Adaptive peptide dispersions enable drying-induced biomolecule encapsulation.

Peptides are promising building blocks of designer materials with wide-ranging applications. These materials are stabilized by directional hydrogen-bonding patterns, giving rise to one-dimensional or two-dimensional assembly. It remains a challenge to mimic biology's context-adaptive and flexible structures.

Supramolecular Copolymerization of Glycopeptide Amphiphiles and Amyloid Peptides Improves Neuron Survival.

Neurodegenerative diseases such as Alzheimer's disease and amyotrophic lateral sclerosis are characterized by progressive neuronal loss and the accumulation of misfolded proteins including amyloid proteins. Current therapeutic options include the use of antibodies for these proteins, but novel chemical strategies need to be developed. The disaccharide trehalose has been widely reported to prevent misfolding and aggregation of proteins, and we therefore investigated the conjugation of this moiety to biocompatible peptide amphiphiles (TPAs) known to undergo supramolecular polymerization.

Tuning Supramolecular Chirality in Iodinated Amphiphilic Peptides Through Tripeptide Linker Editing.

Protease-cleavable supramolecular oligopeptide nanofilaments are promising materials for targeted therapeutics and diagnostics. In these systems, single amino acid substitutions can have profound effects on the supramolecular structure and consequent proteolytic degradation, which are critical parameters for their intended applications. Herein, we describe changes to the self-assembly and proteolytic cleavage of iodine containing sequences for future translation into matrix metalloprotease (MMP-9)-activated supramolecular radio-imaging probes.

Sequence-Tunable Phase Behavior and Intrinsic Fluorescence in Dynamically Interacting Peptides.

A conceptual framework towards understanding biological condensed phases is emerging, derived from biological, biomimetic, and synthetic sequences. However, de novo peptide condensate design remains a challenge due to an incomplete understanding of the structural and interactive complexity. We designed peptide modules based on a simple repeat motif composed of tripeptide spacers (GSG, SGS, GLG) interspersed with adhesive amino acids (R/H and Y).

-Acetylation of Biodegradable Supramolecular Peptide Nanofilaments Selectively Enhances Their Proteolytic Stability for Targeted Delivery of Gold-Based Anticancer Agents.

Peptide materials are promising for various biomedical applications; however, a significant concern is their lack of stability and rapid degradation due to non-specific proteolysis. For materials specifically designed to respond to disease-specific proteases, it would be desirable to retain high susceptibility to target proteases while minimizing the impact of non-specific proteolysis. We describe N-terminal acetylation as a simple synthetic modification of amphiphilic self-assembling peptides that contain an MMP-9-cleavable segment and form soluble, nanoscale filaments.

Encapsulation of Gold-Based Anticancer Agents in Protease-Degradable Peptide Nanofilaments Enhances Their Potency.

We investigated the use of amphiphilic, protease-cleavable peptides as encapsulation moieties for hydrophobic metallodrugs, in order to enhance their bioavailability and consequent activity. Two hydrophobic, gold-containing anticancer agents varying in aromatic ligand distribution (Au(I)-N-heterocyclic carbene compounds and ) were investigated. These were encapsulated into amphiphilic decapeptides that form soluble filamentous structures with hydrophobic cores, varying supramolecular packing arrangements and surface charge.

Expanding the Conformational Landscape of Minimalistic Tripeptides by Their -Glycosylation.

We report on the supramolecular self-assembly of tripeptides and their -glycosylated analogues, in which the carbohydrate moiety is coupled to a central serine or threonine flanked by phenylalanine residues. The substitution of serine with threonine introduces differential side-chain interactions, which results in the formation of aggregates with different morphology. -glycosylation decreases the aggregation propensity because of rebalancing of the π interactions.

Transition metal complexes incorporated with photoswitchable azo-based benzimidazole ligands: Photochromic and solvatochromic studies.

Photochromic compounds are well-known for their promising applications in many areas. It attracts remarkable attention because of their potential ability for optical memory media and optical switching devices. Herein, we have synthesized azo-based benzimidazole ligand and their transition metal complexes for photochromic applications in the liquid state.

Unraveling the Effect on Luminescent Properties by Postsynthetic Covalent and Noncovalent Grafting of gfp Chromophore Analogues in Nanoscale MOF-808.

Here, we demonstrate mimicking of photophysical properties of native green fluorescent protein (gfp) by immobilizing the gfp chromophore analogues in nanoscale MOF-808 and further exploring the bioimaging applications. The two virtually nonfluorescent gfp chromophore analogues carrying different functionalities, BDI-AE (COOH/COOMe) and BDI-EE (COOMe/COOMe) were immobilized in nanosized MOF-808 via postsynthetic modification. An H NMR and IR study confirms that BDI-AE was coordinated in NMOF-808, whereas BDI-EE was just noncovalently encapsulated.