Marta J. Krysmann

Formation Mechanism of Carbogenic Nanoparticles with Dual Photoluminescence Emission

We present a systematic investigation of the formation mechanism of carbogenic nanoparticles (CNPs), otherwise referred to as C-dots, by following the pyrolysis of citric acid (CA)-ethanolamine (EA) precursor at different temperatures. Pyrolysis at 180 °C leads to a CNP molecular precursor with a strongly intense photoluminescence (PL) spectrum and high quantum yield formed by dehydration of CA-EA. At higher temperatures (230 °C) a carbogenic core starts forming and the PL is due to the presence of both molecular fluorophores and the carbogenic core. CNPs that exhibit mostly or exclusively PL arising from carbogenic cores are obtained at even higher temperatures (300 and 400 °C, respectively). Since the molecular fluorophores predominate at low pyrolysis temperatures while the carbogenic core starts forming at higher temperatures, the PL behavior of CNPs strongly depends on the conditions used for their synthesis.

Self-Assembly and Hydrogelation of an Amyloid Peptide Fragment

The self-assembly of a fragment of the amyloid beta peptide that has been shown to be critical in amyloid fibrillization has been studied in aqueous solution. There are conflicting reports in the literature on the fibrillization of Abeta (16-20), i.e., KLVFF, and our results shed light on this. In dilute solution, self-assembly of NH 2-KLVFF-COOH is strongly influenced by aromatic interactions between phenylalanine units, as revealed by UV spectroscopy and circular dichroism. Fourier transform infrared (FTIR) spectroscopy reveals beta-sheet features in spectra taken for more concentrated solutions and also dried films. X-ray diffraction and cryo-transmission electron microscopy (cryo-TEM) provide further support for beta-sheet amyloid fibril formation. A comparison of cryo-TEM images with those from conventional dried and negatively stained TEM specimens highlights the pronounced effects of sample preparation on the morphology. A comparison of FTIR data for samples in solution and dried samples also highlights the strong effect of drying on the self-assembled structure. In more concentrated phosphate-buffered saline (PBS) solution, gelation of NH 2-KLVFF-COOH is observed. This is believed to be caused by screening of the electrostatic charge on the peptide, which enables beta sheets to aggregate into a fibrillar gel network. The rheology of the hydrogel is probed, and the structure is investigated by light scattering and small-angle X-ray scattering.

Gd(III)-doped carbon dots as a dual fluorescent-MRI probe

We describe the synthesis of Gd(III)-doped carbon dots as dual fluorescence-MRI probes for biomedical applications. The derived Gd(III)-doped carbon dots show uniform particle size (3–4 nm) and gadolinium distribution and form stable dispersions in water. More importantly, they exhibit bright fluorescence, strong T1-weighted MRI contrast and low cytotoxicity.

Self-Assembly of Peptide Nanotubes in an Organic Solvent

The self-assembly of a modified fragment of the amyloid beta peptide, based on sequence Abeta(16-20), KLVFF, extended to give AAKLVFF is studied in methanol. Self-assembly into peptide nanotubes is observed, as confirmed by electron microscopy and small-angle X-ray scattering. The secondary structure of the peptide is probed by FTIR and circular dichroism, and UV/visible spectroscopy provides evidence for the important role of aromatic interactions between phenylalanine residues in driving beta-sheet self-assembly. The beta-sheets wrap helically to form the nanotubes, the nanotube wall comprising four wrapped beta-sheets. At higher concentration, the peptide nanotubes form a nematic phase that exhibits spontaneous flow alignment as observed by small-angle neutron scattering.

Fibrillisation of hydrophobically modified amyloid peptide fragments in an organic solvent

The self-assembly of a hydrophobically modified fragment of the amyloid β (Aβ) peptide has been studied in methanol. The peptide FFKLVFF is based on Aβ(16-20) extended at the N terminus by two phenylalanine residues. The formation of amyloid-type fibrils is confirmed by Congo Red staining, thioflavin T fluorescence and circular dichroism experiments. FTIR points to the formation of β-sheet structures in solution and in dried films and suggests that aggregation occurs at low concentration and is not strongly affected by further increase in concentration, i.e. the peptide is a strong fibril-former in methanol. UV fluorescence experiments on unstained peptide and CD point to the importance of aromatic interactions between phenylalanine groups in driving aggregation into β-sheets. The CD spectrum differs from that usually observed for β-sheet assemblies formed by larger peptides or proteins and this is discussed for solutions in methanol and also trifluoroethanol. The fibril structure is imaged by transmission electron microscopy and scanning electron microscopy on dried samples and is confirmed by small-angle X-ray scattering experiments in solution.

Effect of PEG Crystallization on the Self-Assembly of PEG/Peptide Copolymers Containing Amyloid Peptide Fragments

The effect of poly(ethylene glycol) PEG crystallization on beta-sheet fibril formation is studied for a series of three peptide/PEG conjugates containing fragments modified from the amyloid beta peptide, specifically KLVFF, FFKLVFF, and AAKLVFF. These are conjugated to PEG with M n = 3300 g mol (-1). It is found, via small-angle X-ray scattering, X-ray diffraction, atomic force microscopy, and polarized optical microscopy, that PEG crystallinity in dried samples can disturb fibrillization, in particular cross-beta amyloid structure formation, for the conjugate containing the weak fibrillizer KLVFF, whereas this is retained for the conjugates containing the stronger fibrillizers AAKLVFF and FFKLVFF. For these two samples, the alignment of peptide fibrils also drives the orientation of the attached PEG chains. Our results highlight the importance of the antagonistic effects of PEG crystallization and peptide fibril formation in PEG/peptide conjugates.

Photoluminescent carbogenic nanoparticles directly derived from crude biomass

We present an environmentally benign, energy efficient and readily scalable approach to synthesize photoluminescent carbogenic nanoparticles directly from soft tissue biomass. Our approach relies on the pyrolytic decomposition of grass that gives rise to the formation of well-defined nanoparticles. The carbogenic nanoparticles can be readily surface modified, generating a series of highly selective photoluminescent materials that exhibit remarkable stability upon prolonged exposure to aggressive, high-temperature, high-salinity environment.

Nematic and Columnar Ordering of a PEG-Peptide Conjugate in Aqueous Solution

The self-assembly in aqueous solution of a PEG-peptide conjugate is studied by spectroscopy, electron microscopy, rheology and small-angle X-ray and neutron scattering (SAXS and SANS). The peptide fragment, FFKLVFF is based on fragment KLVFF of the amyloid beta-peptide, Abeta(16-20), extended by two hydrophobic phenylalanine units. This is conjugated to PEG which confers water solubility and leads to distinct self-assembled structures. Small-angle scattering reveals the formation of cylindrical fibrils comprising a peptide core and PEG corona. This constrained structure leads to a model parallel beta-sheet self-assembled structure with a radial arrangement of beta sheets. On increasing concentration, successively nematic and hexagonal columnar phases are formed. The flow-induced alignment of both structures was studied in situ by SANS using a Couette cell. Shear-induced alignment is responsible for the shear thinning behaviour observed by dynamic shear rheometry. Incomplete recovery of moduli after cessation of shear is consistent with the observation from SANS of retained orientation in the sample.

Synthesis and properties of core-shell fluorescent hybrids with distinct morphologies based on carbon dots

Fluorescent core–shell nanohybrids with the shells derived from carbon dots and cores differing in the chemical nature and morphology were synthesized. Hybrid nanoparticles combine fluorescence with other functionalities such as magnetic response on a single platform. These hybrids can be used in various bioapplications as demonstrated with labeling of stem cells.

Interactions of an anionic surfactant with poly(oxyalkylene) copolymers in aqueous solution.

The interactions of sodium dodecyl sulfate (SDS) with poly(ethylene oxide)/poly(alkylene oxide) (E/A) block copolymers are explored in this study. With respect to the specific compositional characteristics of the copolymer, introduction of SDS can induce fundamentally different effects to the self-assembly behavior of E/A copolymer solutions. In the case of the E(18)B(10)-SDS system (E = poly(ethylene oxide) and B = poly(butylene oxide)) development of large surfactant-polymer aggregates was observed. In the case of B(20)E(610)-SDS, B(12)E(227)B(12)-SDS, E(40)B(10)E(40)-SDS, E(19)P(43)E(19)-SDS (P = poly(propylene oxide)), the formation of smaller particles compared to pure polymeric micelles points to micellar suppression induced by the ionic surfactant. This effect can be ascribed to a physical binding between the hydrophobic block of unassociated macromolecules and the non-polar tail of the surfactant. Analysis of critical micelle concentrations (cmc(*)) of polymer-surfactant aqueous solutions within the framework of regular solution theory for binary surfactants revealed negative deviations from ideal behavior for E(40)B(10)E(40)-SDS and E(19)P(43)E(19)-SDS, but positive deviations for E(18)B(10)-SDS. Ultrasonic studies performed for the E(19)P(43)E(19)-SDS system enabled the identification of three distinct regions, corresponding to three main steps of the complexation; SDS absorption to the hydrophobic backbone of polymer, development of polymer-surfactant complexes and gradual breakdown of the mixed aggregates.