Themed collection Peptide Materials
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Molecular simulations of peptide amphiphiles
This review describes recent progress in the area of molecular simulations of peptide assemblies, including peptide-amphiphiles, and drug-amphiphiles.
Org. Biomol. Chem., 2017,15, 7993-8005
https://doi.org/10.1039/C7OB01290J
Amyloid scaffolds as alternative chlorosomes
Living systems contain remarkable functional capability built within sophisticated self-organizing frameworks.
Org. Biomol. Chem., 2017,15, 7063-7071
https://doi.org/10.1039/C7OB01170A
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Self-assembly of bioactive peptides, peptide conjugates, and peptide mimetic materials
Self-assembling peptide and peptide conjugates have attracted great attention due to their biocompatibility, biodegradability and biofunctionality. This review covers self-assembly of amphiphilic peptides and peptide mimetic materials, as well as their potential applications.
Org. Biomol. Chem., 2017,15, 5867-5876
https://doi.org/10.1039/C7OB01092C
Supramolecular control of heme binding and electronic states in multi-heme peptide assemblies
Three peptides that are compositionally identical but sequentially distinct have been designed to study the impact of morphology and hydrophobicity on heme coordination and function.
Org. Biomol. Chem., 2017,15, 6725-6730
https://doi.org/10.1039/C7OB01081H
Collagen mimetic peptide discs promote assembly of a broad range of natural protein fibers through hydrophobic interactions
Collagen mimetic peptides bind to a variety of fiber-forming proteins through complementary hydrophobic interactions, resulting in discs-on-a-string nanostructures and bundling of fibers.
Org. Biomol. Chem., 2017,15, 5893-5898
https://doi.org/10.1039/C7OB01073G
Enzymatic self-assembly of an immunoreceptor tyrosine-based inhibitory motif (ITIM)
An immunoreceptor tyrosine-based inhibitory motif (ITIM), LYYYYL, as well as its enantiomeric or retro-inverso peptide, self-assembles in water upon enzymatic dephosphorylation, thus illustrating a new approach to design bioinspired soft materials from an important pool of functional peptides.
Org. Biomol. Chem., 2017,15, 5689-5692
https://doi.org/10.1039/C7OB01074E
Display of functional proteins on supramolecular peptide nanofibrils using a split-protein strategy
The display of functional proteins on self-assembled peptide nanofibrils is accomplished by noncovalent attachment using a split-protein strategy.
Org. Biomol. Chem., 2017,15, 5279-5283
https://doi.org/10.1039/C7OB01057E
Design and self-assembly of PBLG-b-ELP hybrid diblock copolymers based on synthetic and elastin-like polypeptides
The synthesis and self-assembly of amphiphilic copolypeptides containing a recombinant elastin-like polypeptide block used as a macroinitiator for the ROP of γ-BLG NCA are presented.
Org. Biomol. Chem., 2017,15, 10095-10104
https://doi.org/10.1039/C7OB01945A
Synthetic approach to tailored physical associations in peptide-polyurea/polyurethane hybrids
Tailored physical interactions were utilized to tune hierarchical organization and mechanical response in peptide-polymer hybrids.
Org. Biomol. Chem., 2017,15, 7607-7617
https://doi.org/10.1039/C7OB01352C
The effect of comb architecture on complex coacervation
Complex coacervation is a widely utilized technique for effecting phase separation, though predictive understanding of molecular-level details remains underdeveloped.
Org. Biomol. Chem., 2017,15, 7630-7642
https://doi.org/10.1039/C7OB01314K
Self-assembly of an amphipathic ααβ-tripeptide into cationic spherical particles for intracellular delivery
Self-assembly of ultra short peptide into proteolytically stable drug carriers.
Org. Biomol. Chem., 2017,15, 6773-6779
https://doi.org/10.1039/C7OB01693J
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Molecular dynamics simulations reveal disruptive self-assembly in dynamic peptide libraries
Coarse grained molecular dynamic simulations demonstrate that interactions between species in dynamic peptide libraries can cause a disrupting self-assembly effect that affects the possible discovery of new materials.
Org. Biomol. Chem., 2017,15, 6541-6547
https://doi.org/10.1039/C7OB01268C
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Stabilizing bubble and droplet interfaces using dipeptide hydrogels
Hydrophobic dipeptide molecules can be used to create interfacial films covering bubbles and droplets made from a range of oils.
Org. Biomol. Chem., 2017,15, 6342-6348
https://doi.org/10.1039/C7OB01053B
Transition from disordered aggregates to ordered lattices: kinetic control of the assembly of a computationally designed peptide
This work is showing the ability to control the kinetics of peptide assembly while leaving both the designed α-helical and tetrameric helical bundle intact.
Org. Biomol. Chem., 2017,15, 6109-6118
https://doi.org/10.1039/C7OB01197K
The effect of L-DOPA hydroxyl groups on the formation of supramolecular hydrogels
Fmoc-L-DOPA-D-Oxd-OH was prepared starting from commercially available L-DOPA. Its gelation ability was tested by comparison with Fmoc-L-Tyr-D-Oxd-OH and Fmoc-L-Phe-D-Oxd-OH using ten different triggers.
Org. Biomol. Chem., 2017,15, 5797-5804
https://doi.org/10.1039/C7OB01026E
Control of the hierarchical assembly of π-conjugated optoelectronic peptides by pH and flow
Coarse-grained molecular simulations reveal the influence of pH and flow on the self-assembly of DFAG-OPV3-GAFD optoelectronic peptides.
Org. Biomol. Chem., 2017,15, 5484-5502
https://doi.org/10.1039/C7OB00923B
Linear and orthogonal peptide templating of silicified protein fibres
Silica-specific motifs templated into fibre-forming peptides effectively silicify protein fibres.
Org. Biomol. Chem., 2017,15, 5380-5385
https://doi.org/10.1039/C7OB01134B
Multi-responsive polypeptide hydrogels derived from N-carboxyanhydride terpolymerizations for delivery of nonsteroidal anti-inflammatory drugs
Multi-responsive polypeptide-based hydrogels exhibited thermo-, mechano-, and enzyme-responsive properties, enabling performance as a delivery system for encapsulation and release of naproxen.
Org. Biomol. Chem., 2017,15, 5145-5154
https://doi.org/10.1039/C7OB00931C
Balancing the intermolecular forces in peptide amphiphiles for controlling self-assembly transitions
Through balancing the relative repulsive and attractive intermolecular forces, self-assembling peptide amphiphiles with different sizes but similar pH- and concentration-dependent self-assembly behaviour are created.
Org. Biomol. Chem., 2017,15, 5220-5226
https://doi.org/10.1039/C7OB00875A
Self-assembled artificial viral capsids bearing coiled-coils at the surface
A β-annulus-coiled-coil-B peptide self-assembled into an artificial viral capsid and then the addition of a complementary coiled-coil-A peptide showed the formation of capsids with coiled-coil spikes on the surface.
Org. Biomol. Chem., 2017,15, 5070-5077
https://doi.org/10.1039/C7OB00998D
The effect of carbohydrate structures on the hydrogelation ability and morphology of self-assembled structures of peptide–carbohydrate conjugates in water
Carbohydrate structures of peptide–carbohydrate conjugates have a noticeable effect on the morphology of self-assembled structures.
Org. Biomol. Chem., 2017,15, 4595-4600
https://doi.org/10.1039/C7OB00816C
About this collection
Proteins are privileged macromolecules that play critical roles in catalysis, extracellular matrix structure, cargo transport, and cell signalling. Over the past two decades, the role of peptides as functional components of materials systems has been elucidated. These systems have found use in a variety of emerging technologies spanning optoelectronics, energy conversion, regenerative medicine and drug delivery.
In this collection, guest edited by Professors John D. Tovar, Honggang Cui and Dave Adams, we focus on some of the latest exciting research where peptides and peptide mimics are treated not as isolated molecules of therapeutic value but as components of larger collective systems.
New articles will be added to this collection as they are published.