Integrin-Targeting Dye-Doped PEG-Shell/Silica-Core Nanoparticles Mimicking the Proapoptotic Smac/DIABLO Protein

Marco, Rossella De; Rampazzo, Enrico; Zhao, Junwei; Prodi, Luca; Paolillo, Mayra; Picchetti, Pierre; Gallo, Francesca; Calonghi, Natalia; Gentilucci, Luca

doi:10.3390/nano10061211

Cited by 6 publications

(9 citation statements)

References 54 publications

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“…As a consequence, NPs have been decorated with a variety of peptides [3,4,15]. Among them, the cell-penetrating peptides (CPPs) are positively charged sequences that generally consent higher cell penetration, thanks to electrostatic interactions with negatively charged phospholipids.…”

Section: Discussionmentioning

confidence: 99%

“…The peptide CD47 was used to inhibit phagocytosis. In addition, many peptide sequences have been identified that can promote endosome escape after endocytosis of NPs [1][2][3][4].…”

Section: Discussionmentioning

confidence: 99%

“…To the purpose, inorganic fluorescent NPs coated with a biocompatible organic shell were directly functionalized by [3+2] alkyne-azides cycloaddition with an Smac/DIABLOderived peptide and/or a tumor-homing RGD integrin ligand peptide. At low micromolar concentration, these NPs showed significant toxicity towards several cancer cell lines, correlated with high stability and bioavailability, and increased levels of apoptotic activity, while being much less toxic towards model healthy cells [4].…”

Section: Introductionmentioning

confidence: 99%

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Preparation of Non-Toxic Fluorescent Peptide-Coated Silica/PEG Nanoparticles from Peptide-Block Copolymer Conjugates

Santino

Pieraccini

Paolillo

et al. 2022

Micro

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Peptide-decorated nanosystems have demonstrated higher stability and improved cellular uptake as compared to bare NPs and appear highly promising in diagnostics and theranostics of cancer. Herein, we discuss the preparation and structural characterization of peptide-functionalized silica/PEG NPs, starting from peptide–block copolymers, prepared in turn by conjugation of the peptides to block copolymers before NP formation. This synthetic design allowed full control of density and composition of peptide surface coverage. Preliminary experiments support the low toxicity of the fluorescent peptide–NPs and their ability of cell internalization.

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Section: Discussionmentioning

confidence: 99%

“…The peptide CD47 was used to inhibit phagocytosis. In addition, many peptide sequences have been identified that can promote endosome escape after endocytosis of NPs [1][2][3][4].…”

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Preparation of Non-Toxic Fluorescent Peptide-Coated Silica/PEG Nanoparticles from Peptide-Block Copolymer Conjugates

Santino

Pieraccini

Paolillo

et al. 2022

Micro

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“…For the purpose of peptide conjugation, the NPs were prepared from a mixture of PF127 and its diazide derivative PF127-(N 3 ) 2 , and submitted to click chemistry with AVPI-alkyne, containing the pro-apoptotic AVPI N-terminus of Smac/DIABLO ( 21 ), or the integrin-targeting cRGD-alkyne ( 22 ), or a 1:1 mixture of both. At low μM concentration, the bifunctional AVPI/RGD-NPs showed superior toxicity towards A549, U373, and HeLa cancer cells and modest toxicity towards other integrin-expressing cells, correlated with integrin-mediated cell uptake and consequent highly increased levels of apoptotic activity, without perturbing cells not expressing the α5 integrin subunit [ 82 ].…”

Section: Integrin-targeted Npsmentioning

confidence: 99%

Integrin-Targeting Peptides for the Design of Functional Cell-Responsive Biomaterials

et al. 2020

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Integrins are a family of cell surface receptors crucial to fundamental cellular functions such as adhesion, signaling, and viability, deeply involved in a variety of diseases, including the initiation and progression of cancer, of coronary, inflammatory, or autoimmune diseases. The natural ligands of integrins are glycoproteins expressed on the cell surface or proteins of the extracellular matrix. For this reason, short peptides or peptidomimetic sequences that reproduce the integrin-binding motives have attracted much attention as potential drugs. When challenged in clinical trials, these peptides/peptidomimetics let to contrasting and disappointing results. In the search for alternative utilizations, the integrin peptide ligands have been conjugated onto nanoparticles, materials, or drugs and drug carrier systems, for specific recognition or delivery of drugs to cells overexpressing the targeted integrins. Recent research in peptidic integrin ligands is exploring new opportunities, in particular for the design of nanostructured, micro-fabricated, cell-responsive, stimuli-responsive, smart materials.

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“…Unfortunately, most RGD antagonists gave contrasting results and repeatedly failed to demonstrate therapeutic benefits in cancer patients [ 5 ]. In search for alternative utilizations [ 6 ], the RGD ligands have been conjugated to drugs, drug carrier systems, fluorescent tags, nanoparticles (NPs), materials, etc., for cancer therapy or imaging [ 7 , 8 ], and more recently for innovative applications, such as smart and responsive materials [ 9 , 10 ]. To the purpose, several RGD peptides equipped with suitable linkable side chains have been designed.…”

Section: Introductionmentioning

confidence: 99%

Design of α/β-Hybrid Peptide Ligands of α4β1 Integrin Equipped with a Linkable Side Chain for Chemoselective Biofunctionalization of Microstructured Materials

et al. 2021

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Arg-Gly-Asp (RGD)-binding integrins, e.g., αvβ3, αvβ1, αvβ5 integrins, are currently regarded as privileged targets for the delivery of diagnostic and theranostic agents, especially in cancer treatment. In contrast, scarce attention has been paid so far to the diagnostic opportunities promised by integrins that recognize other peptide motifs. In particular, α4β1 integrin is involved in inflammatory, allergic, and autoimmune diseases, therefore, it represents an interesting therapeutic target. Aiming at obtaining simple, highly stable ligands of α4β1 integrin, we designed hybrid α/β peptidomimetics carrying linkable side chains for the expedient functionalization of biomaterials, nano- and microparticles. We identified the prototypic ligands MPUPA-(R)-isoAsp(NHPr)-Gly-OH (12) and MPUPA-Dap(Ac)-Gly-OH (13) (MPUPA, methylphenylureaphenylacetic acid; Dap, 2,3-diamino propionic acid). Modification of 12 and 13 by introduction of flexible linkers at isoAsp or Dap gave 49 and 50, respectively, which allowed for coating with monolayers (ML) of flat zeolite crystals. The resulting peptide–zeolite MLs were able to capture selectively α4β1 integrin-expressing cells. In perspective, the α4β1 integrin ligands identified in this study can find applications for preparing biofunctionalized surfaces and diagnostic devices to control the progression of α4β1 integrin-correlated diseases.

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Integrin-Targeting Dye-Doped PEG-Shell/Silica-Core Nanoparticles Mimicking the Proapoptotic Smac/DIABLO Protein

Cited by 6 publications

References 54 publications

Preparation of Non-Toxic Fluorescent Peptide-Coated Silica/PEG Nanoparticles from Peptide-Block Copolymer Conjugates

Preparation of Non-Toxic Fluorescent Peptide-Coated Silica/PEG Nanoparticles from Peptide-Block Copolymer Conjugates

Integrin-Targeting Peptides for the Design of Functional Cell-Responsive Biomaterials

Design of α/β-Hybrid Peptide Ligands of α4β1 Integrin Equipped with a Linkable Side Chain for Chemoselective Biofunctionalization of Microstructured Materials

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