Supramolecular Peptide/Surface Assembly for Monitoring Proteinase Activity and Cancer Diagnosis

Soum, Claire; Rubio-Albenque, Sandra; Fery–Forgues, Suzanne; Déléris, Gérard; Alouini, Mohamed-Anis; Berthelot, Thomas

doi:10.1021/acsami.5b04871

Cited by 5 publications

(4 citation statements)

References 45 publications

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“…Peptides are often used in the functionalization of solid surfaces due to their high degree of programmability . Applications of material-binding peptides include the formation and functionalization of nanomaterials, − protective or bioactive coatings for medical implants and other biomaterials, , biosensing, , cancer diagnosis, and drug delivery . Peptide adsorption can also be used as a model for that of larger biomolecules such as proteins, which is implicated in desired and otherwise bodily reactions. , For instance, the effect of a surface on the fibrillation of the amyloid β protein, which causes Alzheimer’s disease, has been studied using polypeptide segments of this protein. − …”

Section: Introductionmentioning

confidence: 99%

Energy Landscape Mapping and Replica Exchange Molecular Dynamics of an Adsorbed Peptide

2020

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Adsorption of peptides at the interface between a fluid and a solid occurs widely in both nature and applications. Knowing the dominant conformations of adsorbed peptides and the energy barriers between them is of interest for a variety of reasons. Molecular dynamics (MD) simulation is a widely used technique that can yield such understanding. However, the complexity of the energy landscapes of adsorbed peptides means comprehensive exploration of the energy landscape by MD simulation is challenging. An alternative approach is energy landscape mapping (ELM), which involves the location of stationary points on the potential energy surface, and its analysis to determine, for example, the pathways and energy barriers between them. In the study reported here, comparison is made between this technique and replica exchange molecular dynamics (REMD) for met-enkephalin adsorbed at the interface between graphite and the gas phase: the first ever direct comparison of these techniques for adsorbed peptides. Both methods yield up the dominant adsorbed peptide conformations. Unlike REMD, however, ELM also readily allows the identification of the connectivity and energy barriers between the favored conformations, transition paths and structures between these conformations, and the impact of entropy. It also permits the calculation of the constant volume heat capacity, although the accuracy of this is limited by the sampling of high-energy minima. Overall, compared to REMD, ELM provides additional insight into the adsorbed peptide system provided sufficient care is taken to ensure key parts of the landscape are adequately sampled.

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Section: Introductionmentioning

confidence: 99%

Energy Landscape Mapping and Replica Exchange Molecular Dynamics of an Adsorbed Peptide

2020

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“…Matrix metalloproteinase-7 (MMP-7) is able to degrade a great diversity of extracellular matrix (ECM) consisting of type IV collagen, fibronectin, as well as several non-ECM molecules. − Studies have shown that MMP-7 is almost closely linked to many fatal diseases such as cancer, which thus is considered as an important biomarker for a great many tumors. , Until now, a variety of approaches, including fluorescence resonance energy transfer (FRET)-based assays, and enzyme-linked immunosorbent assays (ELISA), have been developed. However, there remain some drawbacks including expensive, fussy, and low sensitivities .…”

Section: Introductionmentioning

confidence: 99%

DNA Enzyme-Decorated DNA Nanoladders as Enhancer for Peptide Cleavage-Based Electrochemical Biosensor

Kou

Zhang

Xie

et al. 2016

ACS Appl. Mater. Interfaces

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Herein, we developed a label-free electrochemical biosensor for sensitive detection of matrix metalloproteinase-7 (MMP-7) based on DNA enzyme-decorated DNA nanoladders as enhancer. A peptide and single-stranded DNA S1-modified platinum nanoparticles (P1-PtNPs-S1), which served as recognition nanoprobes, were first immobilized on electrode. When target MMP-7 specifically recognized and cleaved the peptide, the PtNPs-S1 bioconjugates were successfully released from electrode. The remaining S1 on electrode then hybridized with ssDNA1 (I1) and ssDNA2 (I2), which could synchronously trigger two hybridization chain reactions (HCRs), resulting in the in situ formation of DNA nanoladders. The desired DNA nanoladders not only were employed as ideal nanocarriers for enzyme loading, but also maintained its catalytic activity. With the help of hydrogen peroxide (H2O2), manganese porphyrin (MnPP) with peroxidase-like activity accelerated the 4-chloro-1-naphthol (4-CN) oxidation with generation of insoluble precipitation on electrode, causing a very low differential pulse voltammetry (DPV) signal for quantitative determination of MMP-7. Under optimal conditions, the developed biosensor exhibited a wide linear ranging from 0.2 pg/mL to 20 ng/mL, and the detection limit was 0.05 pg/mL. This work successfully realized the combination of DNA signal amplification technique with artificial mimetic enzyme-catalyzed precipitation reaction in peptide cleavage-based protein detection, offering a promising avenue for the detection of other proteases.

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“…Supramolecular host–guest interaction can be viewed as a unique alternative for functionalization as it does not involve any covalent modification. − In the host–guest interaction, the hydrophobic cavity of cyclodextrin (CD), cucurbituril, and calixarene can incorporate guest molecules (or a part of guest molecules) via noncovalent and weak interactions. − Such host–guest interaction has been successfully utilized for functionalization of 2D surfaces, , nanoparticles, − cell membranes, and polymers/dendrimers. − Moreover, such type of functional materials have been used in drug delivery, , biosensing, − and other biomedical applications . However, in all these host–guest approaches, only selected host–guest molecules (e.g.…”

Section: Introductionmentioning

confidence: 99%

Supramolecular Host–Guest Chemistry-Based Folate/Riboflavin Functionalization and Cancer Cell Labeling of Nanoparticles

2017

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Nanoparticle-based cellular probes are commonly designed via covalent conjugation with affinity biomolecules. Those nanobioconjugates selectively interact with cell surface receptors and induce endocytosis followed by intracellular trafficking. However, this approach requires functional modification of biomolecules that may alter their biochemical activity. Here, we show that supramolecular host–guest chemistry can be utilized as an alternative approach in nanoparticle functionalization and selective cell labeling. We have used cyclodextrin-conjugated quantum dots (QDs) for supramolecular host–guest interaction-based functionalization with folate (QD-folate) and riboflavin (QD-riboflavin), where cyclodextrin acts as a host for the folate/riboflavin guest. We demonstrate that QD-folate and QD-riboflavin selectively label cells that have over-expressed folate/riboflavin receptors and induce the endocytosis pathway similar to covalently conjugated folate-/riboflavin-based nanoprobes. However, labeling is highly sensitive to the molar ratio of folate/riboflavin to cyclodextrin and incubation time. The presented functionalization/labeling approach is unique as it does not require covalent conjugation and may be extended for in vivo targeting application via simultaneous delivery of host and guest molecules.

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Supramolecular Peptide/Surface Assembly for Monitoring Proteinase Activity and Cancer Diagnosis

Cited by 5 publications

References 45 publications

Energy Landscape Mapping and Replica Exchange Molecular Dynamics of an Adsorbed Peptide

Energy Landscape Mapping and Replica Exchange Molecular Dynamics of an Adsorbed Peptide

DNA Enzyme-Decorated DNA Nanoladders as Enhancer for Peptide Cleavage-Based Electrochemical Biosensor

Supramolecular Host–Guest Chemistry-Based Folate/Riboflavin Functionalization and Cancer Cell Labeling of Nanoparticles

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