scholarly journals Self-assembly of amino acids toward functional biomaterials

2021 ◽  
Vol 12 ◽  
pp. 1140-1150
Author(s):  
Huan Ren ◽  
Lifang Wu ◽  
Lina Tan ◽  
Yanni Bao ◽  
Yuchen Ma ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Self Assembly ◽  
Functional Materials ◽  
Building Blocks ◽  
The Self ◽  
Self Assembled ◽  
Functional Biomaterials ◽  
Proteins And Peptides

Biomolecules, such as proteins and peptides, can be self-assembled. They are widely distributed, easy to obtain, and biocompatible. However, the self-assembly of proteins and peptides has disadvantages, such as difficulty in obtaining high quantities of materials, high cost, polydispersity, and purification limitations. The difficulties in using proteins and peptides as functional materials make it more complicate to arrange assembled nanostructures at both microscopic and macroscopic scales. Amino acids, as the smallest constituent of proteins and the smallest constituent in the bottom-up approach, are the smallest building blocks that can be self-assembled. The self-assembly of single amino acids has the advantages of low synthesis cost, simple modeling, excellent biocompatibility and biodegradability in vivo. In addition, amino acids can be assembled with other components to meet multiple scientific needs. However, using these simple building blocks to design attractive materials remains a challenge due to the simplicity of the amino acids. Most of the review articles about self-assembly focus on large molecules, such as peptides and proteins. The preparation of complicated materials by self-assembly of amino acids has not yet been evaluated. Therefore, it is of great significance to systematically summarize the literature of amino acid self-assembly. This article reviews the recent advances in amino acid self-assembly regarding amino acid self-assembly, functional amino acid self-assembly, amino acid coordination self-assembly, and amino acid regulatory functional molecule self-assembly.

Fmoc-modified amino acids and short peptides: simple bio-inspired building blocks for the fabrication of functional materials

2016 ◽  
Vol 45 (14) ◽  
pp. 3935-3953 ◽  
Author(s):  
Kai Tao ◽  
Aviad Levin ◽  
Lihi Adler-Abramovich ◽  
Ehud Gazit
Keyword(s):  
Amino Acids ◽  
Self Assembly ◽  
Functional Materials ◽  
Building Blocks ◽  
The Self ◽  
Short Peptides

In this review, the studies on the self-assembly of Fmoc-modified biomolecules and their relevant applications in diverse advanced fields are summarized.

Understanding the self-ordering of amino acids into supramolecular architects: Co-assembly based modulation of phenylalanine nanofibrils

2021 ◽  
Author(s):  
Prabhjot Singh ◽  
Satish Kumar Pandey ◽  
Aarzoo Grover ◽  
Rohit K. Sharma ◽  
Nishima Wangoo
Keyword(s):  
Amino Acids ◽  
Thermodynamic Stability ◽  
Self Assembly ◽  
Functional Materials ◽  
The Self ◽  
Self Assembled ◽  
Bio Compatibility

Amino acids have emerged as promising molecular frameworks for the generation of functional materials owing to the bio-compatibility and thermodynamic stability of their self-assembled architects. The homogeneous and heterogeneous self-assembly...

scholarly journals Self-Assembly of Shape-Tunable Oblate Colloidal Particles into Orientationally Ordered Crystals, Glassy Crystals and Plastic Crystals

Soft Matter ◽  
2021 ◽  
Author(s):  
Jiawei Lu ◽  
Xiangyu Bu ◽  
Xinghua Zhang ◽  
Bing Liu
Keyword(s):  
Crystal Structures ◽  
Self Assembly ◽  
Colloidal Particles ◽  
Building Blocks ◽  
Fundamental Question ◽  
The Self ◽  
Plastic Crystals ◽  
Self Assembled ◽  
Glassy Crystals ◽  
The Relationship

The shapes of colloidal particles are crucial to the self-assembled superstructures. Understanding the relationship between the shapes of building blocks and the resulting crystal structures is an important fundamental question....

A Dynamic Route to Structure and Function: Recent Advances in Imine-Based Organic Nanostructured Materials

2013 ◽  
Vol 66 (1) ◽  
pp. 9 ◽  
Author(s):  
Yi Liu ◽  
Zhan-Ting Li
Keyword(s):  
Self Assembly ◽  
Reaction System ◽  
Functional Materials ◽  
Building Blocks ◽  
The Self ◽  
Interlocked Molecules ◽  
Functional Aspects ◽  
Imine Bond ◽  
And Function ◽  
Dynamic Route

The chemistry of imine bond formation from simple aldehyde and amine precursors is among the most powerful dynamic covalent chemistries employed for the construction of discrete molecular objects and extended molecular frameworks. The reversible nature of the C=N bond confers error-checking and proof-reading capabilities in the self-assembly process within a multi-component reaction system. This review highlights recent progress in the self-assembly of complex organic molecular architectures that are enabled by dynamic imine chemistry, including molecular containers with defined geometry and size, mechanically interlocked molecules, and extended frameworks and polymers, from building blocks with preprogrammed steric and electronic information. The functional aspects associated with the nanometer-scale features not only place these dynamically constructed nanostructures at the frontier of materials sciences, but also bring unprecedented opportunities for the discovery of new functional materials.

scholarly journals Modification of a Single Atom Affects the Physical Properties of Double Fluorinated Fmoc-Phe Derivatives

2021 ◽  
Vol 22 (17) ◽  
pp. 9634
Author(s):  
Moran Aviv ◽  
Dana Cohen-Gerassi ◽  
Asuka A. Orr ◽  
Rajkumar Misra ◽  
Zohar A. Arnon ◽  
...  
Keyword(s):  
Amino Acid ◽  
Physical Properties ◽  
Self Assembly ◽  
Deep Understanding ◽  
Building Blocks ◽  
The Self ◽  
Single Atom ◽  
Supramolecular Organization ◽  
Assembly Process ◽  
Wide Range

Supramolecular hydrogels formed by the self-assembly of amino-acid based gelators are receiving increasing attention from the fields of biomedicine and material science. Self-assembled systems exhibit well-ordered functional architectures and unique physicochemical properties. However, the control over the kinetics and mechanical properties of the end-products remains puzzling. A minimal alteration of the chemical environment could cause a significant impact. In this context, we report the effects of modifying the position of a single atom on the properties and kinetics of the self-assembly process. A combination of experimental and computational methods, used to investigate double-fluorinated Fmoc-Phe derivatives, Fmoc-3,4F-Phe and Fmoc-3,5F-Phe, reveals the unique effects of modifying the position of a single fluorine on the self-assembly process, and the physical properties of the product. The presence of significant physical and morphological differences between the two derivatives was verified by molecular-dynamics simulations. Analysis of the spontaneous phase-transition of both building blocks, as well as crystal X-ray diffraction to determine the molecular structure of Fmoc-3,4F-Phe, are in good agreement with known changes in the Phe fluorination pattern and highlight the effect of a single atom position on the self-assembly process. These findings prove that fluorination is an effective strategy to influence supramolecular organization on the nanoscale. Moreover, we believe that a deep understanding of the self-assembly process may provide fundamental insights that will facilitate the development of optimal amino-acid-based low-molecular-weight hydrogelators for a wide range of applications.

scholarly journals Unusual Aggregation Properties of Single Amino Acid L-Lysine Hydrochloride

2021 ◽  
Author(s):  
Bharti Koshti ◽  
Ramesh Singh ◽  
Vivekshinh Kshtriya ◽  
Shanka Walia ◽  
Dhiraj Bhatia ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Self Assembly ◽  
Short Term Memory ◽  
Deionized Water ◽  
The Body ◽  
The Self ◽  
Single Amino Acid ◽  
Maple Syrup ◽  
Self Assembling

<p>.<br></p><p>The self-assembly of single amino acids is very important topic of research since there are plethora of diseases like phenylketonuria, tyrosinemia, hypertryptophanemia, hyperglycinemia, cystinuria and maple syrup urine disease to name a few which are caused by the accumulation or excess of amino acids. These are in-born errors of metabolisms (IEM’s) which are caused due to the deficiency of enzymes involved in catabolic pathways of these enzymes. Hence, it is very pertinent to understand the fate of these excess amino acids in the body and their self-assembling behaviour at molecular level. From the previous literature reports it may be surmised that the single amino acids like Phenylalanine, Tyrosine, Tryptophan, Cysteine and Methionine assemble to amyloid like structures, and hence have important implications in the pathophysiology of IEM’s like phenylketonuria, tyrosinemia, hypertryptophanemia, cystinuria and hypermethioninemia respectively. In this manuscript we report the self-assembly of lysine hydrocholride to fiber like structures in deionized water. It could be observed that lysine assemble to globular structures in fresh condition and then gradually changes to fiber like morphologies by self-association over time after 24 hours. These fibers gradually change to tubular morphologies after 3 day followed by fractal irregular morphologies in 10 and 15 days respectively. Notably, lysine exists as positively charged amino acid at physiological pH and the amine groups in lysine remain protonated. Hence, the self-assembling properties of lysine hydrochloride in deionized water is also pertinent and give insights into the fate of this amino acid in body in case it remains unmetabolized. Further, MTT assays were done to analyse the toxicities of these aggregates and the assay suggest their cytotoxic nature on SHSY5Y neural cell lines. Hence, the aggregation of lysine may be attributed to the pathological symptoms caused in diseases like hyperlysinemia which is associated with the neurological problems like seizures and short-term memory as observed in case of amyloid diseases like Parkinson’s and Alzheimer’s to name a few.</p>

scholarly journals Diverse protein assembly driven by metal and chelating amino acids with selectivity and tunability

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Minwoo Yang ◽  
Woon Ju Song
Keyword(s):  
Amino Acids ◽  
Self Assembly ◽  
Protein Structures ◽  
Functional Materials ◽  
Building Blocks ◽  
Unnatural Amino Acid ◽  
Metal Coordination ◽  
Specific Chemical ◽  
Natural Building ◽  
Kinetics Of

AbstractProteins are versatile natural building blocks with highly complex and multifunctional architectures, and self-assembled protein structures have been created by the introduction of covalent, noncovalent, or metal-coordination bonding. Here, we report the robust, selective, and reversible metal coordination properties of unnatural chelating amino acids as the sufficient and dominant driving force for diverse protein self-assembly. Bipyridine-alanine is genetically incorporated into a D3 homohexamer. Depending on the position of the unnatural amino acid, 1-directional, crystalline and noncrystalline 2-directional, combinatory, and hierarchical architectures are effectively created upon the addition of metal ions. The length and shape of the structures is tunable by altering conditions related to thermodynamics and kinetics of metal-coordination and subsequent reactions. The crystalline 1-directional and 2-directional biomaterials retain their native enzymatic activities with increased thermal stability, suggesting that introducing chelating ligands provides a specific chemical basis to synthesize diverse protein-based functional materials while retaining their native structures and functions.

Amino Acid Functional Polymers: Biomimetic Polymer Design Enabling Catalysis, Chiral Materials, and Drug Delivery

2016 ◽  
Vol 69 (7) ◽  
pp. 705 ◽  
Author(s):  
Emma R. L. Brisson ◽  
Zeyun Xiao ◽  
Luke A. Connal
Keyword(s):  
Drug Delivery ◽  
Amino Acids ◽  
Amino Acid ◽  
Self Assembly ◽  
Building Blocks ◽  
Functional Polymers ◽  
Responsive Materials ◽  
Biomimetic Polymer ◽  
Tunable Optical Properties ◽  
Natural Building

Amino acids are the natural building blocks for the world around us. Highly functional, these small molecules have unique catalytic properties, chirality, and biocompatibility. Imparting these properties to surfaces and other macromolecules is highly sought after and represents a fast-growing field. Polymers functionalized with amino acids in the side chains have tunable optical properties, pH responsiveness, biocompatibility, structure and self-assembly properties. Herein, we review the synthesis of amino acid functional polymers, discuss manipulation of available strategies to achieve the desired responsive materials, and summarize some exciting applications in catalysis, chiral particles, and drug delivery.

Co-assembly of helical β3-peptides: a self-assembled analogue of a statistical copolymer

2017 ◽  
Vol 89 (12) ◽  
pp. 1809-1816 ◽  
Author(s):  
Claire Buchanan ◽  
Christopher J. Garvey ◽  
Patrick Perlmutter ◽  
Adam Mechler
Keyword(s):  
Amino Acids ◽  
Physical Properties ◽  
Self Assembly ◽  
Unnatural Amino Acids ◽  
The Self ◽  
Microscopy Imaging ◽  
Wide Range ◽  
Self Assembled ◽  
Unnatural Peptides ◽  
Natural Amino Acids

AbstractUnnatural peptide self-assembly offers the means to design hierarchical nanostructures of controlled geometries, chemical function and physical properties. N-acyl β3 peptides, where all residues are unnatural amino acids, are able to form helical fibrous structures by a head-to-tail assembly of helical monomers, extending the helix via a three point supramolecular hydrogen bonding motif. These helical nanorods were shown to be stable under a wide range of physical conditions, offering a self-assembled analogue of polymeric fibres. Hitherto the self-assembly has only been demonstrated between identical monomers; however the self-assembly motif is sequence-independent, offering the possibility of hetero-assembly of different peptide monomers. Here we present a proof of principle study of head-to-tail co-assembly of two different helical unnatural peptides Ac-β3[WELWEL] and Ac-β3[LIA], where the letters denote the β3 analogues of natural amino acids. By atomic force microscopy imaging it was demonstrated that the homo-assembly and co-assembly of these peptides yield characteristically different structures. Synchrotron small angle X-ray scattering experiments have confirmed the presence of the fibres in the solution and the averaged diameters from modelled data correlate well to the results of AFM imaging. Hence, there is evidence of co-assembly of the fibrous superstructures; given that different monomers may be used to introduce variations into chemical and physical properties, the results demonstrate a self-assembled analogue of a statistical co-polymer that can be used in designing complex functional nanomaterials.

scholarly journals Unveiling the Key Templates in the Self-Assembly of Gigantic Molybdenum Blue Wheels

2018 ◽  
Author(s):  
Weimin Xuan ◽  
Robert Pow ◽  
Qi Zheng, ◽  
Nancy Watfa ◽  
De-Liang Long ◽  
...  
Keyword(s):  
Self Assembly ◽  
Electrostatic Interactions ◽  
Structural Evolution ◽  
Functional Materials ◽  
Building Blocks ◽  
Underlying Mechanism ◽  
The Self ◽  
Supramolecular Systems ◽  
Structure Directing Agent ◽  
Molybdenum Blue

Template synthesis is a powerful and useful approach to build a variety of functional materials and complicated supramolecular systems. Systematic study on how templates structurally evolve from basic building blocks and then affect the templated self-assembly is critical to understand the underlying mechanism and gain more guidance for designed assembly but remains challenging. Here we describe the templated self-assembly of a series of gigantic Mo Blue (MB) clusters 1-4 using L-ornithine as structure-directing agent. L-ornithine is essential for the formation of such kind of template⊂host assemblies by providing directional forces of hydrogen bonding and electrostatic interactions. Based on the structural relationship between encapsulated templates of {Mo8} (1), {Mo17} (2) and {Mo36} (4), a plausible pathway of the structural evolution of templates is proposed, thus giving more insight on the templated self-assembly of Mo Blue clusters.

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