Abstract:ABSTRACT:Although biopolymers and synthetic polymers share many common features, each of these two classes of materials is also characterized by a distinct and very specific set of advantages and disadvantages. Combining biopolymer elements with synthetic polymers into a single macromolecular conjugate is an interesting strategy for synergetically merging the properties of the individual components and overcoming some of their limitations. This article focuses on a special class of biological-synthetic hybrids… Show more
“…[129] The formation of nanostructures, including nanofibrils, from block copolymers containing peptide sequences has been the focus of much recent activity, as summarized in several reviews. [82,130,131] Fibrils result from intermolecular hydrogen bonding of the polymers into b-sheet structures. The conjugation of b-sheet peptides to PEG confers enhanced solubility and is of interest in peptide therapeutics, because PEG can provide steric stabilization of a peptide drug.…”
Section: Fibrillization Of Peptides and Proteinsmentioning
With one or two exceptions, biological materials are "soft", meaning that they combine viscous and elastic elements. This mechanical behavior results from self-assembled supramolecular structures that are stabilized by noncovalent interactions. It is an ongoing and profound challenge to understand the self-organization of biological materials. In many cases, concepts can be imported from soft-matter physics and chemistry, which have traditionally focused on materials such as colloids, polymers, surfactants, and liquid crystals. Using these ideas, it is possible to gain a new perspective on phenomena as diverse as DNA condensation, protein and peptide fibrillization, lipid partitioning in rafts, vesicle fusion and budding, and others, as discussed in this selective review of recent highlights from the literature.
“…[129] The formation of nanostructures, including nanofibrils, from block copolymers containing peptide sequences has been the focus of much recent activity, as summarized in several reviews. [82,130,131] Fibrils result from intermolecular hydrogen bonding of the polymers into b-sheet structures. The conjugation of b-sheet peptides to PEG confers enhanced solubility and is of interest in peptide therapeutics, because PEG can provide steric stabilization of a peptide drug.…”
Section: Fibrillization Of Peptides and Proteinsmentioning
With one or two exceptions, biological materials are "soft", meaning that they combine viscous and elastic elements. This mechanical behavior results from self-assembled supramolecular structures that are stabilized by noncovalent interactions. It is an ongoing and profound challenge to understand the self-organization of biological materials. In many cases, concepts can be imported from soft-matter physics and chemistry, which have traditionally focused on materials such as colloids, polymers, surfactants, and liquid crystals. Using these ideas, it is possible to gain a new perspective on phenomena as diverse as DNA condensation, protein and peptide fibrillization, lipid partitioning in rafts, vesicle fusion and budding, and others, as discussed in this selective review of recent highlights from the literature.
“…24,26 Individual fibrillar nanostructures are characterized by cylindrical nanofibers that exhibit β-sheet elements on the surface with a hydrophobic core. 2,11 Early design principles of PA molecules have primarily emphasized structural modifications to improve biocompatibility or to minimize immunogenic properties; 11,27 however, with the aims to use PA self-assembled nanostructures as a synthetic hydrogel scaffold that mimics extracellular matrix, consideration is also placed on the relationship between structural characteristics and mechanical behavior. For example, modifying the mechanical rigidity of hydrogels serving as extracellular matrix results in different cell adhesion and cell differentiation behaviors.…”
Three-dimensional networks of nanofibers, which are formed through self-assembly of peptide amphiphiles, serve as a biomimetic hydrogel scaffold for tissue engineering. With an emphasis to improve hydrogel properties for cell-specific behavior, a better understanding between structural characteristics and physical properties of the macroscopic gel is sought. Large-scale molecular dynamics simulations were performed on two PA sequences with identical composition (palmitoyl-V 3 A 3 E 3 and palmitoyl-A 3 V 3 E 3 ) showing different self-assembly kinetic mechanisms. While both sequences yielded cylindrical nanofibers, these structures have contrasting internal arrangement with respect to the hydrophobic core; the former is continuous with predominately alkyl tails, whereas the latter is disjointed with interconnecting micelles. Two additional sequences (palmitoyl-V 6 E 3 and palmitoyl-A 6 E 3 ) were examined to determine the effects of a homogeneous β-sheet forming segment that is either strongly or mildly hydrophobic on self-assembly. Results from this study indicate that internal structural arrangement of nanofibers can provide a correlation with structural stability and mechanical behavior of hydrogel nanostructures.
“…[1][2][3][4][5][6] The self-assembly of the peptide can be influenced by the synthetic polymer, resulting in distinct tertiary structures. From another viewpoint, peptide functionalities can be attached to synthetic polymers conferring novel ligands that can self-assemble or interact with biomaterials in a targeted fashion.…”
Ordered nanostructures are observed in the melt and solid state for a series of three peptide/PEG conjugates containing fragments of amyloid β‐peptides. These are conjugated to PEG with $\overline M _{\rm n}$ = 3 300 g · mol−1 and a melting temperature Tm = 45–50 °C. The morphology at room temperature is examined by AFM and POM. This shows spherulite formation for the weakly fibrillizing KLVFF‐PEG sample but fibril formation for FFKLVFF‐PEG. The fibrillization tendency of the latter is enhanced by multiple phenylalanine residues. Simultaneous SAXS and WAXS was used to investigate the morphology as a function of temperature. The secondary structure is probed by FTIR.magnified image
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