Publications by authors named "Dimitrios Priftis"

The global spread of COVID-19 led the World Health Organization to declare a pandemic on 11 March 2020. To decelerate this spread, countries have taken strict measures that have affected the lifestyles and economies. Various studies have focused on the identification of COVID-19's impact on the mental health of children and adolescents via traditional statistical approaches.

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Due to their unique structure, the optical and mechanical properties graphene and its derivatives ( graphene oxide, reduced graphene oxide) have captured the attention of a constantly increasing number of scientists with regards to biomolecule sensing. This mini review focuses on one specific type of sensor, that consisting of graphene and polyelectrolytes. Polyelectrolyte-graphene nanocomposites exhibit outstanding detection capabilities by synergistically combining the characteristics of both components, outperforming traditional sensors in many cases.

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Reported is the ability of α-helical polypeptides to self-assemble with oppositely-charged polypeptides to form liquid complexes while maintaining their α-helical secondary structure. Coupling the α-helical polypeptide to a neutral, hydrophilic polymer and subsequent complexation enables the formation of nanoscale coacervate-core micelles. While previous reports on polypeptide complexation demonstrated a critical dependence of the nature of the complex (liquid versus solid) on chirality, the α-helical structure of the positively charged polypeptide prevents the formation of β-sheets, which would otherwise drive the assembly into a solid state, thereby, enabling coacervate formation between two chiral components.

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Polyelectrolyte complexes present new opportunities for self-assembled soft matter. Factors determining whether the phase of the complex is solid or liquid remain unclear. Ionic polypeptides enable examination of the effects of stereochemistry on complex formation.

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Proteins have gained increasing success as therapeutic agents; however, challenges exist in effective and efficient delivery. In this work, we present a simple and versatile method for encapsulating proteins via complex coacervation with oppositely charged polypeptides, poly(l-lysine) (PLys) and poly(d/l-glutamic acid) (PGlu). A model protein system, bovine serum albumin (BSA), was incorporated efficiently into coacervate droplets via electrostatic interaction up to a maximum loading of one BSA per PLys/PGlu pair and could be released under conditions of decreasing pH.

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We consider polyelectrolyte solutions which, under suitable conditions, phase separate into a liquid-like coacervate phase and a coexisting supernatant phase that exhibit an extremely low interfacial tension. Such interfacial tension provides the basis for most coacervate-based applications, but little is known about it, including its dependence on molecular weight, charge density, and salt concentration. By combining a Debye-Hückel treatment for electrostatic interactions with the Cahn-Hilliard theory, we derive explicit expressions for this interfacial tension.

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This study is aimed at understanding the complex coacervation of two systems: branched poly(ethyleneimine) with linear poly(D,L-glutamic acid) or poly(D,L-aspartic acid), and identify differences and similarities with previously reported systems. Three different techniques (turbidity, isothermal titration microcalorimetry-ITC and rheology) were used in a comprehensive study of coacervation. Sample turbidity was used to show how various parameters (salt, stoichiometry, pH, temperature) affect complex coacervation.

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Carbon nanotubes (CNTs) represent one of the most promising materials in nanoscience today, with their unique electronic, chemical and mechanical properties. Strong van der Waals interactions and poor solubility greatly affect their potential for applications in various fields. In the past decade, great efforts have been undertaken to modify CNTs into organophilic material via covalent and non-covalent grafting strategies.

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The interactions between a series of oppositely charged polypeptide pairs are probed using isothermal titration calorimetry (ITC) in combination with turbidity measurements and optical microscopy. Polypeptide complex coacervation is described as a sequence of two distinct binding steps using an empirical extension of a simple ITC binding model. The first step consists of the formation of soluble complexes from oppositely charged polypeptides (ion pairing), which in turn aggregate into insoluble interpolymer complexes in the second step (complex coacervation).

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A systematic study of the interfacial energy (γ) of polypeptide complex coacervates in aqueous solution was performed using a surface forces apparatus (SFA). Poly(L-lysine hydrochloride) (PLys) and poly(L-glutamic acid sodium salt) (PGA) were investigated as a model pair of oppositely charged weak polyelectrolytes. These two synthetic polypeptides of natural amino acids have identical backbones and differ only in their charged side groups.

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