The morphology and structural features of self-aggregating hexapeptides with antibiofilm formation activity-Reference-Cited by-同舟云学术

The morphology and structural features of self-aggregating hexapeptides with antibiofilm formation activity

Published:2023 Issue:18 Volume:4 Page:4110-4118
ISSN:2633-5409
Container-title:Materials Advances
language:en
Short-container-title:Mater. Adv.

Author:

Chen Dongru¹^ORCID,Wang Tingyu¹,Huang Yiyi²,Chen Yucong²,Lin Huancai²,Wu Liping¹

Affiliation:

1. Department of Orthodontics, Hospital of Stomatology, Guanghua School of Stomatology, Sun Yat-sen University, Guangdong Provincial Key Laboratory of Stomatology, Guangzhou, Guangdong, China

2. Department of Preventive Dentistry, Hospital of Stomatology, Guanghua School of Stomatology, Sun Yat-sen University, Guangdong Provincial Key Laboratory of Stomatology, Guangzhou, Guangdong, China

Abstract

Though self-aggregating peptides all aggregate into fibrils, they have been found to exert different roles against microbes, and the reasons remain unknown.

Funder

National Natural Science Foundation of China

Basic and Applied Basic Research Foundation of Guangdong Province

Publisher

Royal Society of Chemistry (RSC)

Subject

General Materials Science,Chemistry (miscellaneous)

Link

http://pubs.rsc.org/en/content/articlepdf/2023/MA/D3MA00014A

Reference33 articles.

1. Toward complex matter: Supramolecular chemistry and self-organization

2. Molecular Insight into the Effects of Enhanced Hydrophobicity on Amyloid-like Aggregation

3. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade

4. Functional Amyloids

5. Self-assembling dipeptide antibacterial nanostructures with membrane disrupting activity

Cited by 2 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. The effects and mechanisms of novel antibacterial amyloid peptides derived from Streptococcus mutans proteome;Chemical Engineering Journal;2024-10

2. Optimizing Antimicrobial Peptide Design: Integration of Cell-Penetrating Peptides, Amyloidogenic Fragments, and Amino Acid Residue Modifications;International Journal of Molecular Sciences;2024-05-30