23 June 2024
Multiscale peptide self-assembly: Order to disorder

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Multiscale Peptide Self-Assembly: A Fascinating Journey from Order to Disorder

Peptides, the building blocks of proteins, have garnered significant interest in the field of biomolecular self-assembly due to their ability to form intricate structures with diverse functionalities. Recent research led by Prof. Yan Xuehai from the Institute of Process Engineering (IPE) of the Chinese Academy of Sciences has shed light on the progress in peptide self-assembly (PSA) and the multi-scale process mechanisms involved in this fascinating phenomenon. This research not only enhances our understanding of cell functions and disease pathogenesis but also paves the way for the development of innovative ecological material systems with unique properties.

Exploring the Transition: From Ordered to Disordered Structures

Biomolecular self-assembly plays a crucial role in generating distinct biological functions such as molecular recognition and signal transduction through both ordered and disordered supramolecular structures. While ordered structures have been extensively studied, disordered structures present a unique challenge due to their thermodynamic metastable nature, making them elusive and short-lived. The team at IPE has made significant strides in uncovering droplet-like disordered structures and elucidating a novel mechanism for liquid-liquid phase separation (LLPS)-mediated multi-step desolvation in PSA. By delving into the development of solid glass materials with long-range disorder, the researchers have opened up new avenues for designing next-generation peptide materials with enhanced functionalities.

Regulating the Self-Assembly Process: A Key Challenge

The journey from ordered to disordered structures in peptide self-assembly poses a significant challenge in terms of controlling the process to ensure the stability and integrity of the resulting structures. The team at IPE has focused on developing innovative methods to modulate the PSA process, particularly in the context of transiently occurring droplet-like disordered structures. By unraveling the multistep desolvation process mediated by LLPS, the researchers have paved the way for steering the metastable droplets towards the formation of ordered structures with diverse morphologies and functions. Furthermore, the discovery of long-range disordered solid glass structures with superior degradability and processability holds immense promise for the development of novel implantable devices and drug delivery systems.

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Published on: August 27, 2016 Description: The review text: http://pubs.acs.org/doi/full/10.1021/acs.chemrev.6b00163 Movie for download and license information: ...
Coarse-grained and multiscale modeling of proteins [review paper presentation]
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Future Directions: Unraveling the Potential of Disordered Structures

As research on peptide self-assembly progresses from ordered to disordered structures, exciting avenues for exploring the properties and applications of disordered structures emerge. Techniques such as computer simulations, in situ imaging, and tracking methods offer new insights into predicting and characterizing disordered structures, paving the way for their precise regulation and functional applications. The study of amino acids and peptides forming coacervates through LLPS not only provides a window into biomimetic primitive cells but also offers valuable insights into biological evolution and disease pathogenesis. The versatility of disordered glass structures, with their biodegradability, processability, and environmental friendliness, holds great promise for a wide range of biomedical applications, including drug delivery systems and wearable devices.

The research on multiscale peptide self-assembly represents a fascinating journey from ordered to disordered structures, offering profound insights into the intricate processes governing biomolecular self-assembly. By bridging the gap between ordered and disordered structures, researchers are not only unraveling the mysteries of nature but also paving the way for the development of innovative materials with diverse functionalities and applications. The future of peptide self-assembly holds immense potential for revolutionizing fields ranging from biomedicine to materials science, with a focus on harnessing the unique properties of disordered structures for transformative advancements in science and technology.

Links to additional Resources:

1. www.nature.com 2. www.science.org 3. www.pnas.org

Related Wikipedia Articles

Topics: Peptide self-assembly, Biomolecular self-assembly, Liquid-liquid phase separation

Peptide
Peptides are short chains of amino acids linked by peptide bonds. A polypeptide is a longer, continuous, unbranched peptide chain. Polypeptides that have a molecular mass of 10,000 Da or more are called proteins. Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides....
Read more: Peptide

Molecular self-assembly
In chemistry and materials science, molecular self-assembly is the process by which molecules adopt a defined arrangement without guidance or management from an outside source. There are two types of self-assembly: intermolecular and intramolecular. Commonly, the term molecular self-assembly refers to the former, while the latter is more commonly called...
Read more: Molecular self-assembly

Liquid helium
Liquid helium is a physical state of helium at very low temperatures at standard atmospheric pressures. Liquid helium may show superfluidity. At standard pressure, the chemical element helium exists in a liquid form only at the extremely low temperature of −269 °C (−452.20 °F; 4.15 K). Its boiling point and...
Read more: Liquid helium

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