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1.
Integr Biol (Camb) ; 2020 Mar 20.
Artigo em Inglês | MEDLINE | ID: mdl-32195539

RESUMO

The blood-brain barrier plays a critical role in delivering oxygen and nutrients to the brain while preventing the transport of neurotoxins. Predicting the ability of potential therapeutics and neurotoxicants to modulate brain barrier function remains a challenge due to limited spatial resolution and geometric constraints offered by existing in vitro models. Using soft lithography to control the shape of microvascular tissues, we predicted blood-brain barrier permeability states based on structural changes in human brain endothelial cells. We quantified morphological differences in nuclear, junction, and cytoskeletal proteins that influence, or indicate, barrier permeability. We established a correlation between brain endothelial cell pair structure and permeability by treating cell pairs and tissues with known cytoskeleton-modulating agents, including a Rho activator, a Rho inhibitor, and a cyclic adenosine monophosphate analog. Using this approach, we found that high-permeability cell pairs showed nuclear elongation, loss of junction proteins, and increased actin stress fiber formation, which were indicative of increased contractility. We measured traction forces generated by high- and low-permeability pairs, finding that higher stress at the intercellular junction contributes to barrier leakiness. We further tested the applicability of this platform to predict modulations in brain endothelial permeability by exposing cell pairs to engineered nanomaterials, including gold, silver-silica, and cerium oxide nanoparticles, thereby uncovering new insights into the mechanism of nanoparticle-mediated barrier disruption. Overall, we confirm the utility of this platform to assess the multiscale impact of pharmacological agents or environmental toxicants on blood-brain barrier integrity.

2.
Nanoscale ; 11(38): 17878-17893, 2019 Oct 03.
Artigo em Inglês | MEDLINE | ID: mdl-31553035

RESUMO

Engineered nanomaterials (ENMs) are increasingly used in consumer products due to their unique physicochemical properties, but the specific hazards they pose to the structural and functional integrity of endothelial barriers remain elusive. When assessing the effects of ENMs on vascular barrier function, endothelial cell monolayers are commonly used as in vitro models. Monolayer models, however, do not offer a granular understanding of how the structure-function relationships between endothelial cells and tissues are disrupted due to ENM exposure. To address this issue, we developed a micropatterned endothelial cell pair model to quantitatively evaluate the effects of 10 ENMs (8 metal/metal oxides and 2 organic ENMs) on multiple cellular parameters and determine how these parameters correlate to changes in vascular barrier function. This minimalistic approach showed concerted changes in endothelial cell morphology, intercellular junction formation, and cytoskeletal organization due to ENM exposure, which were then quantified and compared to unexposed pairs using a "similarity scoring" method. Using the cell pair model, this study revealed dose-dependent changes in actin organization and adherens junction formation following exposure to representative ENMs (Ag, TiO2 and cellulose nanocrystals), which exhibited trends that correlate with changes in tissue permeability measured using an endothelial monolayer assay. Together, these results demonstrate that we can quantitatively evaluate changes in endothelial architecture emergent from nucleo-cytoskeletal network remodeling using micropatterned cell pairs. The endothelial pair model therefore presents potential applicability as a standardized assay for systematically screening ENMs and other test agents for their cellular-level structural effects on vascular barriers.


Assuntos
Núcleo Celular/metabolismo , Células Endoteliais da Veia Umbilical Humana/metabolismo , Modelos Biológicos , Nanopartículas/química , Células Endoteliais da Veia Umbilical Humana/citologia , Humanos
3.
ACS Appl Mater Interfaces ; 11(37): 33535-33547, 2019 Sep 18.
Artigo em Inglês | MEDLINE | ID: mdl-31369233

RESUMO

Engineering bioscaffolds for improved cutaneous tissue regeneration remains a healthcare challenge because of the increasing number of patients suffering from acute and chronic wounds. To help address this problem, we propose to utilize alfalfa, an ancient medicinal plant that contains antibacterial/oxygenating chlorophylls and bioactive phytoestrogens, as a building block for regenerative wound dressings. Alfalfa carries genistein, which is a major phytoestrogen known to accelerate skin repair. The scaffolds presented herein were built from composite alfalfa and polycaprolactone (PCL) nanofibers with hydrophilic surface and mechanical stiffness that recapitulate the physiological microenvironments of skin. This composite scaffold was engineered to have aligned nanofibrous architecture to accelerate directional cell migration. As a result, alfalfa-based composite nanofibers were found to enhance the cellular proliferation of dermal fibroblasts and epidermal keratinocytes in vitro. Finally, these nanofibers exhibited reproducible regenerative functionality by promoting re-epithelialization and granulation tissue formation in both mouse and human skin, without requiring additional proteins, growth factors, or cells. Overall, these findings demonstrate the potential of alfalfa-based nanofibers as a regenerative platform toward accelerating cutaneous tissue repair.


Assuntos
Derme , Queratinócitos , Medicago sativa/química , Nanocompostos , Nanofibras , Cicatrização/efeitos dos fármacos , Linhagem Celular , Derme/lesões , Derme/metabolismo , Derme/patologia , Humanos , Queratinócitos/metabolismo , Queratinócitos/patologia , Nanocompostos/química , Nanocompostos/uso terapêutico , Nanofibras/química , Nanofibras/uso terapêutico , Poliésteres/química
4.
Langmuir ; 35(6): 2270-2282, 2019 Feb 12.
Artigo em Inglês | MEDLINE | ID: mdl-30642185

RESUMO

The co-assembly behavior of peptide-π-peptide and peptide-alkyl-peptide triblock molecules that form one-dimensional (1D) nanostructures under acidic, aqueous environments is dependent on the peptide sequence and the torsional constraints imposed within the nanomaterial volume. Although a hydrophilic tripeptide sequence (Asp-Asp-Asp, DDD-) previously promoted isolation/dilution of minority π-electron components in the matrix of aliphatic peptides, a ß-sheet promoting sequence (Asp-Val-Val, DVV-) led to blocks of the two components distributed within larger 1D self-assembled nanostructures. Furthermore, torsional restrictions exerted on the oligoaromatic π-electron unit by the self-assembly process can lead to changes in its conformation (for example, planarity), which has ramifications on its functionality within the peptide matrix. Here, we study this impact on thiophene-based π-electron units with inherently different geometries, viz., relatively planar 2,2':5',2″:5″,2‴-quaterthiophene and 3″,4'-dimethyl-2,2':5',2″:5″,2‴-quaterthiophene, which is twisted at the core bithiophene unit due to the presence of two methyl groups. These peptides were co-assembled at 5 and 20 mol % with peptide- n-decyl-peptide triblock molecules, and the resultant assemblies were studied using UV-vis absorption, photoluminescence, and circular dichroism spectroscopies. We found that torsional restriction in dimethylated quaterthiophene units can impact the stacking behavior of these 1D peptide nanoassemblies and have consequences on their photophysical properties. Additionally, these insights help in the understanding of the dependence of the optoelectronic properties of these materials on both the intrinsic conformation of π-units and the geometric constraints imposed by their immediate local environment under aqueous conditions.

5.
Nano Lett ; 19(2): 793-804, 2019 02 13.
Artigo em Inglês | MEDLINE | ID: mdl-30616354

RESUMO

Understanding the uptake and transport dynamics of engineered nanomaterials (ENMs) by mammalian cells is an important step in designing next-generation drug delivery systems. However, to track these materials and their cellular interactions, current studies often depend on surface-bound fluorescent labels, which have the potential to alter native cellular recognition events. As a result, there is still a need to develop methods capable of monitoring ENM-cell interactions independent of surface modification. Addressing these concerns, here we show how scatter enhanced phase contrast (SEPC) microscopy can be extended to work as a generalized label-free approach for monitoring nanoparticle uptake and transport dynamics. To determine which materials can be studied using SEPC, we turn to Lorenz-Mie theory, which predicts that individual particles down to ∼35 nm can be observed. We confirm this experimentally, demonstrating that SEPC works for a variety of metal and metal oxides, including Au, Ag, TiO2, CeO2, Al2O3, and Fe2O3 nanoparticles. We then demonstrate that SEPC microscopy can be used in a quantitative, time-dependent fashion to discriminate between distinct modes of active cellular transport, including intracellular transport and membrane-assisted transport. Finally, we combine this technique with microcontact printing to normalize transport dynamics across multiple cells, allowing for a careful study of ensemble TiO2 nanoparticle uptake. This revealed three distinct regions of particle transport across the cell, indicating that membrane dynamics play an important role in regulating particle flow. By avoiding fluorescent labels, SEPC allows for a rational exploration of the surface properties of nanomaterials in their native state and their role in endocytosis and cellular transport.


Assuntos
Microscopia de Contraste de Fase/instrumentação , Nanopartículas/metabolismo , Transporte Biológico , Endocitose , Desenho de Equipamento , Células Endoteliais da Veia Umbilical Humana , Humanos , Metais/análise , Metais/metabolismo , Microscopia de Contraste de Fase/métodos , Nanopartículas/análise , Óxidos/análise , Óxidos/metabolismo , Propriedades de Superfície
6.
Anal Bioanal Chem ; 410(24): 6141-6154, 2018 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-29744562

RESUMO

Due to the unique physicochemical properties exhibited by materials with nanoscale dimensions, there is currently a continuous increase in the number of engineered nanomaterials (ENMs) used in consumer goods. However, several reports associate ENM exposure to negative health outcomes such as cardiovascular diseases. Therefore, understanding the pathological consequences of ENM exposure represents an important challenge, requiring model systems that can provide mechanistic insights across different levels of ENM-based toxicity. To achieve this, we developed a mussel-inspired 3D microphysiological system (MPS) to measure cardiac contractility in the presence of ENMs. While multiple cardiac MPS have been reported as alternatives to in vivo testing, most systems only partially recapitulate the native extracellular matrix (ECM) structure. Here, we show how adhesive and aligned polydopamine (PDA)/polycaprolactone (PCL) nanofiber can be used to emulate the 3D native ECM environment of the myocardium. Such nanofiber scaffolds can support the formation of anisotropic and contractile muscular tissues. By integrating these fibers in a cardiac MPS, we assessed the effects of TiO2 and Ag nanoparticles on the contractile function of cardiac tissues. We found that these ENMs decrease the contractile function of cardiac tissues through structural damage to tissue architecture. Furthermore, the MPS with embedded sensors herein presents a way to non-invasively monitor the effects of ENM on cardiac tissue contractility at different time points. These results demonstrate the utility of our MPS as an analytical platform for understanding the functional impacts of ENMs while providing a biomimetic microenvironment to in vitro cardiac tissue samples. Graphical Abstract Heart-on-a-chip integrated with mussel-inspired fiber scaffolds for a high-throughput toxicological assessment of engineered nanomaterials.


Assuntos
Bivalves , Coração/efeitos dos fármacos , Dispositivos Lab-On-A-Chip , Nanofibras/toxicidade , Nanoestruturas/toxicidade , Tecidos Suporte , Adesivos , Animais , Células Cultivadas , Técnicas In Vitro , Indóis/química , Microscopia Eletrônica de Varredura , Miócitos Cardíacos/citologia , Poliésteres/química , Polímeros/química , Ratos , Ratos Sprague-Dawley , Espectroscopia de Infravermelho com Transformada de Fourier
7.
ACS Cent Sci ; 3(9): 986-994, 2017 Sep 27.
Artigo em Inglês | MEDLINE | ID: mdl-28979940

RESUMO

Advances in supramolecular assembly have enabled the design and synthesis of functional materials with well-defined structures across multiple length scales. Biopolymer-synthetic hybrid materials can assemble into supramolecular structures with a broad range of structural and functional diversity through precisely controlled noncovalent interactions between subunits. Despite recent progress, there is a need to understand the mechanisms underlying the assembly of biohybrid/synthetic molecular building blocks, which ultimately control the emergent properties of hierarchical assemblies. In this work, we study the concentration-driven self-assembly and gelation of π-conjugated synthetic oligopeptides containing different π-conjugated cores (quaterthiophene and perylene diimide) using a combination of particle tracking microrheology, confocal fluorescence microscopy, optical spectroscopy, and electron microscopy. Our results show that π-conjugated oligopeptides self-assemble into ß-sheet-rich fiber-like structures at neutral pH, even in the absence of electrostatic screening of charged residues. A critical fiber formation concentration cfiber and a critical gel concentration cgel are determined for fiber-forming π-conjugated oligopeptides, and the linear viscoelastic moduli (storage modulus G' and loss modulus G″) are determined across a wide range of peptide concentrations. These results suggest that the underlying chemical structure of the synthetic π-conjugated cores greatly influences the self-assembly process, such that oligopeptides appended to π-conjugated cores with greater torsional flexibility tend to form more robust fibers upon increasing peptide concentration compared to oligopeptides with sterically constrained cores. Overall, our work focuses on the molecular assembly of π-conjugated oligopeptides driven by concentration, which is controlled by a combination of enthalpic and entropic interactions between oligopeptide subunits.

8.
Langmuir ; 33(30): 7435-7445, 2017 08 01.
Artigo em Inglês | MEDLINE | ID: mdl-28683194

RESUMO

Peptide nanostructures with built-in electronic functions offer a new platform for biomaterial science. In this report, we interrogate the influences of the immediate peptide environment around oligo(p-phenylenevinylene) (OPV3) electronic units embedded within one-dimensional peptide nanostructures on the resulting photophysics as assessed by UV-vis, photoluminescence (PL), and circular dichroism spectroscopies. To do so, we studied peptide-core-peptide molecules where the core was either OPV3 or an aliphatic n-decyl chain. Coassemblies of these molecules wherein the π-core was diluted as a minority component within a majority aliphatic matrix allowed for the variation of interchromophore exciton coupling commonly found in homoassemblies of peptide-OPV3-peptide monomers. Upon coassembly of the peptides, a hydrophilic tripeptide sequence (Asp-Asp-Asp-, DDD-) promoted the dilution/isolation of the peptide-π-peptide molecules in the majority peptide-decyl-peptide matrix whereas a hydrophobic tripeptide sequence (Asp-Val-Val-, DVV-) promoted the formation of self-associated stacks within the nanostructures. We also performed temperature variation studies to induce the reorganization of π-electron units in the spatially constrained n-decyl environment. This study elucidates the nonresonant (e.g., conformational) and local peptide field effects enforced within the internal environment of peptide nanomaterials and how they lead to varied photophysical properties of the embedded π-electron cores. It offers new insights on tuning the optoelectronic properties of these types of materials on the basis of the local electronic and steric environment available within the nanostructures.


Assuntos
Nanoestruturas , Conformação Molecular , Peptídeos , Polivinil
9.
J Am Chem Soc ; 139(25): 8685-8692, 2017 06 28.
Artigo em Inglês | MEDLINE | ID: mdl-28578581

RESUMO

We report a peptide-based multichromophoric hydrogelator system, wherein π-electron units with different inherent spectral energies are spatially controlled within peptidic 1-D nanostructures to create localized energy gradients in aqueous environments. This is accomplished by mixing different π-conjugated peptides prior to initiating self-assembly through solution acidification. We can vary the kinetics of the assembly and the degree of self-sorting through the choice of the assembly trigger, which changes the kinetics of acidification. The hydrolysis of glucono-δ-lactone (GdL) provides a slow pH drop that allows for stepwise triggering of peptide components into essentially self-sorted nanostructures based on subtle pKa differences, whereas HCl addition leads to a rapid formation of mixed components within a nanostructure. Using 1H NMR spectroscopy and fiber X-ray diffraction, we determine the conditions and peptide mixtures that favor self-sorting or intimate comixing. Photophysical investigations in the solution phase provide insight into the correlation of energy-transport processes occurring within the assemblies to the structural organization of the π-systems.


Assuntos
Hidrogéis/química , Peptídeos/química , Cinética , Espectroscopia de Ressonância Magnética , Microscopia Eletrônica de Transmissão , Estrutura Molecular , Nanoestruturas/química , Difração de Raios X
10.
Bioconjug Chem ; 28(3): 751-759, 2017 03 15.
Artigo em Inglês | MEDLINE | ID: mdl-28292179

RESUMO

Self-assembling peptides are extensively exploited as bioactive materials in applications such as regenerative medicine and drug delivery despite the fact that their relatively weak noncovalent interactions often render them susceptible to mechanical destruction and solvent erosion. Herein, we describe how covalent cross-linking enhances the mechanical stability of self-assembling π-conjugated peptide hydrogels. We designed short peptide-chromophore-peptide sequences displaying different reactive functional groups that can form cross-links with appropriately modified bifunctional polyethylene glycol (PEG)-based small guest molecules. These peptides self-assemble into one-dimensional fibrillar networks in response to pH in the aqueous environment. The cross-linking reactions were promoted to create a secondary network locked in place by covalent bonds within the physically cross-linked (preassembled) π-conjugated peptide strands. Rheology measurements were used to evaluate the mechanical modifications of the network, and the chemical changes that accompany the cross-linking were further confirmed by infrared spectroscopy. Furthermore, we modified these cross-linkable π-conjugates by incorporating extracellular matrix (ECM)-derived Ile-Lys-Val-Ala-Val (IKVAV) and Arg-Gly-Asp (RGD) bioactive epitopes to support human neural stem and progenitor cell (hNSCs) differentiation. The hNSCs undergo differentiation into neurons on IKVAV-derived π-conjugates while RGD-containing peptides failed to support cell attachment. These findings provide significant insight into the biochemical and electronic properties of π-conjugated peptide hydrogelators for creating artificial ECM to enable advanced tissue-engineering applications.


Assuntos
Materiais Biocompatíveis/química , Reagentes para Ligações Cruzadas/química , Hidrogéis/química , Laminina/química , Oligopeptídeos/química , Fragmentos de Peptídeos/química , Peptídeos/química , Polietilenoglicóis/química , Adesão Celular , Elétrons , Humanos , Células-Tronco Neurais/citologia , Neurogênese , Reologia , Engenharia Tecidual , Tecidos Suporte/química
11.
ACS Appl Mater Interfaces ; 9(4): 3977-3984, 2017 Feb 01.
Artigo em Inglês | MEDLINE | ID: mdl-28067038

RESUMO

Supramolecular assembly is a powerful method that can be used to generate materials with well-defined structures across multiple length scales. Supramolecular assemblies consisting of biopolymer-synthetic polymer subunits are specifically known to exhibit exceptional structural and functional diversity as well as programmable control of noncovalent interactions through hydrogen bonding in biopolymer subunits. Despite recent progress, there is a need to control and quantitatively understand assembly under nonequilibrium conditions. In this work, we study the nonequilibrium self-assembly of π-conjugated synthetic oligopeptides using a combination of experiments and analytical modeling. By isolating an aqueous peptide solution droplet within an immiscible organic layer, the rate of peptide assembly in the aqueous solution can be controlled by tuning the transport rate of acid that is used to trigger assembly. Using this approach, peptides are guided to assemble under reaction-dominated and diffusion-dominated conditions, with results showing a transition from a diffusion-limited reaction front to spatially homogeneous assembly as the transport rate of acid decreases. Interestingly, our results show that the morphology of self-assembled peptide fibers is controlled by the assembly kinetics such that increasingly homogeneous structures of self-assembled synthetic oligopeptides were generally obtained using slower rates of assembly. We further developed an analytical reaction-diffusion model to describe oligopeptide assembly, and experimental results are compared to the reaction-diffusion model across a range of parameters. Overall, this work highlights the importance of molecular self-assembly under nonequilibrium conditions, specifically showing that oligopeptide assembly is governed by a delicate balance between reaction kinetics and transport processes.

12.
ACS Nano ; 9(12): 12401-9, 2015 Dec 22.
Artigo em Inglês | MEDLINE | ID: mdl-26554697

RESUMO

π-Conjugated peptide materials are attractive for bioelectronics due to their unique photophysical characteristics, biofunctional interfaces, and processability under aqueous conditions. In order to be relevant for electrical applications, these types of materials must be able to support the passage of current and the transmission of applied voltages. Presented herein is an investigation of both the current and voltage transmission activities of one-dimensional π-conjugated peptide nanostructures. Observations of the nanostructures as both semiconducting and gate layers in organic field-effect transistors (OFETs) were made, and the effect of systematic changes in amino acid composition on the semiconducting/conducting functionality of the nanostructures was investigated. These molecular variations directly impacted the hole mobility values observed for the nanomaterial active layers over 3 orders of magnitude (∼0.02 to 5 × 10(-5) cm(2) V(-1) s(-1)) when the nanostructures had quaterthiophene cores and the assembled peptide materials spanned source and drain electrodes. Peptides without the quaterthiophene core were used as controls and did not show field-effect currents, verifying that the transport properties of the nanostructures rely on the semiconducting behavior of the π-electron core and not just ionic rearrangements. We also showed that the nanomaterials could act as gate electrodes and assessed the effect of varying the gate dielectric layer thickness in devices where the conventional organic semiconductor pentacene spanned the source and drain electrodes in a top-contact OFET, showing an optimum performance with 35-40 nm dielectric thickness. This study shows that these peptides that self-assemble in aqueous environments can be used successfully to transmit electronic signals over biologically relevant distances.


Assuntos
Nanoestruturas/química , Peptídeos/química , Transistores Eletrônicos , Eletrônica , Modelos Teóricos
13.
Bioconjug Chem ; 26(12): 2290-302, 2015 Dec 16.
Artigo em Inglês | MEDLINE | ID: mdl-26439806

RESUMO

Highly ordered arrays of π-conjugated molecules are often viewed as a prerequisite for effective charge-transporting materials. Studies involving these materials have traditionally focused on organic electronic devices, with more recent emphasis on biological systems. In order to facilitate the transition to biological environments, biomolecules that can promote hierarchical ordering and water solubility are often covalently appended to the π-electron unit. This review highlights recent work on π-conjugated systems bound to peptide moieties that exhibit self-assembly and aims to provide an overview on the development and emerging applications of peptide-based supramolecular π-electron systems.


Assuntos
Eletrônica/métodos , Elétrons , Nanoestruturas/química , Peptídeos/química , Corantes/química , Hidrocarbonetos Aromáticos/química , Modelos Moleculares , Polímero Poliacetilênico , Polímeros/química , Polivinil/química , Poli-Inos/química , Tiofenos/química
14.
Chem Sci ; 6(2): 1474-1484, 2015 Feb 01.
Artigo em Inglês | MEDLINE | ID: mdl-29560236

RESUMO

Steady-state and time-resolved photophysical measurements demonstrate energy transfer within π-conjugated peptide nanostructures composed of oligo-(p-phenylenevinylene)-based donor units and quaterthiophene-based acceptor units in completely aqueous environments. These peptide-based assemblies encourage energy migration along the stacking axis, thus resulting in the quenching of donor emission peaks along with the development of new spectral features reminiscent of acceptor emission. These spectral changes were observed even at minute amounts of the acceptor (starting at 1 mol%), suggesting that exciton migration is involved in energy transport and supporting a funnel-like energy transduction mechanism. The reversibility of nanostructure formation and the associated photophysical responses under different conditions (pH, temperature) were also studied. This unique material design incorporates two different semiconducting units coassembled within peptide nanostructures and offers a new platform for the engineering of energy migration through bioelectronic materials in aqueous environments.

15.
Langmuir ; 30(38): 11375-85, 2014 Sep 30.
Artigo em Inglês | MEDLINE | ID: mdl-25181015

RESUMO

This photophysical study characterizes the generality of intermolecular electronic interactions present within nanomaterials derived from self-assembling oligopeptides with embedded π-conjugated oligophenylenevinylene (OPV) subunits stilbene and distyrylbenzene that in principle present two distinct ß-sheet motifs. Two different synthetic approaches led to oligopeptides that upon self-assembly are expected to self-assemble into multimeric aggregates stabilized by ß-sheet-like secondary structures. The target molecules express either two C-termini linked to the central OPV core (symmetric peptides) or the more common N-termini to C-termini polarity typical of natural oligopeptides (nonsymmetric peptides). Both peptide secondary structures were shown to form extended 1-D peptide aggregates with intimate intermolecular π-electron interactions. Differences in length of the π-conjugated OPV segments resulted in differing extents of intermolecular interactions and the resulting photophysics. The peptides containing the shorter stilbene (OPV2) units showed little ground state interactions and resulted in excimeric emission, while the longer distyrylbenzene (OPV3) peptides had different ground state interactions between adjacent π-conjugated subunits resulting in either perturbed electronic properties arising from exciton coupling or excimer-like excited states. Molecular dynamics simulations of nascent aggregate formation predict peptide dimerization to be a spontaneous process, possessing thermodynamic driving potentials in the range 2-6 kcal/mol for the four molecules considered. Antiparallel stacking of the peptides containing an OPV3 subunit is thermodynamically favored over the parallel orientation, whereas both arrangements are equally favored for the peptides containing an OPV2 subunit. This study validates the generality of peptide-π-peptide self-assembly to provide electronically delocalized supramolecular structures and suggests flexibility in peptide sequence design as a way to tune the material properties of π-conjugated supramolecular polymers.


Assuntos
Nanoestruturas/química , Oligopeptídeos/química , Elétrons , Ligações de Hidrogênio , Simulação de Dinâmica Molecular , Estrutura Molecular , Estilbenos/química , Estirenos/química
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