Learning the rules ofpeptide self assemblythrough data mining with large language models Peptide self-assembly is a fundamental process where short chains of amino acids spontaneously organize into ordered nanostructures.作者：P Janković·2021·被引用次数：31—Peptide self-assemblyis a versatile tool that allows mimicking viruses by creating their simplified versions through the design of functional, ... This phenomenon, driven by a complex interplay of noncovalent interactions like hydrogen bonding, hydrophobic forces, electrostatic interactions, and π-π stacking, is crucial for understanding biological systems and engineering novel functional materials.作者：PWJM Frederix·2015·被引用次数：839—Peptides that self-assemble into nanostructuresare of tremendous interest for biological, medical, photonic and nanotechnological ... The ability of peptides to self-assemble into diverse architectures, ranging from simple fibers and micelles to intricate hydrogels and vesicles, makes them highly versatile building blocks for advanced applications. Understanding how peptides self-assemble is key to harnessing their potential in fields such as biomedicine, nanotechnology, and materials science.作者：NJ Sinha·2021·被引用次数：271—In this review, we shall focus on theself-assembly of peptides that consist of tens of amino acids. We highlight both natural and non-natural ...
The spontaneous organization of peptides into ordered structures is governed by a delicate balance of thermodynamic and kinetic factorsPeptide Design and Self-assembly into Targeted .... These forces dictate the specific conformation and arrangement of individual peptide molecules, ultimately determining the macroscopic properties of the resulting assembliesSelf-assembling peptide.
* Hydrogen Bonding: This ubiquitous interaction, primarily occurring along the peptide backbone, plays a significant role in stabilizing secondary structures like β-sheets, which are common motifs in self-assembled peptides.作者：N Cao·2024·被引用次数：43—Peptidestend to exhibit a higher propensity forself-assemblywhen hydrophilic and hydrophobic amino acids are arranged alternately. An investigation into the ...
* Hydrophobic Interactions: The tendency of nonpolar amino acid side chains to avoid contact with water drives the aggregation of peptides, leading to the formation of ordered structures where hydrophobic residues are sequestered from the aqueous environment.
* Electrostatic Interactions: Charged amino acid residues can engage in attractive or repulsive forces, influencing peptide association and the overall architecture of the assembled structures.作者：X Yang·2024·被引用次数：15—Theassemblyofpeptidesis mainly controlled by forces such as hydrogen bonding, hydrophobic interaction, electrostatic interaction, and π-π ... Salt bridges, a form of electrostatic interaction, are particularly important in this regard.
* π-π Stacking: Aromatic amino acid residues, such as phenylalanine, tyrosine, and tryptophan, can interact through π-π stacking, contributing to the stability and organization of peptide assemblies, especially in structures like amyloid fibrils.Exploring the sequence space for (tri-)peptide self ...
The versatility of peptide self-assembly allows for the creation of a wide array of nanostructures with tailored properties. These engineered materials are finding applications across various scientific and technological domainsSelf-Assembling Peptides: From Design to Biomedical ....
* Hydrogels: Self-assembled peptide hydrogels form three-dimensional networks capable of encapsulating water, making them highly promising for drug delivery, tissue engineering, and regenerative medicine.Peptide Self‐Assembly and Engineering Their biocompatibility and tunable mechanical properties are key advantagesSelf-assembling peptidesrefer to peptide materials that can form assemblies under certain conditions through intermolecular forces such as π-π stacking and ....
* Micelles and Vesicles: These spherical or vesicular structures formed by peptide self-assembly can serve as nanoscale carriers for hydrophobic drugs or therapeutic agents, enabling targeted delivery and improved bioavailabilityExploring the sequence space for (tri-)peptide self ....
* Fibers and Nanofibers: Ordered assemblies into fibrous structures, often resembling natural protein assemblies, are explored for biomimetic applications, including scaffolding for cell growth and as components in biosensors.Self-assembling peptide
* Biomimetic Materials: Peptide self-assembly provides a powerful strategy to mimic natural biological structures and functions.Peptide Self-assembly: From Ordered to Disordered This includes the creation of artificial viruses, mimicking protein folding, and developing materials with enhanced biocompatibility.
The rational design of peptide sequences is paramount to controlling the self-assembly process and achieving desired nanostructures and functions. Researchers are employing various strategies, including computational modeling and high-throughput screening, to predict and engineer peptides with specific self-assembly behaviors.
* Sequence Design: Alternating hydrophilic and hydrophobic amino acids, for instance, can promote specific assembly pathways. Modulating the length and composition of peptides, including the use of non-natural amino acids, offers further control over self-assembly.
* Stimuli-Responsive Assemblies: Peptide self-assembly can be triggered or modulated by external stimuli such as changes in pH, ionic strength, temperature, or the presence of specific molecules.Peptide-based nanomaterials: Self-assembly, properties ... This allows for dynamic control over material properties and the development of responsive systems.
* Liquid-Liquid Phase Separation (LLPS): Recent research highlights the role of LLPS in peptide self-assembly, where peptides can undergo phase separation to form condensed droplets that can further evolve into ordered aggregates.作者：J Wang·2016·被引用次数：1068—In this review, we focus on the influence of thermodynamic and kinetic factors on structuralassemblyand regulation based on different types of peptide ... Understanding the thermodynamic and kinetic mechanisms governing LLPS is crucial for designing complex peptide-based materials.
Despite significant advancements, challenges remain in precisely controlling peptide self-assembly and translating laboratory findings into practical applications作者：X Hu·2020·被引用次数：152—Over the past few decades, extensive studies have been devoted to understandingpeptide self-assembly, with a focus on the rational design of peptides composed .... Predicting the precise outcome of self-assembly for a given peptide sequence remains complex, and scaling up the production of peptide-based nanomaterials efficiently is an ongoing area of research.
Future directions include developing more sophisticated computational tools for peptide design, exploring novel peptide sequences for advanced functionalities, and further integrating self-assembled peptides into biomedical devices, diagnostics, and therapeutic strategies.作者：N Cao·2024·被引用次数：43—Peptidestend to exhibit a higher propensity forself-assemblywhen hydrophilic and hydrophobic amino acids are arranged alternately. An investigation into the ... The ability to precisely tune noncovalent interactions will continue to be essential for engineering sophisticated peptide self-assembled structures with unique properties and unprecedented applications.
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