Domain swapping in materials design.

Peptide self-assembly can be used as a bottom-up approach to material fabrication. Although many different types of materials can be prepared from peptides, hydrogels are perhaps one of the most common. Gels typically result from the self-assembly of peptides into fibrillar networks.

Effects of matrix composition, microstructure, and viscoelasticity on the behaviors of vocal fold fibroblasts cultured in three-dimensional hydrogel networks.

Vocal fold diseases and disorders are difficult to treat surgically or therapeutically. Tissue engineering offers an alternative strategy for the restoration of functional vocal folds. As a first step toward vocal fold tissue engineering, we investigated the responses of primary vocal fold fibroblasts (PVFFs) to two types of collagen and hyaluronic acid (HA)-based hydrogels that are compositionally similar, but structurally variable and mechanically different.

Structural Analysis and Mechanical Characterization of Hyaluronic Acid-Based Doubly Cross-Linked Networks.

We have created a new class of hyaluronic acid (HA)-based hydrogel materials with HA hydrogel particles (HGPs) embedded in and covalently cross-linked to a secondary network. HA HGPs with an average diameter of ∼900 nm and narrow particle size distribution were synthesized using a refined reverse micelle polymerization technique. The average mesh size of the HGPs was estimated to be approximately 5.

Helical-ribbon formation by a beta-amino acid modified amyloid beta-peptide fragment.

An addition to the family: The introduction of beta-amino acid residues into a modified amyloid beta peptide fragment resulted in well-defined helical nanoribbons (see cryo-TEM image) comprising beta strands mainly oriented perpendicular to the ribbon axis. The nanoribbons order into a flow-aligning nematic phase at higher concentration. The beta-strand nanoribbon structure is an addition to the known set of secondary structures adopted by beta-peptides.

Dependence of Self-Assembled Peptide Hydrogel Network Structure on Local Fibril Nanostructure.

Physically cross-linked, fibrillar hydrogel networks are formed by the self-assembly of β-hairpin peptide molecules with varying degrees of strand asymmetry. The peptide registry in the self-assembled state can be used as a design element to generate fibrils with twisting, nontwisting, or laminated morphology. The mass density of the networks varies significantly, and can be directly related to the local fibrillar morphology as evidenced by small angle neutron scattering (SANS) and in situ substantiation using cryogenic transmission electron microscopy (cryo-TEM) under identical concentrations and conditions.

Correlations between structure, material properties and bioproperties in self-assembled beta-hairpin peptide hydrogels.

A de novo designed beta-hairpin peptide (MAX8), capable of undergoing intramolecular folding and consequent intermolecular self-assembly into a cytocompatible hydrogel, has been studied. A combination of small angle neutron scattering (SANS) and cryogenic-transmission electron microscopy (cryo-TEM) have been used to quantitatively investigate the MAX8 nanofibrillar hydrogel network morphology. A change in the peptide concentration from 0.

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.

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.

De novo design of strand-swapped beta-hairpin hydrogels.

De novo designed peptides, capable of undergoing a thermally triggered beta-strand-swapped self-assembly event leading to hydrogel formation were prepared. Strand-swapping peptide 1 (SSP1) incorporates an exchangeable beta-strand domain composed of eight residues appended to a nonexchangeable beta-hairpin domain. CD shows that, at pH 9 and temperatures less than 35 degrees C, this peptide adopts a random coil conformation, rendering it soluble in aqueous solution.

Structural effects on the biodistribution and positron emission tomography (PET) imaging of well-defined (64)Cu-labeled nanoparticles comprised of amphiphilic block graft copolymers.

The synthesis of poly(methyl methacrylate-co-methacryloxysuccinimide-graft-poly(ethylene glycol)) (PMMA-co-PMASI-g-PEG) via living free radical polymerization provides a convenient route to well-defined amphiphilic graft copolymers having a controllable number of reactive functional groups, variable length PEG grafts, and low polydispersity. These copolymers were shown to form PMMA-core/PEG-shell nanoparticles upon hydrophobic collapse in water, with the hydrodynamic size being defined by the molecular weight of the backbone and the PEG grafts. Functionalization of these polymeric nanoparticles with a 1,4,7,10-tetraazacyclododecanetetraacetic acid (DOTA) ligand capable of chelating radioactive 64Cu nuclei enabled the biodistribution and in vivo positron emission tomography of these materials to be studied and directly correlated to the initial structure.