In Vivo Self‐Assembly Induced Cell Membrane Phase Separation for Improved Peptide Drug Internalization

Wang, Hao; Guo, Ruochen; Zhang, Xuehao; Fan, Peng-Sheng; Song, Ben-Li; Li, Zhixiang; Duan, Zhongyu; Qiao, Zeng‐Ying

doi:10.1002/ange.202111839

Cited by 25 publications

(5 citation statements)

References 47 publications

(15 reference statements)

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“…The phosphorylation of the peptide strand determines its interaction with the membrane‐abundant alkalyne phosphatase (ALP). The dephosphorylation of KYp by the enzyme induces self‐assembly of the peptidic strands, which subsequently determines phase change and therefore membrane leakage and internalization of the peptide 80 …”

Section: Cell‐penetrating Peptidesmentioning

confidence: 99%

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Artificial peptides to induce membrane denaturation and disruption and modulate membrane composition and fusion

Lāce

Cotroneo

Hesselbarth

et al. 2022

Journal of Peptide Science

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Membranes consisting of phospholipid bilayers are an essential constituent of eukaryotic cells and their compartments. The alteration of their composition, structure, and morphology plays an important role in modulating physiological processes, such as transport of molecules, cell migration, or signaling, but it can also lead to lethal effects. The three main classes of membrane‐active peptides that are responsible for inducing such alterations are cell‐penetrating peptides (CPPs), antimicrobial peptides (AMPs), and fusion peptides (FPs). These peptides are able to interact with lipid bilayers in highly specific and tightly regulated manners. They can either penetrate the membrane, inducing nondestructive, transient alterations, or disrupt, permeabilize, or translocate through it, or induce membrane fusion by generating attractive forces between two bilayers. Because of these properties, membrane‐active peptides have attracted the attention of the pharmaceutical industry, and naturally occurring bioactive structures have been used as a platform for synthetic modification and the development of artificial analogs with optimized therapeutic properties to transport biologically active cargos or serve as novel antimicrobial agents. In this review, we focus on synthetic membrane interacting peptides with bioactivity comparable with their natural counterparts and describe their mechanism of action.

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Section: Cell‐penetrating Peptidesmentioning

confidence: 99%

“…The dephosphorylation of KYp by the enzyme induces self-assembly of the peptidic strands, which subsequently determines phase change and therefore membrane leakage and internalization of the peptide. 80…”

Section: Inverted Micelles Are Another Internalization Strategy Utili...mentioning

confidence: 99%

Artificial peptides to induce membrane denaturation and disruption and modulate membrane composition and fusion

Lāce

Cotroneo

Hesselbarth

et al. 2022

Journal of Peptide Science

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“…[ 106 ] The interaction of the phosphorylated molecule with ALP causes the hydrophilic phosphorylated tyrosine to break down to produce a hydrophobic tyrosine (Y). Based on above, our group [ 107 ] reported an in vivo ALP‐responsive self‐assembly strategy, which is developed to induce phase separation of cell membrane, improving the internalization of KLAK peptide drug. The KYp peptide contains an anticancer peptide [KLAKLAK] 2 (K) and a responsive moiety phosphorylated Y (Yp) (Figure 7A).…”

Section: In Vivo Self‐assembly Control At Various Biological Levelmentioning

confidence: 99%

Precise Control of Self‐assembly in vivo Based on Polymer‐Peptide Conjugates^†

Wang

Qiao

2022

Chin. J. Chem.

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The self-assembled nanomaterials based on peptides, which have not only good biocompatibility and low toxicity but also high stability and performance, are increasingly becoming an important way for cancer treatment. In this review, we highlight the progress of in vivo self-assembled polymer-peptide conjugates (PPCs) and their application, showing the recent advances in the development of "in vivo self-assembly" strategy for cancer treatment. Given the diverse microenvironments of tumor cells, different responsive assembly strategies (enzyme, pH, redox, temperature, etc.) have been developed to precisely control the assembly at different biological levels, realizing enhanced drug delivery and improved anticancer efficacy.

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“…Experimentation with peptide hydrogels is vast, which speaks to its ever‐growing list of examples and applications [6–40] . We reported the first use of an Fmoc based dipeptide which forms gels, and responds to a ligand‐receptor interaction [41] .…”

Section: Introductionmentioning

confidence: 99%

An Exploration of Multiple Component Peptide Assemblies by Enzyme‐Instructed Self‐Assembly

Shy

Kim

et al. 2023

ChemSystemsChem

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Based on the motifs (RNISY (M) and DEEVELILGDT (D)) in the protein crystal structures of Merlin and CRL4 DCAFÀ 1 , we phosphorylated the tyrosine residue in M and conjugated M to a self-assembling motif to produce a phosphopeptide (1P) and examined enzyme-instructed self-assembly (EISA) of 1P with and without the presence of D (4). Our results show that EISA of 1P forms a hydrogel at exceedingly low volume fraction (~0.03 %) even with the presence of the hydrophilic peptide, 4. Unlike 1P, 2P (a diastereomer of 1P) or 3P (the enantiomer of 1P) forms a hydrogel via EISA when their concentration is four or three times that of 1P, respectively. Circular dichroism (CD) spectra show that increasing the concentration of the phosphopeptides lowers the CD signals of the mixtures, and the magnitudes of the CD signals depends on the interaction between M and D. This work provides insight for understanding multi-component hydrogels formed by self-assembly, which involves both specific intermolecular interaction and enzymatic reactions.

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In Vivo Self‐Assembly Induced Cell Membrane Phase Separation for Improved Peptide Drug Internalization

Cited by 25 publications

References 47 publications

Artificial peptides to induce membrane denaturation and disruption and modulate membrane composition and fusion

Artificial peptides to induce membrane denaturation and disruption and modulate membrane composition and fusion

Precise Control of Self‐assembly in vivo Based on Polymer‐Peptide Conjugates^†

An Exploration of Multiple Component Peptide Assemblies by Enzyme‐Instructed Self‐Assembly

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In Vivo Self‐Assembly Induced Cell Membrane Phase Separation for Improved Peptide Drug Internalization

Cited by 25 publications

References 47 publications

Artificial peptides to induce membrane denaturation and disruption and modulate membrane composition and fusion

Artificial peptides to induce membrane denaturation and disruption and modulate membrane composition and fusion

Precise Control of Self‐assembly in vivo Based on Polymer‐Peptide Conjugates†

An Exploration of Multiple Component Peptide Assemblies by Enzyme‐Instructed Self‐Assembly

Contact Info

Product

Resources

About

Precise Control of Self‐assembly in vivo Based on Polymer‐Peptide Conjugates^†