An Intrinsically Disordered Peptide Facilitates Non‐Endosomal Cell Entry

Medina, Scott H.; Miller, S.A.; Keim, Allison I.; Gorka, Alexander P.; Schnermann, Martin J.; Schneider, Judith C.

doi:10.1002/ange.201510518

Cited by 9 publications

(2 citation statements)

References 23 publications

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“…Currently, by manually controlling the number, type, and sequence composition of amino acids, researchers have designed and synthesized different self-assembling peptides, including peptide amphiphiles (lipidated peptides and surfactant-like peptides), ionic complementary peptides, , β-hairpin peptides, , aromatic peptides, , and so on. The sequence characteristics of the self-assembling peptides are shown in Table .…”

Section: Self-assembling Peptidesmentioning

confidence: 99%

Peptide Supramolecular Self-Assembly: Regulatory Mechanism, Functional Properties, and Its Application in Foods

Chen,

Liu,

et al. 2024

J. Agric. Food Chem.

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Peptide self-assembly, due to its diverse supramolecular nanostructures, excellent biocompatibility, and bright application prospects, has received wide interest from researchers in the fields of biomedicine and green life technology and the food industry. Driven by thermodynamics and regulated by dynamics, peptides spontaneously assemble into supramolecular structures with different functional properties. According to the functional properties derived from peptide self-assembly, applications and development directions in foods can be found and explored. Therefore, in this review, the regulatory mechanism is elucidated from the perspective of self-assembly thermodynamics and dynamics, and the functional properties and application progress of peptide self-assembly in foods are summarized, with a view to more adaptive application scenarios of peptide self-assembly in the food industry.

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Section: Self-assembling Peptidesmentioning

confidence: 99%

Peptide Supramolecular Self-Assembly: Regulatory Mechanism, Functional Properties, and Its Application in Foods

Chen,

Liu,

et al. 2024

J. Agric. Food Chem.

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“…To improve the cell-permeability of CREBLL-tide, cell-penetrating peptides (CPP) CLIP6 or TAT with a diglycine spacer were added to the N-terminus of the MLL portion of CREBLLtide and its negative control mutant. 38,39 A FITC tag was attached to the CLIP6-CREBLL-tides and the uptake and localization of peptides were observed by confocal microscopy. CLIP6-CREBLL-tides were incubated with the breast cancer cell lines MDA-MB-231 and VARI068 for 3, 6, and 9 hours, and the MCF7 cell line for 3 hours.…”

mentioning

confidence: 99%

Inhibition of CREB binding and function with a dual-targeting ligand

Liu,

Joy,

Henley

et al. 2023

Preprint

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CBP/p300 is a master transcriptional coactivator, regulating gene activation by interacting with multiple transcriptional activators. Dysregulation of protein-protein interactions (PPIs) between the CBP/p300 KIX domain and its activators is implicated in a number of cancers including breast, leukemia, and colorectal cancer. However, KIX is typically considered ‘undruggable’ because of its shallow binding surfaces lacking both significant topology and promiscuous binding profiles. We previously reported a dual-targeting peptide (MybLL-tide) that inhibits the KIX-Myb interaction with excellent specificity and potency. Here we demonstrate a branched, second-generation analog, CREBLL-tide, that inhibits the KIX-CREB PPI with higher potency and selectivity. Additionally, the best of these CREBLL-tide analogs shows excellent and selective anti-proliferation activity in breast cancer cells. These results indicate CREBLL-tide is an effective tool for assessing the role of KIX-activator interactions in breast cancer and expanding the dual-targeting strategy for inhibiting KIX and other coactivators that contain multiple binding surfaces.

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De novo Design of Selective Membrane‐Active Peptides by Enzymatic Control of Their Conformational Bias on the Cell Surface

Shi

2019

Angewandte Chemie

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Selectively targeting the membrane-perturbing potential of peptides towards ad istinct cellular phenotype allows one to target distinct populations of cells.W ereport the de novo design of an ew class of peptide whose ability to perturb cellular membranes is coupled to an enzyme-mediated shift in the folding potential of the peptide into its bioactive conformation. Cells rich in negatively charged surface components that also highly express alkaline phosphatase,f or example many cancers,a re susceptible to the action of the peptide.T he unfolded, inactive peptide is dephosphorylated, shifting its conformational bias towards cell-surface-induced folding to form af acially amphiphilic membrane-active conformer.T he fate of the peptide can be further tuned by peptide concentration to affect either lytic or cell-penetrating properties,whichare useful for selective drug delivery.This is an ew design strategy to affordp eptides that are selective in their membrane-perturbing activity.

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An Intrinsically Disordered Peptide Facilitates Non‐Endosomal Cell Entry

Cited by 9 publications

References 23 publications

Peptide Supramolecular Self-Assembly: Regulatory Mechanism, Functional Properties, and Its Application in Foods

Peptide Supramolecular Self-Assembly: Regulatory Mechanism, Functional Properties, and Its Application in Foods

Inhibition of CREB binding and function with a dual-targeting ligand

De novo Design of Selective Membrane‐Active Peptides by Enzymatic Control of Their Conformational Bias on the Cell Surface

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