奠定基础。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a147/8416663/fb616400718b/fmolb-08-705069-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a147/8416663/54f3882aa581/fmolb-08-705069-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a147/8416663/fb616400718b/fmolb-08-705069-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a147/8416663/54f3882aa581/fmolb-08-705069-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a147/8416663/fb616400718b/fmolb-08-705069-g002.jpg

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本文引用的文献

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Int J Mol Sci. 2021 Jul 7;22(14):7291. doi: 10.3390/ijms22147291.
2
Impact of a Single Point Mutation on the Antimicrobial and Fibrillogenic Properties of Cryptides from Human Apolipoprotein B.单点突变对人载脂蛋白B隐肽的抗菌和纤维原性特性的影响。
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[Antibacterial effects of peptides synthesized based on the sequence of ribosome protein S1].基于核糖体蛋白S1序列合成的肽的抗菌作用
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Amyloidogenic Peptides: New Class of Antimicrobial Peptides with the Novel Mechanism of Activity.淀粉样肽:具有新型作用机制的新型抗菌肽。
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Multiple Antimicrobial Effects of Hybrid Peptides Synthesized Based on the Sequence of Ribosomal S1 Protein from .基于核糖体 S1 蛋白序列合成的杂合肽的多种抗菌作用。
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