Daohong Xia

Self-assembly of short peptide amphiphiles: the cooperative effect of hydrophobic interaction and hydrogen bonding.

The interplay between hydrogen bonding, hydrophobic interaction and the molecular geometry of amino acid side-chains is crucial to the development of nanostructures of short peptide amphiphiles. An important step towards developing their practical use is to understand how different amino acid side-chains tune hydrophobic interaction and hydrogen bonding and how this process leads to the control of the size and shape of the nanostructures. In this study, we have designed and synthesized three sets of short amphiphilic peptides (I(3)K, LI(2)K and L(3)K; L(3)K, L(4)K and L(5)K; I(3)K, I(4)K and I(5)K) and investigated how I and L affected their self-assembly in aqueous solution. The results have demonstrated a strong tendency of I groups to promote the growth of β-sheet hydrogen bonding and the subsequent formation of nanofibrillar shapes. All I(m)K (m = 3-5) peptides assembled into nanofibers with consistent β-sheet conformation, whereas the nanofiber diameters decreased as m increased due to geometrical constraint in peptide chain packing. In contrast, L groups had a weak tendency to promote β-sheet structuring and their hydrophobicity became dominant and resulted in globular micelles in L(3)K assembly. However, increase in the number of hydrophobic sequences to L(5)K induced β-sheet conformation due to the cooperative hydrophobic effect and the consequent formation of long nanofibers. The assembly of L(4)K was, therefore, intermediate between L(3)K and L(5)K, similar to the case of LI(2)K within the set of L(3)K, LI(2)K and I(3)K, with a steady transition from the dominance of hydrophobic interaction to hydrogen bonding. Thus, changes in hydrophobic length and swapping of L and I can alter the size and shape of the self-assembled nanostructures from these simple peptide amphiphiles.

Immobilization of Lipases on Alkyl Silane Modified Magnetic Nanoparticles: Effect of Alkyl Chain Length on Enzyme Activity

Background Biocatalytic processes often require a full recycling of biocatalysts to optimize economic benefits and minimize waste disposal. Immobilization of biocatalysts onto particulate carriers has been widely explored as an option to meet these requirements. However, surface properties often affect the amount of biocatalysts immobilized, their bioactivity and stability, hampering their wide applications. The aim of this work is to explore how immobilization of lipases onto magnetite nanoparticles affects their biocatalytic performance under carefully controlled surface modification. Methodology/Principal Findings Magnetite nanoparticles, prepared through a co-precipitation method, were coated with alkyl silanes of different alkyl chain lengths to modulate their surface hydrophobicity. Candida rugosa lipase was then directly immobilized onto the modified nanoparticles through hydrophobic interaction. Enzyme activity was assessed by catalytic hydrolysis of p-nitrophenyl acetate. The activity of immobilized lipases was found to increase with increasing chain length of the alkyl silane. Furthermore, the catalytic activities of lipases immobilized on trimethoxyl octadecyl silane (C18) modified Fe3O4 were a factor of 2 or more than the values reported from other surface immobilized systems. After 7 recycles, the activities of the lipases immobilized on C18 modified nanoparticles retained 65%, indicating significant enhancement of stability as well through hydrophobic interaction. Lipase immobilized magnetic nanoparticles facilitated easy separation and recycling with high activity retaining. Conclusions/Significance The activity of immobilized lipases increased with increasing alkyl chain length of the alkyl trimethoxy silanes used in the surface modification of magnetite nanoparticles. Lipase stability was also improved through hydrophobic interaction. Alkyl silane modified magnetite nanoparticles are thus highly attractive carriers for enzyme immobilization enabling efficient enzyme recovery and recycling.

Role of ovalbumin in the stabilization of metastable vaterite in calcium carbonate biomineralization

The role of proteins in biomineralization has been examined in this work by studying the effect of ovalbumin on the stabilization of metastable CaCO(3) phases. In the absence of ovalbumin, the mixing of Na(2)CO(3) with CaCl(2) in an aqueous solution led to the formation of metastable phases that swiftly transformed into stable calcite crystals within 4 h under the experimental conditions. However, ovalbumin was found to favor the formation and stabilization of spherical vaterites, and the effect was concentration dependent. In the presence of 2 g/L ovalbumin, for example, vaterite microspheres with diameters ranging from 0.9 to 3.0 mum, composed of much smaller nanosized particles, were produced and stabilized even after 24 h following the initial mixing. In addition, the influence of ovalbumin on the CaCO(3) mineralization process from the very beginning was carefully examined. Both amorphous calcium carbonate (ACC) and vaterite were favored with ovalbumin present, but the ACC phase formed predominantly at the initial stage of mixing followed by the vaterite formation. Vaterite could then be embedded further in the mineralization process and become stabilized many hours afterward. The stabilizing effect of ovalbumin could arise from the strong binding between carboxylate groups of ovalbumin and the calcium ions on the CaCO(3) surface, preventing the metastable CaCO(3) from transformation via dissolution-recrystallization processes. The strong ovalbumin adsorption on vaterite microspheres was revealed from transmission electron microscopy imaging and thermogravimetric analysis, thereby providing useful evidence to support the proposed stabilizing mechanism.

Influence of ovalbumin on CaCO3 precipitation during in vitro biomineralization.

As a major constituent of egg white matrix, ovalbumin has long been perceived to be implicated in the formation of avian eggshells, in particular, the mammillary layer. However, very little is known about the detailed mechanism by which this protein mediates shell calcification. By the combined studies of AFM, SEM, and TEM, we have investigated the influence of ovalbumin on CaCO(3) precipitation under in vitro mineralization conditions. We observed that the influence was multifold. This protein modified the morphology of calcite crystals through a distinct anisotropic process with respect to the four crystal step edges. AFM characterization revealed that the modification was initiated at the obtuse-obtuse step corner and propagated predominantly along the obtuse steps. Furthermore, the protein favored the existence of unstable phases such as amorphous calcium carbonate and crystalline vaterite. In contrast, lysozyme, another protein also present in the system, played a very different role in modifying calcite morphology. The mechanistic understanding gained from this study is clearly also of practical significance in developing advanced inorganic CaCO(3) materials with the aid of morphological manipulation of crystalline structures via different protein mediation.

Short peptide-directed synthesis of one-dimensional platinum nanostructures with controllable morphologies

Although one dimensional (1D) Pt nanostructures with well-defined sizes and shapes have fascinating physiochemical properties, their preparation remains a great challenge. Here we report an easy and novel synthesis of 1D Pt nanostructures with controllable morphologies, through the combination of designer self-assembling I3K and phage-displayed P7A peptides. The nanofibrils formed via I3K self-assembly acted as template. Pt precursors ((PtCl4)2− and (PtCl6)2−) were immobilized by electrostatic interaction on the positively charged template surface and subsequent reduction led to the formation of 1D Pt nanostructures. P7A was applied to tune the continuity of the Pt nanostructures. Here, the electrostatic repulsion between the deprotonated C-terminal carboxyl groups of P7A molecules was demonstrated to play a key role. We finally showed that continuous and ordered 1D Pt morphology had a significantly improved electrochemical performance for the hydrogen and methanol electro-oxidation in comparison with either 1D discrete Pt nanoparticle assemblies or isolated Pt nanoparticles.

Effects of anions on nanostructuring of cationic amphiphilic peptides

The effects of addition of a series of stoichiometric salts on the nanostructuring of cationic amphiphilic peptides have been investigated through the combination of atomic force microscopy (AFM), circular dichroism (CD), and turbidity measurements. The results revealed that anions had more pronounced effects than cations in tuning the nanostructures formed from these peptides. Addition of ClO(3)(-), NO(3)(-), and Br(-) could stabilize the primary nanostructures (nanostacks, nanospheres, or short nanorods) formed by A(9)K and I(3)K and effectively inhibit their growth into longer nanostructures (nanorods or nanotubes). In contrast, the anions of Cl(-), SO(4)(2-), HPO(4)(2-), PO(4)(3-), and C(6)H(5)O(7)(3-) (citrate) favored the axial growth of these peptides to form long intersecting nanofibrils and led to an increase in diameter and surface roughness, as well, clearly enhancing their propensity for nanostructuring. The efficiency of different anions in promoting the growth of peptide nanoaggregates into larger ones could be ordered as ClO(3)(-) < NO(3)(-) ≤ Br(-) < Cl(-) < SO(4)(2-) < HPO(4)(2-) < PO(4)(3-) < C(6)H(5)O(7)(3-), broadly consistent with the Hofmeister anion sequence. These observations were well rationalized by considering different aspects of direct interactions of the anions with the peptide molecules.

Tuning of peptide assembly through force balance adjustment.

Controlled self-assembly of amphiphilic tripeptides into distinct nanostructures is achieved via a controlled design of the molecular architecture. The tripeptide Ac-Phe-Phe-Lys-CONH2 (FFK), hardly soluble in water, forms long amyloid-like tubular structures with the aid of β-sheet hydrogen bonding and aromatic π-π stacking. Substitution of phenylalanine (F) with tyrosine (Y), that is, only a subtle structural variation in adding a hydroxyl group to the phenyl ring, results in great change in molecular self-assembly behavior. When one F is substituted with Y, the resulting molecules of FYK and YFK self-assemble into long thinner fibrils with high propensity for lateral association. When both Fs are substituted with Y, the resulting YYK molecule forms spherical aggregates. Introduction of hydroxyl groups into the molecule modifies aromatic interactions and introduces hydrogen bonding. Moreover, since the driving forces for peptide self-assembly including hydrogen bonding, electrostatic repulsion, and π-π stacking have high interdependence with each other, changes in aromatic interaction induce a Domino effect and cause a shift of force balance to a new state. This leads to significant variations in self-assembly behavior.

Structure and adsorptive desulfurization performance of the composite material MOF-5@AC

A composite material (MOF-5@AC) of MOF-5 and AC was successfully prepared. After characterization by a variety of means, it was shown that MOF-5 was covered on the surface of AC and existed in the form of microcrystals. A new micro-mesoporous pore appeared at 1.8–5 nm, while MOF-5 and AC are both microporous materials. And the thermal and water stability of MOF-5@AC is better than that of MOF-5. The adsorptive desulfurization experiment showed that the performance of the composite material was higher than that of the two parent materials, especially for the large molecular thiophenic sulfur compounds. And the reuse performance of MOF-5@AC after regeneration was also significantly improved compared the parent materials. The ratio of raw materials of composite materials plays an important role in the microstructure, morphology and desulfurization properties. After screening the ratio of raw materials, MOF-5@AC with a ratio of 1 : 5 showed the best desulfurization performance. The theoretical calculation results are in accordance with the desulfurization performance of the composite material (MOF-5@AC), which shows that MOF-5 is well dispersed on the AC surface and the pores are well exposed.

Molecular recognition with cyclodextrin polymer: a novel method for removing sulfides efficiently

A series of cyclodextrin polymers (CDPs) were synthesized and they were used for removing different sulfides by molecular recognition. Different CDPs showed a higher desulfurization efficiency for sulfides with an aromatic ring structure than those with an aliphatic chain structure. For different cyclodextrin polymers, β-CDP has a more suitable cavity size for removing DBT. Moreover, it has a good synergetic effect of adjacent cyclodextrin cavities and good electronic interactions with DBT. For these reasons, β-CDP showed the best desulfurization performance, in particular it has good performance for deep desulfurization by forming inclusion complexes and excellent selectivity for removing DBT. Meanwhile, the β-CDP showed good regeneration performance. Various characterization measurements were used to characterize the β-CDP before and after desulfurization of DBT, the results of which showed that it had advantages of wide application temperature range and good structure stability before and after desulfurization. Finally, a molecular recognition mechanism for removing sulfides efficiently was proposed.

Short peptide mediated self-assembly of platinum nanocrystals with selective spreading property

Spherical assemblies with core/shell configurations are prepared through C-terminal amidated short peptide mediated self-association of platinum nanocrystals. The interactions between the peptides might drive the self-assembly of platinum nanocrystals and determine their surface properties. Thus, the nanosize assemblies collapse and spread on a hydrophilic surface, whereas maintaining their spherical shapes on a hydrophobic surface.