Structural Mimics of Viruses Through Peptide/DNA Co-Assembly

Ni, Rong; Chau, Ying

doi:10.1021/ja507833x

Cited by 89 publications

(90 citation statements)

References 24 publications

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“…39–41 In this work, we found that, although TR4 has an amphiphilic structure, it exhibits good water solubility. By transmission electron microscopy (TEM), we found that TR4 could not form ordered aggregates in buffer solution when its concentration was less than 100 µ M (Figure 4A).…”

Section: Resultsmentioning

confidence: 72%

Virus-Inspired Self-Assembled Nanofibers with Aggregation-Induced Emission for Highly Efficient and Visible Gene Delivery

Zhang

Jin

et al. 2017

ACS Appl. Mater. Interfaces

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High-efficiency gene transfer and suitably low cytotoxicity are the main goals of gene transfection systems based on nonviral vectors. In addition, it is desirable to track the gene transfer process in order to observe and explain the mechanism. Herein, inspired by viral structures that are optimized for gene delivery, we designed a small-molecule gene vector (TR4) with aggregation-induced emission properties by capping a peptide containing four arginine residues with tetraphenylethene (TPE) and a lipophilic tail. This novel vector can self-assemble with plasmid DNA to form nanofibers in solution with low cytotoxicity, high stability, and high transfection efficiency. pDNA@TR4 complexes were able to transfect a variety of different cell lines, including stem cells. The self-assembly process induces bright fluorescence from TPE, which makes the nanofibers visible by confocal laser scanning microscopy (CLSM). This allows us for the tracking of the gene delivery process.

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Section: Resultsmentioning

confidence: 72%

Virus-Inspired Self-Assembled Nanofibers with Aggregation-Induced Emission for Highly Efficient and Visible Gene Delivery

Zhang

Jin

et al. 2017

ACS Appl. Mater. Interfaces

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“…22 The central b-sheet region (LVFFA) of K3C6SPD is derived from amyloid b-peptide, and two phenylalanine (F) residues are critical to the peptide assembly. [23][24][25] Therefore, by the substitution of F20 with histidine (called F20H) (Fig.…”

Section: Resultsmentioning

confidence: 99%

Ultrasound-facilitated assembly and disassembly of a pH-sensitive self-assembly peptide

Liu

Chau

2018

RSC Adv.

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In this report, we investigated the impact of external stimulus (ultrasound) and internal stimulus (pH) on peptide assembly and disassembly. Two short rationally designed peptides K3C6SPD and F20H differing in the presence of a single pH-sensitive histidine residue were studied as the model peptides. The assembly kinetics studies demonstrated that the substitution of phenylalanine in K3C6SPD with histidine (F20H) significantly slowed down the peptide assembly rate at all three tested pHs (pH 9.5, pH 7.4 and pH 5.0). At the same time, this F to H substitution led to the increased pH-responsive assembly kinetics.By treating the peptide sample at the beginning of the assembly process at pH 9.5 for 5 min with the ultrasound power of 2.1 W cm À2, the assembly rate of peptide F20H was significantly accelerated with the lag phase being shortened from 10 days to 2 days. For the disassembly of F20H peptide nanofibrils preformed at pH 9.5, upon pH adjustment from pH 9.5 to pH 5.0, 5 min ultrasonication of the nanofibrils resulted in the nanofibril disassembly within 6 hours, instead of 5 days in the absence of ultrasound. On the contrary, similar ultrasound treatment of the peptide K3C6SPD did not produce any obvious effect on both assembly and disassembly processes. This study offers an effective strategy to modulate the stimuli-responsiveness of the peptide-based biomaterials.

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“…[7] Thes hort peptide strand contains three main segments:1 )anN -terminal Figure 1. [7] The structural characterization of nanococoons has led to amodel for co-assembly that involves:1 )the peptide strands preorganize along the DNAb ackbone through electrostatic interactions;2 )the peptides self-assemble into nanofibrils; and 3) inter-nanofibril association places the DNAinside the nanococoon ( Figure 1A). B) The peptides studied in this work.…”

Section: Rong Ni and Ying Chau*mentioning

confidence: 99%

Tuning the Inter‐nanofibril Interaction To Regulate the Morphology and Function of Peptide/DNA Co‐assembled Viral Mimics

Chau

2017

Angew Chem Int Ed

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The ability to tune the inter-subunit interaction within the virus capsid may be critical to assembly and biological function. This process was extended here with peptide/DNA co-assembled viral mimics. The resulting co-assemblies, formed and stabilized by both peptide nanofibril-DNA and peptide nanofibril-nanofibril interactions, were tuned through hydrophobic packing interactions of the peptide sequences. By strengthening peptide side-chain complementarity and/or elongating the peptide chain (from 4 to 8 residues), we report strengthening the inter-nanofibril interaction to create stable nanococoons that give high gene-transfection efficacy.

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Structural Mimics of Viruses Through Peptide/DNA Co-Assembly

Cited by 89 publications

References 24 publications

Virus-Inspired Self-Assembled Nanofibers with Aggregation-Induced Emission for Highly Efficient and Visible Gene Delivery

Virus-Inspired Self-Assembled Nanofibers with Aggregation-Induced Emission for Highly Efficient and Visible Gene Delivery

Ultrasound-facilitated assembly and disassembly of a pH-sensitive self-assembly peptide

Tuning the Inter‐nanofibril Interaction To Regulate the Morphology and Function of Peptide/DNA Co‐assembled Viral Mimics

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