Self-assembly of peptide amphiphiles for drug delivery: the role of peptide primary and secondary structures

2017 ◽  
Vol 5 (12) ◽  
pp. 2369-2380 ◽  
Author(s):  
Zhenhua Song ◽  
Xing Chen ◽  
Xinru You ◽  
Keqing Huang ◽  
Arvind Dhinakar ◽  
...  
Keyword(s):  
Drug Delivery ◽  
Self Assembly ◽  
Secondary Structures ◽  
Peptide Amphiphiles ◽  
Alkyl Chains ◽  
Self Assembling

Peptide amphiphiles (PAs), functionalized with alkyl chains, are capable of self-assembling into various nanostructures.

Directive Effect of Chain Length in Modulating Peptide Nano-assemblies

2020 ◽  
Vol 27 (9) ◽  
pp. 923-929
Author(s):  
Gaurav Pandey ◽  
Prem Prakash Das ◽  
Vibin Ramakrishnan
Keyword(s):  
Electron Microscopy ◽  
Amino Acids ◽  
Light Scattering ◽  
Chain Length ◽  
Self Assembly ◽  
The Self ◽  
Ionic Charge ◽  
Self Assembling ◽  
Biophysical Techniques

Background: RADA-4 (Ac-RADARADARADARADA-NH2) is the most extensively studied and marketed self-assembling peptide, forming hydrogel, used to create defined threedimensional microenvironments for cell culture applications. Objectives: In this work, we use various biophysical techniques to investigate the length dependency of RADA aggregation and assembly. Methods: We synthesized a series of RADA-N peptides, N ranging from 1 to 4, resulting in four peptides having 4, 8, 12, and 16 amino acids in their sequence. Through a combination of various biophysical methods including thioflavin T fluorescence assay, static right angle light scattering assay, Dynamic Light Scattering (DLS), electron microscopy, CD, and IR spectroscopy, we have examined the role of chain-length on the self-assembly of RADA peptide. Results: Our observations show that the aggregation of ionic, charge-complementary RADA motifcontaining peptides is length-dependent, with N less than 3 are not forming spontaneous selfassemblies. Conclusion: The six biophysical experiments discussed in this paper validate the significance of chain-length on the epitaxial growth of RADA peptide self-assembly.

Sticky ends in a self-assembling ABA triblock copolymer: the role of ureas in stimuli-responsive hydrogels

2019 ◽  
Vol 4 (1) ◽  
pp. 91-102 ◽  
Author(s):  
Ryan T. Shafranek ◽  
Joel D. Leger ◽  
Song Zhang ◽  
Munira Khalil ◽  
Xiaodan Gu ◽  
...  
Keyword(s):  
Self Assembly ◽  
Viscoelastic Properties ◽  
Triblock Copolymer ◽  
Thermal Response ◽  
Stimuli Responsive ◽  
Self Assembling ◽  
Polymeric Hydrogels ◽  
Aba Triblock Copolymer ◽  
Responsive Hydrogels

Directed self-assembly in polymeric hydrogels allows tunability of thermal response and viscoelastic properties.

scholarly journals A Self-Assembling Amphiphilic Peptide Dendrimer-Based Drug Delivery System for Cancer Therapy

Pharmaceutics ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1092
Author(s):  
Dandan Zhu ◽  
Huanle Zhang ◽  
Yuanzheng Huang ◽  
Baoping Lian ◽  
Chi Ma ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Drug Delivery ◽  
Drug Resistance ◽  
Cancer Therapy ◽  
Self Assembly ◽  
Cancer Drug ◽  
Acquired Drug Resistance ◽  
Self Assembling ◽  
Amphiphilic Peptide ◽  
Peptide Dendrimer

Despite being a mainstay of clinical cancer treatment, chemotherapy is limited by its severe side effects and inherent or acquired drug resistance. Nanotechnology-based drug-delivery systems are widely expected to bring new hope for cancer therapy. These systems exploit the ability of nanomaterials to accumulate and deliver anticancer drugs at the tumor site via the enhanced permeability and retention effect. Here, we established a novel drug-delivery nanosystem based on amphiphilic peptide dendrimers (AmPDs) composed of a hydrophobic alkyl chain and a hydrophilic polylysine dendron with different generations (AmPD KK2 and AmPD KK2K4). These AmPDs assembled into nanoassemblies for efficient encapsulation of the anti-cancer drug doxorubicin (DOX). The AmPDs/DOX nanoformulations improved the intracellular uptake and accumulation of DOX in drug-resistant breast cancer cells and increased permeation in 3D multicellular tumor spheroids in comparison with free DOX. Thus, they exerted effective anticancer activity while circumventing drug resistance in 2D and 3D breast cancer models. Interestingly, AmPD KK2 bearing a smaller peptide dendron encapsulated DOX to form more stable nanoparticles than AmPD KK2K4 bearing a larger peptide dendron, resulting in better cellular uptake, penetration, and anti-proliferative activity. This may be because AmPD KK2 maintains a better balance between hydrophobicity and hydrophilicity to achieve optimal self-assembly, thereby facilitating more stable drug encapsulation and efficient drug release. Together, our study provides a promising perspective on the design of the safe and efficient cancer drug-delivery nanosystems based on the self-assembling amphiphilic peptide dendrimer.

scholarly journals Self-assembly of alkyl chains of fatty acids in papermaking systems: A review of related pitch issues, hydrophobic sizing, and pH effects

BioResources ◽  
2020 ◽  
Vol 15 (2) ◽  
pp. 4591-4635
Author(s):  
Martin A. Hubbe ◽  
Douglas S. McLean ◽  
Karen R. Stack ◽  
Xiaomin Lu ◽  
Anders Strand ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Self Assembly ◽  
Review Article ◽  
Ph Effects ◽  
Monolayer Films ◽  
Alkyl Chains ◽  
Ph Values ◽  
Self Association ◽  
Long Chain

This review article considers the role of fatty acids and the mutual association of their long-chain (e.g. C18) alkyl and alkenyl groups in some important aspects of papermaking. In particular, published findings suggest that interactions involving fatty acids present as condensed monolayer films can play a controlling role in pitch deposition problems. Self-association among the tails of fatty acids and their soaps also helps to explain some puzzling aspects of hydrophobic sizing of paper. When fatty acids and their soaps are present as monolayers in papermaking systems, the pH values associated with their dissociation, i.e. their pKa values, tend to be strongly shifted. Mutual association also appears to favor non-equilibrium multilayer structures that are tacky and insoluble, possibly serving as a nucleus for deposition of wood extractives, such, as resins and triglyceride fats, in pulp and paper systems.

The self-assembly and secondary structure of peptide amphiphiles determine the membrane permeation activity

RSC Advances ◽  
2014 ◽  
Vol 4 (58) ◽  
pp. 30654-30657 ◽  
Author(s):  
Rie Wakabayashi ◽  
Yuko Abe ◽  
Noriho Kamiya ◽  
Masahiro Goto
Keyword(s):  
Secondary Structure ◽  
Membrane Permeability ◽  
Self Assembly ◽  
The Self ◽  
Peptide Amphiphiles ◽  
Membrane Permeation ◽  
Related Peptide ◽  
Self Assembling

New GALA-related peptide amphiphiles were designed and the influence of their self-assembling propensity and the secondary structure on the membrane permeability was studied.

Dissipative Particle Dynamics Studies on the Self-Assembling Dynamics of the Peptide Amphiphiles

2008 ◽  
Vol 1135 ◽  
Author(s):  
Taiga Seki ◽  
Noriyoshi Arai ◽  
Taku Ozawa ◽  
Tomoko Shimada ◽  
Kenji Yasuoka ◽  
...  
Keyword(s):  
Self Assembly ◽  
Dissipative Particle Dynamics ◽  
Particle Dynamics ◽  
The Self ◽  
Peptide Amphiphiles ◽  
Coarse Grained ◽  
Coarse Grained Model ◽  
Self Assembling ◽  
Micro Structures ◽  
Good Agreement

ABSTRACTA coarse-grained model of peptide amphiphiles (PA) dissolved in aqueous solution was presented, where the effects of PA concentration, temperature and shear stress upon the self-assembly of PA were numerically studied by dissipative particle dynamics (DPD) simulation. We technically investigate the repulsion parameter aHW which indicates the repulsion force between the hydrophilic head of PA and water molecules, hence, at the same time, indicating the change in temperature. It was found that aHW played an important role in the self-assembly dynamics and in the resulting micro-structures of PA. By imposing shear strain on the simulation system, the formation of wormlike PA micelles was accelerated. The simulation results were in good agreement with our previous experimental results and the mechanism of shear-induced transition was proposed.

scholarly journals Peptide Nanomaterials for Drug Delivery Applications

2020 ◽  
Vol 21 (4) ◽  
pp. 401-412 ◽  
Author(s):  
Sreekanth Pentlavalli ◽  
Sophie Coulter ◽  
Garry Laverty
Keyword(s):  
Drug Delivery ◽  
Self Assembly ◽  
Diverse Range ◽  
Drug Molecules ◽  
Sustained Drug Delivery ◽  
Self Assembling ◽  
Wide Range ◽  
Methods Of Synthesis ◽  
Self Assembled

Self-assembled peptides have been shown to form well-defined nanostructures which display outstanding characteristics for many biomedical applications and especially in controlled drug delivery. Such biomaterials are becoming increasingly popular due to routine, standardized methods of synthesis, high biocompatibility, biodegradability and ease of upscale. Moreover, one can modify the structure at the molecular level to form various nanostructures with a wide range of applications in the field of medicine. Through environmental modifications such as changes in pH and ionic strength and the introduction of enzymes or light, it is possible to trigger self-assembly and design a host of different self-assembled nanostructures. The resulting nanostructures include nanotubes, nanofibers, hydrogels and nanovesicles which all display a diverse range of physico-chemical and mechanical properties. Depending on their design, peptide self-assembling nanostructures can be manufactured with improved biocompatibility and in vivo stability and the ability to encapsulate drugs with the capacity for sustained drug delivery. These molecules can act as carriers for drug molecules to ferry cargo intracellularly and respond to stimuli changes for both hydrophilic and hydrophobic drugs. This review explores the types of self-assembling nanostructures, the effects of external stimuli on and the mechanisms behind the assembly process, and applications for such technology in drug delivery.

scholarly journals Balancing the intermolecular forces in peptide amphiphiles for controlling self-assembly transitions

2017 ◽  
Vol 15 (24) ◽  
pp. 5220-5226 ◽  
Author(s):  
C. J. Buettner ◽  
A. J. Wallace ◽  
S. Ok ◽  
A. A. Manos ◽  
M. J. Nicholl ◽  
...  
Keyword(s):  
Self Assembly ◽  
Intermolecular Forces ◽  
Peptide Amphiphiles ◽  
Self Assembling

Through balancing the relative repulsive and attractive intermolecular forces, self-assembling peptide amphiphiles with different sizes but similar pH- and concentration-dependent self-assembly behaviour are created.

scholarly journals Control over the fibrillization yield by varying the oligomeric nucleation propensities of self-assembling peptides

2020 ◽  
Vol 3 (1) ◽  
Author(s):  
Chun Yin Jerry Lau ◽  
Federico Fontana ◽  
Laurens D. B. Mandemaker ◽  
Dennie Wezendonk ◽  
Benjamin Vermeer ◽  
...  
Keyword(s):  
Thermodynamic Stability ◽  
Self Assembly ◽  
Biomedical Applications ◽  
Supramolecular Assemblies ◽  
Mechanistic Studies ◽  
Molecular Changes ◽  
Self Assembling ◽  
Charged Residues ◽  
Β Sheet

AbstractSelf-assembling peptides are an exemplary class of supramolecular biomaterials of broad biomedical utility. Mechanistic studies on the peptide self-assembly demonstrated the importance of the oligomeric intermediates towards the properties of the supramolecular biomaterials being formed. In this study, we demonstrate how the overall yield of the supramolecular assemblies are moderated through subtle molecular changes in the peptide monomers. This strategy is exemplified with a set of surfactant-like peptides (SLPs) with different β-sheet propensities and charged residues flanking the aggregation domains. By integrating different techniques, we show that these molecular changes can alter both the nucleation propensity of the oligomeric intermediates and the thermodynamic stability of the fibril structures. We demonstrate that the amount of assembled nanofibers are critically defined by the oligomeric nucleation propensities. Our findings offer guidance on designing self-assembling peptides for different biomedical applications, as well as insights into the role of protein gatekeeper sequences in preventing amyloidosis.

scholarly journals EVOLVING INDUCTIVE GENERALIZATION VIA GENETIC SELF-ASSEMBLY

2006 ◽  
Vol 09 (01n02) ◽  
pp. 1-29 ◽  
Author(s):  
RUDOLF M. FÜCHSLIN ◽  
THOMAS MAEKE ◽  
UWE TANGEN ◽  
JOHN S. McCASKILL
Keyword(s):  
Complex Systems ◽  
Infinite Number ◽  
Self Assembly ◽  
Evolutionary Design ◽  
Full Generality ◽  
Inductive Generalization ◽  
Self Assembling ◽  
Genetic Encoding ◽  
Evolutionary Role

We propose that genetic encoding of self-assembling components greatly enhances the evolution of complex systems and provides an efficient platform for inductive generalization, i.e. the inductive derivation of a solution to a problem with a potentially infinite number of instances from a limited set of test examples. We exemplify this in simulations by evolving scalable circuitry for several problems. One of them, digital multiplication, has been intensively studied in recent years, where hitherto the evolutionary design of only specific small multipliers was achieved. The fact that this and other problems can be solved in full generality employing self-assembly sheds light on the evolutionary role of self-assembly in biology and is of relevance for the design of complex systems in nano- and bionanotechnology.

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