A frog-derived bionic peptide with discriminative inhibition of tumors based on integrin αvβ3 identification

Han, Zhihao; Lian, Chen; Ma, Yuxuan; Zhang, Congying; Liu, Zicun; Tu, Yuanbiao; Ma, Yi; Gu, Yueqing

doi:10.1039/d0bm01187h

Cited by 2 publications

(2 citation statements)

References 52 publications

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“…Advances of simulation empowers the utilization of natural molecules inherent capacities for cancer therapy purposes. 29 Generating mutations and changes such as increasing hydrophobicity by replacing Isoleucine amino acid, enhancing positive charge by replacing lysine amino acid, and adding cell-penetrating peptide sequence (R5) in the Aur anticancer peptide optimize Aur molecule anticancer activity. These effects lead to cancer cells structural stability changes and enhancing membrane permeability.…”

Section: Discussionmentioning

confidence: 99%

Designing Potent Anticancer Peptides by Aurein 1.2 Key Residues Mutation and Catenate Cell-Penetrating Peptide

et al. 2022

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Purpose: Aurein 1.2 (Aur) peptide is known for possessing anticancer characteristics devoid of conventional therapeutics side effects. For improving Aur peptide anticancer functionality, different anticancer peptides were constructed based on Aur peptide through targeting two separate strategies, including 1) sequence-based mutations and 2) adding a cell-penetrating peptide linker. Methods: The study was approached by designing three different analogs of Aur, including a) Aur mutant (Aurm), b) Aur with N-terminal polyarginine linker (R5-Aur), and c) Aurm with R5 (R5-Aurm). Computational molecular dynamics simulations clearly showed higher structural stability of R5-Aur and R5-Aurm compared to Aur, solely. The α-helical properties of R5-Aur and R5-Aurm were protected during 500 ns simulations in water solution while no such structural conservation was seen for Aur in silico. Results: The results of the current study highlight response to one of the main challenges of cancer therapy through selective invasion of Aur to cancer cells without significant involvement of normal cells. This issue was confirmed by different assays, including: MTT assay, flow cytometry, qPCR, and nuclei morphological observations. Furthermore, this study intensifies exploiting in silico approaches for adjusting drug delivery. The results of different assessments on designed peptides reveal an anticancer activity pattern rising from Aur toward Aurm, and R5-Aur, consecutively. Conclusion: The designed structure of Aur shows improved anticancer activity through molecular changes which makes it suggestable for anticancer therapies.

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Section: Discussionmentioning

confidence: 99%

Designing Potent Anticancer Peptides by Aurein 1.2 Key Residues Mutation and Catenate Cell-Penetrating Peptide

et al. 2022

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“…By imitating the structure-activity relationship of Aurein natural peptides, Han and co-workers fused the strong anticancer A1 peptide with the screened targeted linear peptide RWr with the ability to bind to integrin α and β3, and obtained hybrid peptide nanomaterials with high stability and good therapeutic effect. Due to the existence of excellent fusion peptide RA3 (RWrGGGGGLFDIIKIAESF), this biomimetic synthesis of fusion peptide RA3 had good selectivity for tumors [35]. Different linkers were selected, and the structure and function of the constructed multiple peptide sequences were analyzed by molecular simulation and molecular docking technology, and the RA3 fusion peptide was finally selected.…”

Section: Bioinspired Peptide Nanomaterialsmentioning

confidence: 99%

Self-assembly of bioinspired peptides for biomimetic synthesis of advanced peptide-based nanomaterials: a mini-review

Kong¹,

Yang²,

He³

et al. 2023

Nano Futures

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The design and motif-tailoring of peptide sequence are crucial for mediating the self-assembly of peptide molecules and the biomimetic synthesis of functional peptide-based nanomaterials. It is well known that nature provides the guidance and inspiration for the design and molecular tailoring of functional peptide sequences, which can further self-assemble into complex peptide nanomaterials with adjustable dimensions. In this mini-review, we summarize recent advance in the bioinspired design and regulation of functional peptide sequences by natural things, such as the mussels, milk protein, silkworm silks, frogs, and Alzheimer's disease. The self-assembly of bioinspired peptides in vitro and in vivo for controlled synthesis of various peptide-based nanomaterials is introduced and analyzed. In addition, various applications of biomimetic peptide nanomaterials for biosensors, bioimaging, cancer therapy, antibacterial materials, tissue engineering, as well as energy storage and environmental science are demonstrated in detail. Finally, we give the perspectives on future development of this promising research topic. By these efforts, it is hopeful to promote the understanding on the optimization of bioinspired peptides and the design of novel peptide nanomaterials for advanced applications.

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A frog-derived bionic peptide with discriminative inhibition of tumors based on integrin αvβ3 identification

Abstract: Combined with an integrin αvβ3 binding element, fusion peptides maintained the prime activity of membrane cracking, simultaneously increasing precision of cancer treatment by using computational simulation technology.

Cited by 2 publications

References 52 publications

Designing Potent Anticancer Peptides by Aurein 1.2 Key Residues Mutation and Catenate Cell-Penetrating Peptide

Designing Potent Anticancer Peptides by Aurein 1.2 Key Residues Mutation and Catenate Cell-Penetrating Peptide

Self-assembly of bioinspired peptides for biomimetic synthesis of advanced peptide-based nanomaterials: a mini-review

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