Catalytic Assembly of Peptides Mediated by Complex Coacervates DOI
Liping Wang, Yang Zhou,

Tianyi Tong

et al.

ACS Nano, Journal Year: 2025, Volume and Issue: unknown

Published: Jan. 9, 2025

The assembly of peptides is generally mediated by liquid–liquid phase separation, which enables control over kinetics, final structure, and functions peptide-based supramolecular materials. Modulating separation can alter the kinetics changing solvents or introducing external fields. Herein, we demonstrate that be effectively catalyzed complex coacervates. negatively charged sodium alginate (SA) form coacervates with positively KLVFFAE (Aβ16–22, abbreviated as KE) peptide, thereby lowering nucleation barrier promoting peptide. As binding affinity SA-KE dosage SA decrease, system shifts from a relatively inefficient template-induced to highly efficient catalytic before ultimately reverting slow spontaneous assembly. Therefore, both well stoichiometry do not follow intuitive rule "more better", but rather there exists an optimal value maximizes rate

Language: Английский

Self-assembled amphiphilic peptide hydrogels for antimicrobial application DOI
Haifeng Sun, Xiao Fu,

Chaojuan Yang

et al.

Current Opinion in Colloid & Interface Science, Journal Year: 2024, Volume and Issue: 73, P. 101828 - 101828

Published: July 4, 2024

Language: Английский

Citations

6

Peptide-Based Biomimetic Condensates via Liquid–Liquid Phase Separation as Biomedical Delivery Vehicles DOI
Siyu Song, Tsvetomir Ivanov, Dandan Yuan

et al.

Biomacromolecules, Journal Year: 2024, Volume and Issue: 25(9), P. 5468 - 5488

Published: Aug. 23, 2024

Biomolecular condensates are dynamic liquid droplets through intracellular liquid-liquid phase separation that function as membraneless organelles, which highly involved in various complex cellular processes and functions. Artificial analogs formed via similar pathways can be integrated with biological complexity advanced functions have received tremendous research interest the field of synthetic biology. The coacervate droplet-based compartments partition concentrate a wide range solutes, regarded attractive candidates for mimicking phase-separation behaviors biophysical features biomolecular condensates. use peptide-based materials phase-separating components has advantages such diversity amino acid residues customized sequence design, allows programming their physicochemical properties resulting compartments. In this Perspective, we highlight recent advancements design construction biomimicry from peptides relevant to protein, specific reference molecular self-assembly separation, biorelated applications, envisage emerging biomedical delivery vehicles.

Language: Английский

Citations

6

Tunable Chirality of Self‐Assembled Dipeptides Mediated by Bipyridine Derivative DOI
Aoli Wu, Yongxian Guo, Meiqi Li

et al.

Angewandte Chemie International Edition, Journal Year: 2023, Volume and Issue: 62(52)

Published: Nov. 8, 2023

Supramolecular peptide assemblies have been widely used for the development of biomedical, catalytical, and optical materials with chiral nanostructures in view intrinsic chirality peptides. However, assembly pathway transformation behavior various peptides remain largely elusive especially transient under out-of-equilibrium conditions. Herein, N-fluorenylmethoxycarbonyl-protected phenylalanine-tyrosine dipeptide (Fmoc-FY) was as a platform, which showed that proceeds multistep evolution. The original spheres caused by liquid-liquid phase separation (LLPS) can nucleate elongate into formation right-handed helices were metastable easily converted microribbons. Interestingly, bipyridine derivative be introduced to effectively control induce thermodynamically stable or left-handed at different stoichiometric ratios. In addition, also regulated ultrasound enzyme catalysis. This minimalistic system not only broadens nucleation-elongation mechanisms protein aggregates but promotes controllable design biomaterials.

Language: Английский

Citations

15

Harnessing Competitive Interactions to Regulate Supramolecular “Micelle-Droplet-Fiber” Transition and Reversibility in Water DOI Creative Commons
Heleen Duijs, Mohit Kumar, Shikha Dhiman

et al.

Journal of the American Chemical Society, Journal Year: 2024, Volume and Issue: 146(43), P. 29759 - 29766

Published: Oct. 15, 2024

The supramolecular assembly of proteins into irreversible fibrils is often associated with diseases in which aberrant phase transitions occur. Due to the complexity biological systems and their surrounding environments, mechanism underlying separation-mediated poorly understood, making reversal so-called fibrillization a significant challenge. Therefore, it crucial develop simple model that provide insights mechanistic process monomers phase-separated droplets ordered assemblies. Such models can help investigating strategies either reverse or modulate these states. Herein, we present synthetic system composed three components, including benzene-1,3,5-tricarboxamide-based monomer, surfactant, water, mimic condensate pathway observed systems. This highly dynamic undergo "micelle-droplet-fiber" transition over time space concentration gradient field, regulated by competitive interactions. Importantly, manipulating interactions through guest molecules, temperature changes, cosolvents fibers disordered liquid micellar state. Our provides new critical balance between various among components determine reversibility process. Extending this "competitive interaction" approach from complex macromolecules, e.g., proteins, could open avenues for biomedical applications, such as condensate-modifying therapeutics.

Language: Английский

Citations

4

Catalytic Assembly of Peptides Mediated by Complex Coacervates DOI
Liping Wang, Yang Zhou,

Tianyi Tong

et al.

ACS Nano, Journal Year: 2025, Volume and Issue: unknown

Published: Jan. 9, 2025

The assembly of peptides is generally mediated by liquid–liquid phase separation, which enables control over kinetics, final structure, and functions peptide-based supramolecular materials. Modulating separation can alter the kinetics changing solvents or introducing external fields. Herein, we demonstrate that be effectively catalyzed complex coacervates. negatively charged sodium alginate (SA) form coacervates with positively KLVFFAE (Aβ16–22, abbreviated as KE) peptide, thereby lowering nucleation barrier promoting peptide. As binding affinity SA-KE dosage SA decrease, system shifts from a relatively inefficient template-induced to highly efficient catalytic before ultimately reverting slow spontaneous assembly. Therefore, both well stoichiometry do not follow intuitive rule "more better", but rather there exists an optimal value maximizes rate

Language: Английский

Citations

0