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.

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.

scholarly journals Self-Assembling Drug Formulations with Tunable Permeability and Biodegradability

Molecules ◽  
2021 ◽  
Vol 26 (22) ◽  
pp. 6786
Author(s):  
Gulnara Gaynanova ◽  
Leysan Vasileva ◽  
Ruslan Kashapov ◽  
Darya Kuznetsova ◽  
Rushana Kushnazarova ◽  
...  
Keyword(s):  
Drug Delivery ◽  
Self Assembly ◽  
Targeted Delivery ◽  
Building Blocks ◽  
Biological Barriers ◽  
Self Assembling ◽  
Low Toxicity ◽  
Natural Building ◽  
Dynamic Structures ◽  
Supramolecular Aggregates

This review focuses on key topics in the field of drug delivery related to the design of nanocarriers answering the biomedicine criteria, including biocompatibility, biodegradability, low toxicity, and the ability to overcome biological barriers. For these reasons, much attention is paid to the amphiphile-based carriers composed of natural building blocks, lipids, and their structural analogues and synthetic surfactants that are capable of self-assembly with the formation of a variety of supramolecular aggregates. The latter are dynamic structures that can be used as nanocontainers for hydrophobic drugs to increase their solubility and bioavailability. In this section, biodegradable cationic surfactants bearing cleavable fragments are discussed, with ester- and carbamate-containing analogs, as well as amino acid derivatives received special attention. Drug delivery through the biological barriers is a challenging task, which is highlighted by the example of transdermal method of drug administration. In this paper, nonionic surfactants are primarily discussed, including their application for the fabrication of nanocarriers, their surfactant-skin interactions, the mechanisms of modulating their permeability, and the factors controlling drug encapsulation, release, and targeted delivery. Different types of nanocarriers are covered, including niosomes, transfersomes, invasomes and chitosomes, with their morphological specificity, beneficial characteristics and limitations discussed.

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.

Single Amino Acid Based Self-Assemblies of Cysteine and Methionine

2018 ◽  
Author(s):  
Nidhi Gour ◽  
Bharti Koshti ◽  
Chandra Kanth P. ◽  
Dhruvi Shah ◽  
Vivek Shinh Kshatriya ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Self Assembly ◽  
Aromatic Amino Acids ◽  
Neutral Condition ◽  
Single Amino Acid ◽  
Binding Assays ◽  
Human Neuroblastoma ◽  
Cytotoxicity Assays ◽  
First Time

We report for the very first time self-assembly of Cysteine and Methionine to discrenible strucutres under neutral condition. To get insights into the structure formation, thioflavin T and Congo red binding assays were done which revealed that aggregates may not have amyloid like characteristics. The nature of interactions which lead to such self-assemblies was purported by coincubating assemblies in urea and mercaptoethanol. Further interaction of aggregates with short amyloidogenic dipeptide diphenylalanine (FF) was assessed. While cysteine aggregates completely disrupted FF fibres, methionine albeit triggered fibrillation. The cytotoxicity assays of cysteine and methionine structures were performed on Human Neuroblastoma IMR-32 cells which suggested that aggregates are not cytotoxic in nature and thus, may not have amyloid like etiology. The results presented in the manuscript are striking, since to the best of our knowledge,this is the first report which demonstrates that even non-aromatic amino acids (cysteine and methionine) can undergo spontaneous self-assembly to form ordered aggregates.

Self-assembly of cyclic homo- and hetero-β-peptides with cis- furanoid sugar amino acid and β-hGly as building blocks

2006 ◽  
pp. 4847-4849 ◽  
Author(s):  
Bulusu Jagannadh ◽  
Marepally Srinivasa Reddy ◽  
Chennamaneni Lohitha Rao ◽  
Anabathula Prabhakar ◽  
Bharatam Jagadeesh ◽  
...  
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Building Blocks

scholarly journals Redox-sensitive reversible self-assembly of amino acid–naphthalene diimide conjugates

2017 ◽  
Vol 7 (6) ◽  
pp. 20160099 ◽  
Author(s):  
Wathsala Liyanage ◽  
Paul W. Rubeo ◽  
Bradley L. Nilsson
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Functional Materials ◽  
Supramolecular Materials ◽  
Responsive Materials ◽  
Naphthalene Diimide ◽  
Reducing Conditions ◽  
Aqueous Solvent ◽  
Stimulus Responsive ◽  
Fibril Aggregates

Peptide and low molecular weight amino acid-based materials that self-assemble in response to environmental triggers are highly desirable candidates in forming functional materials with tunable biophysical properties. In this paper, we explore redox-sensitive self-assembly of cationic phenylalanine derivatives conjugated to naphthalene diimide (NDI). Self-assembly of the cationic Phe-NDI conjugates into nanofibrils was induced in aqueous solvent at high ionic strength. Under reducing conditions, these self-assembled Phe-NDI conjugate fibrils underwent a morphological change to non-fibril aggregates. Upon reoxidation, the initially observed fibrils were reformed. The study herein provides an interesting strategy to effect reversible switching of the structure of supramolecular materials that can be applied to the development of sophisticated stimulus-responsive 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 Synthesis and characterization of poly(amino acid methacrylate)-stabilized diblock copolymer nano-objects

2015 ◽  
Vol 6 (10) ◽  
pp. 1805-1816 ◽  
Author(s):  
Vincent Ladmiral ◽  
Alexandre Charlot ◽  
Mona Semsarilar ◽  
Steven. P. Armes
Keyword(s):  
Amino Acid ◽  
Diblock Copolymer ◽  
Michael Addition ◽  
Self Assembly ◽  
Building Blocks ◽  
Synthesis And Characterization

Two amino acid methacrylates prepared via Michael addition are used as building blocks to prepare novel diblock copolymer nano-objects via polymerisation-induced self-assembly.

A modular approach towards drug delivery vehicles using oxanorbornane-based non-ionic amphiphiles

2016 ◽  
Vol 4 (48) ◽  
pp. 8025-8032 ◽  
Author(s):  
D. Sirisha Janni ◽  
U. Chandrasekhar Reddy ◽  
Soumya Saroj ◽  
K. M. Muraleedharan
Keyword(s):  
Drug Delivery ◽  
Amino Acid ◽  
Self Assembly ◽  
The Self ◽  
Head Group ◽  
Modular Approach ◽  
Drug Delivery Vehicles ◽  
Delivery Vehicles ◽  
Drug Delivery Applications ◽  
Supramolecular Aggregates

The self-assembly of non-ionic amphiphiles with hydroxylated oxanorbornane head-group was controlled using amino acid units as spacers between hydrophilic and lipophilic domains to get spherical supramolecular aggregates suitable for drug delivery applications.

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