Rong Ni

Peptides Organized as Bilayer Membranes

From the organizing poten-tial of two-dimensional phospholipid membranes to theinformation-rich DNA helices, from the mechanical actinand tubulin cables to the structural collagen and elastinnetworks, these self-assembling asymmetric arrays define thearchitectures of all cells and tissues. Recent covalent hybridsof traditional biological macromolecular families (e.g.,nucleic acids with proteins

Kinetic Intermediates in Amyloid Assembly

In contrast to an expected Ostwald-like ripening of amyloid assemblies, the nucleating core of the Dutch mutant of the Aβ peptide of Alzheimers disease assembles through a series of conformational transitions. Structural characterization of the intermediate assemblies by isotope-edited IR and solid-state NMR reveals unexpected strand orientation intermediates and suggests new nucleation mechanisms in a progressive assembly pathway.

Peptide membranes in chemical evolution

Simple surfactants achieve remarkable long-range order in aqueous environments. This organizing potential is seen most dramatically in biological membranes where phospholipid assemblies both define cell boundaries and provide a ubiquitous structural scaffold for controlling cellular chemistry. Here we consider simple peptides that also spontaneously assemble into exceptionally ordered scaffolds, and review early data suggesting that these structures maintain the functional diversity of proteins. We argue that such scaffolds can achieve the required molecular order and catalytic agility for the emergence of chemical evolution.

Piezoelectric quartz crystal sensor array with optimized oscillator circuit for analysis of organic vapors mixtures

Abstract An array of piezoelectric quartz crystal sensors (PQCs) has been prepared for analyzing organic vapor mixtures. The circuit of oscillators has been modified and optimized to circumvent the problems associated with mutual interference among different oscillators connecting to sensors in the array. Organic coating materials were clustered into four groups according to their polarity and compounds representing different groups were selected including silicone OV-101, silicone OV-17, silicone OV-275, span 85, and polyethylene glycol 1000. The sensor array constructed gives characteristic response patterns for different organic vapors such as methanol, 1,2-dichloroethane, benzene and cyclohexane. The feasibility of using the sensor array for analysis of binary and tertiary mixtures has been tested by using PLS and MLR data treatment algorithms.

Nucleobase-Directed Amyloid Nanotube Assembly

Cytosine nucleobases were successfully incorporated into the side chain of the self-assembling amyloid peptide fragment HHQALVFFA to give ccAQLVFFA. At a pH range of 3-4, where cytosine is expected to be partially protonated, small-angle X-ray scattering analyses revealed the nucleobase peptide assembles to be well-defined nanotubes with an outer diameter of 24.8 nm and wall thicknesses of 3.3 nm. FT-IR and X-ray diffraction confirmed beta-sheet-rich assembly with the characteristic cross-beta architecture of amyloid. The beta-sheet registry, determined by measuring (13)CO-(13)CO backbone distances with solid-state NMR and linear dichroism, placed the cytosine bases roughly perpendicular to the nanotube axis, resulting in a model where the complementary interactions between the cytosine bases increases beta-sheet stacking to give the nanotube architecture. These scaffolds then extend the templates used to encode biological information beyond the nucleic acid duplexes and into covalent networks whose self-assembly is still defined by a precise complementarity of the side-chain registry.

Virus-Inspired Nucleic Acid Delivery System: Linking Virus and Viral Mimicry

Targeted delivery of nucleic acids into disease sites of human body has been attempted for decades, but both viral and non-viral vectors are yet to meet our expectations. Safety concerns and low delivery efficiency are the main limitations of viral and non-viral vectors, respectively. The structure of viruses is both ordered and dynamic, and is believed to be the key for effective transfection. Detailed understanding of the physical properties of viruses, their interaction with cellular components, and responses towards cellular environments leading to transfection would inspire the development of safe and effective non-viral vectors. To this goal, this review systematically summarizes distinctive features of viruses that are implied for efficient nucleic acid delivery but not yet fully explored in current non-viral vectors. The assembly and disassembly of viral structures, presentation of viral ligands, and the subcellular targeting of viruses are emphasized. Moreover, we describe the current development of cationic material-based viral mimicry (CVM) and structural viral mimicry (SVM) in these aspects. In light of the discrepancy, we identify future opportunities for rational design of viral mimics for the efficient delivery of DNA and RNA.

Tuning the Inter-nanofibril Interaction to Regulate the Morphology and Function of Peptide/DNA Co-assembled Viral Mimics

The ability to tune the inter-subunit interaction within the virus capsid may be critical to assembly and biological function. This process was extended here with peptide/DNA co-assembled viral mimics. The resulting co-assemblies, formed and stabilized by both peptide nanofibril-DNA and peptide nanofibril-nanofibril interactions, were tuned through hydrophobic packing interactions of the peptide sequences. By strengthening peptide side-chain complementarity and/or elongating the peptide chain (from 4 to 8 residues), we report strengthening the inter-nanofibril interaction to create stable nanococoons that give high gene-transfection efficacy.

Ultrasound-facilitated assembly and disassembly of a pH-sensitive self-assembly peptide

In this report, we investigated the impact of external stimulus (ultrasound) and internal stimulus (pH) on peptide assembly and disassembly. Two short rationally designed peptides K3C6SPD and F20H differing in the presence of a single pH-sensitive histidine residue were studied as the model peptides. The assembly kinetics studies demonstrated that the substitution of phenylalanine in K3C6SPD with histidine (F20H) significantly slowed down the peptide assembly rate at all three tested pHs (pH 9.5, pH 7.4 and pH 5.0). At the same time, this F to H substitution led to the increased pH-responsive assembly kinetics. By treating the peptide sample at the beginning of the assembly process at pH 9.5 for 5 min with the ultrasound power of 2.1 W cm−2, the assembly rate of peptide F20H was significantly accelerated with the lag phase being shortened from 10 days to 2 days. For the disassembly of F20H peptide nanofibrils preformed at pH 9.5, upon pH adjustment from pH 9.5 to pH 5.0, 5 min ultrasonication of the nanofibrils resulted in the nanofibril disassembly within 6 hours, instead of 5 days in the absence of ultrasound. On the contrary, similar ultrasound treatment of the peptide K3C6SPD did not produce any obvious effect on both assembly and disassembly processes. This study offers an effective strategy to modulate the stimuli-responsiveness of the peptide-based biomaterials.

Polymeric Vesicle Formation via Temperature-Assisted Nanoprecipitation

We here report an easy and efficient strategy to prepare submicron-sized polymeric vesicles with tetrahydrofuran (THF) as a good solvent through temperature-assisted nanoprecipitation (TAN). While conventional nanoprecipitation did not yield vesicles from block co-polymers (PEG-b-PCL), TAN produced vesicles with morphology and membrane thickness similar to those obtained by film rehydration method. Elevated temperature to allow fast evaporation of THF was identified to be the key process parameter of TAN.