期刊
BIOMOLECULES
卷 10, 期 1, 页码 -出版社
MDPI
DOI: 10.3390/biom10010007
关键词
computational biology; molecular dynamics; peptide; amyloid; scaffold; gene transfer
资金
- Artie McFerrin Department of Chemical Engineering of Texas AM award
- project Advanced Research Activities in Biomedical and Agro alimentary Technologies - Operational Program Competitiveness, Entrepreneurship, and Innovation (NSRF 2014-2020) [MIS 5002469]
- European Union (European Regional Development Fund)
Cell-penetrating peptides are used extensively to deliver molecules into cells due to their unique characteristics such as rapid internalization, charge, and non-cytotoxicity. Amyloid fibril biomaterials were reported as gene transfer or retroviral infection enhancers; no cell internalization of the peptides themselves is reported so far. In this study, we focus on two rationally and computationally designed peptides comprised of beta-sheet cores derived from naturally occurring protein sequences and designed positively charged and aromatic residues exposed at key residue positions. The beta-sheet cores bestow the designed peptides with the ability to self-assemble into amyloid fibrils. The introduction of positively charged and aromatic residues additionally promotes DNA condensation and cell internalization by the self-assembled material formed by the designed peptides. Our results demonstrate that these designer peptide fibrils can efficiently enter mammalian cells while carrying packaged luciferase-encoding plasmid DNA, and they can act as a protein expression enhancer. Interestingly, the peptides additionally exhibited strong antimicrobial activity against the enterobacterium Escherichia coli.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据