Aug 2026· Journal of the American Chemical Society· 0 citations· 54 references
Abstract
Peptide-based materials have enormous potential for applications including therapeutics, sensing, catalysis, and flexible electronics. Recent material discovery screenings through peptide sequence space have identified a class of amphiphilic heme-containing peptides that self-assemble at the nanoscale while efficiently sequestering heme as a prerequisite for electron transfer. However, the assemblies are remarkably sensitive to changes in peptide sequence, even at the single-residue level, impacting heme uptake, aggregate characteristics, and stability. In a combined experimental and molecular simulation study, we examine the interplay between hydrophobicity and charge–charge repulsion on the heme uptake performance and physicochemical characteristics of the assemblies of representative peptides, ExL4–xL5HL6 for x = 2, 3, 4. We find that membrane permeability and compressibility are beneficial for heme uptake, while striking a balance with the overall stability of the assembly. This work highlights the sensitivity of material performance within peptide design space while providing insight into the compromise that must be struck between competing characteristics.
Understanding how molecular interactions evolve into ordered architectures at reactive solid/liquid interfaces remains a major challenge because surface reactivity can profoundly influence adsorption mechanisms. In such systems, multiple interfacial processes, including redox reactions, adsorption/desorption, coordinat...
Hédi Bouloussa, Joanne Lê-Chesnais, L. Valentin et al.· ACS Applied Materials and In...· 0 citations
This review provides a comprehensive overview of the structural and mechanistic principles that underpin the bioengineering of heme proteins for both natural and abiological transformations, concluding that the core of reactivity of such metalloenzymes is the iron-porphyrin cofactor, whose tunable oxidation and spin st...
Epari Sai Santosh Kumar, K. Dubey· FEBS Letters· 0 citations
Efficient and green separation of rare earth elements (REE) remains a critical challenge, with conventional solvent extraction relying heavily on toxic organic solvents. Herein, three biomimetic peptides (NF-H1, NF-H2, and NF-H3) integrating the Nap-FF hydrophobic assembly motif with EF-hand-derived REE-recognition s...
Hai-Li Wang, Xing-Liang Shen, Jing Wang et al.· Langmuir· 0 citations
Palmitoylation is a widely employed strategy for anchoring peptides to lipid membranes, but it can also lead to uncontrolled self-assembly. The lipid moieties can promote clustering into heterodispersed aggregates that distribute unevenly, thereby reducing accessibility and inducing undesired uptake mechanisms that lim...
Juan Toledo-Marcos, Bruno Di Geronimo, Sanja Curcic et al.· Materials Advances· 0 citations
The integration of protein secondary structures with metal ions offers a promising strategy for designing highly ordered self-assembled structures with enhanced stability and functionality. The nature of the amino acids plays a crucial role in dictating the secondary structures of peptides. Here, we report highly stabl...
Sanjit Dey, Souvik Roy, Sandip U. Toraskar et al.· Chemistry - An Asian Journal· 0 citations
It is shown that the single peptide pPorA, derived from porin PorACj, self-assembles into flexible α-helical nanopores, inserts in lipid membranes and exists in distinct small- and large-conductance states, providing a versatile platform for ultrasensitive profiling of disease biomarkers.
