An amphiphilic peptide with cell penetrating sequence for highly efficient gene transfection

Wang, Yu; Nie, Yong; Ding, Zhaozhao; Yao, Mingyu; Du, Rui; Zhang, Lan; Wang, Shu; Li, Dongxiang; Wang, Yilin; Cao, Meiwen

doi:10.1016/j.colsurfa.2020.124529

Cited by 12 publications

(10 citation statements)

References 44 publications

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“…RK and RKRK are surfactant-like with two segments. Their hydrophobic segment is the same as Nap-FFGPLGLA- [ 61 , 62 , 63 ], while they have a different number of positive residues (-RK- or -RKRK-) to form the hydrophilic segments. In contrast, by having one lysine residue located in the middle of the hydrophobic region, K-RK shows four distinct segments in its molecular structure.…”

Section: Resultsmentioning

confidence: 99%

Peptide-Mediated Synthesis of Zeolitic Imidazolate Framework-8: Effect of Molecular Hydrophobicity, Charge Number and Charge Location

et al. 2021

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Three amphiphilic peptides with varied molecular hydrophobicity, charge number and charge location have been designed as regulators to modulate the crystal growth of zeolitic imidazolate framework-8 (ZIF-8). All three peptides can interact with ZIF-8 to inhibit {100} facet growth and produce truncated cubic crystals. The peptide’s molecular hydrophobicity plays a dominant role in defining the final morphology and size of the ZIF-8 crystals. The peptides with less charge and higher hydrophobicity can promote nuclei formation and crystal growth to give smaller ZIF-8 crystals. However, the charge located in the center of the molecular hydrophobic region has little effect on the crystal nucleation and growth due to the shielding of its charge by molecular aggregation. The study provides insights into the effect of molecular charge and hydrophobicity on ZIF-8 crystal growth and is helpful for guiding the molecular design for regulating the synthesis of metal-organic framework materials.

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Section: Resultsmentioning

confidence: 99%

Peptide-Mediated Synthesis of Zeolitic Imidazolate Framework-8: Effect of Molecular Hydrophobicity, Charge Number and Charge Location

et al. 2021

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“…Compared to conventional, cytotoxic DNA condensation agents such as polyelectrolytes and lipidic surfactants, short peptides have higher biocompatibility and consequently lower toxicity. Moreover, their structure can easily be modified to obtain high affinity DNA binders ( Wang et al, 2020 ). Furthermore, the condensation with the peptidic vector confers protection from DNases.…”

Section: Viral Mimeticsmentioning

confidence: 99%

“…Bola amphiphiles, composed of a central hydrophobic segment flanked by two hydrophilic ones, have the ability to self-assemble into fibrillar or spherical nanostructures depending on the sequence design ( Chen et al, 2013 ). Examples are the purely peptidic RGD-GPLGLAG-I 3 -G-R 8 ( Wang et al 2020 ) and the fatty acid containing RGD-C 12 -R 8 ( Chen et al, 2013 ) that accommodate both functional and structural motifs, where RGD is crucial for integrin-binding and R 8 for cell penetration. Additionally, the PLGLA sequence serves as an enzyme-cleavable segment, while I 3 confers hydrophobicity.…”

Section: Viral Mimeticsmentioning

confidence: 99%

“…A stable peptide-DNA complex is formed when all the negative charges are successfully neutralized. For example, RGD-GPLGLAG-I 3 -G-R 8 that self-assembles into spheres, upon the interaction with DNA and depending on the R + / - values forms thread-like (R + / - = 0.5) complexes or highly condensed rod-like or spherical (R + / - = 3) nanostructures ( Wang et al, 2020 ). In another example, the R + / - of 10 is the minimum requirement for DNA condensation with K 3 C 6 SPD, where the peptide alone self-assembles into nanoribbons.…”

Section: Viral Mimeticsmentioning

confidence: 99%

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Exploiting Peptide Self-Assembly for the Development of Minimalistic Viral Mimetics

et al. 2021

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Viruses are natural supramolecular nanostructures that form spontaneously by molecular self-assembly of complex biomolecules. Peptide self-assembly is a versatile tool that allows mimicking viruses by creating their simplified versions through the design of functional, supramolecular materials with modularity, tunability, and responsiveness to chemical and physical stimuli. The main challenge in the design and fabrication of peptide materials is related to the precise control between the peptide sequence and its resulting supramolecular morphology. We provide an overview of existing sequence patterns employed for the development of spherical and fibrillar peptide assemblies that can act as viral mimetics, offering the opportunity to tackle the challenges of viral infections.

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“…[169] Based on such collective advantages, various CPPs have been developed rapidly in recent years. [170][171][172][173] Although these peptides possess various secondary structures and sequences, they share some common features, including hydrophobic domain and high content of basic amino acids. [174] It has been proposed that the hydrophobic domain of CPPs can promote hydrophobic interactions with phospholipids to encourage cell membrane penetration and the protonated basic residues promote ionic binding with negatively charged nucleic acids as well as proteoglycans being present at the cell membrane surface.…”

Section: Cationic Peptides and Nucleic Acidsmentioning

confidence: 99%

Recent Progress in Ionic Coassembly of Cationic Peptides and Anionic Species

Xie

Zheng

2020

Macromol. Rapid Commun.

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innovative insight into understanding the properties of the material systems beyond molecular level. [6-8] Through the last decades, supramolecular chemistry has deeply permeated and fused with biology and materials science, and has gradually growth into an interdisciplinary platform for the creation of self-assembled systems with extraordinary properties. [9-12] Among the numerous systems, self-assembled peptide is one of the most important branches, because of its rich chemical diversity, versatile characters, inherent biocompatibility, and bioactivity. [13-15] Specifically, the natural or chemically engineered amino acids encoded in the sequence of peptide molecules enable the formation of customizable secondary structures, the cooperative interactions between main chains and side chains of peptide molecules can be further leveraged to produce hierarchical nanostructures [16-22] and important biofunctions, such as drug delivery, [23-25] tissue engineering, [26-28] regenerative medicine, [29-31] and biomineralization. [32-35] Moreover, many studies have disclosed that self-assembled peptide nanostructures can offer higher performance (catalytic, therapeutic, targeting, etc.) than peptide itself. [36-42] For those reasons, peptide self-assembly has been recognized as a subject of great importance in supramolecular chemistry, biology, and nanotechnology, and the breadth and depth of peptide selfassemblies have been documented and demonstrated in several excellent reviews. [43-51] Besides the self-assembly of unimolecular peptides, multicomponent coassembly between peptides and other building blocks has recently become increasingly prevalent, as the modular approach offers a simple and effective way to arrive at supramolecular materials with wide structural complexity and value-added properties for multiple tasks applications. [52-56] This integrated characteristic further stimulates researchers to explore the scope of peptide coassembly with the aim of expanding the space of functional utility. To selectively form the multicomponent nanostructures, the interplay of the driving forces should be energetically much more favorable for strengthening the coassembly of distinct components than the self-sorting of the same type of components. [57-59] Following this design criteria, the introduction of complementary noncovalent interactions into the multicomponent systems is Peptide assembly has been extensively exploited as a promising platform for the creation of hierarchical nanostructures and tailor-made bioactive materials. Ionic coassembly of cationic peptides and anionic species is paving the way to provide particularly important contribution to this topic. In this review, the recent progress of ionic coassembly soft materials derived from the electrostatic coupling between cationic peptides and anionic species in aqueous solution is systematically summarized. The presentation of this review starts from a brief background on the general importance and advantages of peptide-based ionic coassembly. After that, divers...

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An amphiphilic peptide with cell penetrating sequence for highly efficient gene transfection

Cited by 12 publications

References 44 publications

Peptide-Mediated Synthesis of Zeolitic Imidazolate Framework-8: Effect of Molecular Hydrophobicity, Charge Number and Charge Location

Peptide-Mediated Synthesis of Zeolitic Imidazolate Framework-8: Effect of Molecular Hydrophobicity, Charge Number and Charge Location

Exploiting Peptide Self-Assembly for the Development of Minimalistic Viral Mimetics

Recent Progress in Ionic Coassembly of Cationic Peptides and Anionic Species

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