Light-Driven Dissipative Self-Assembly of a Peptide Hydrogel

2021 ◽  
Author(s):  
Mengmeng Liu ◽  
Cassidy Creemer ◽  
Thomas Reardon ◽  
Jon Parquette
Keyword(s):  
Temporal Resolution ◽  
Self Assembly ◽  
Light Energy ◽  
Waste Production ◽  
Wavelength Tunability ◽  
Fuel Source ◽  
Peptide Hydrogel

Light energy provides an attractive fuel source for energy dissipating systems because of the lack of waste production, wavelength tunability and the potential for spatial and temporal resolution. In this...

scholarly journals Nanostructure, Self-Assembly, Mechanical Properties, and Antioxidant Activity of a Lupin-Derived Peptide Hydrogel

Biomedicines ◽  
2021 ◽  
Vol 9 (3) ◽  
pp. 294
Author(s):  
Raffaele Pugliese ◽  
Anna Arnoldi ◽  
Carmen Lammi
Keyword(s):  
Mechanical Properties ◽  
Antioxidant Activity ◽  
Self Assembly ◽  
Antioxidant Activities ◽  
Functional Materials ◽  
Cd Spectroscopy ◽  
Beneficial Effects ◽  
Naturally Occurring ◽  
New Research ◽  
Peptide Hydrogel

Naturally occurring food peptides are frequently used in the life sciences due to their beneficial effects through their impact on specific biochemical pathways. Furthermore, they are often leveraged for applications in areas as diverse as bioengineering, medicine, agriculture, and even fashion. However, progress toward understanding their self-assembling properties as functional materials are often hindered by their long aromatic and charged residue-enriched sequences encrypted in the parent protein sequence. In this study, we elucidate the nanostructure and the hierarchical self-assembly propensity of a lupin-derived peptide which belongs to the α-conglutin (11S globulin, legumin-like protein), with a straightforward N-terminal biotinylated oligoglycine tag-based methodology for controlling the nanostructures, biomechanics, and biological features. Extensive characterization was performed via Circular Dichroism (CD) spectroscopy, Fourier Transform Infrared spectroscopy (FT-IR), rheological measurements, and Atomic Force Microscopy (AFM) analyses. By using the biotin tag, we obtained a thixotropic lupin-derived peptide hydrogel (named BT13) with tunable mechanical properties (from 2 to 11 kPa), without impairing its spontaneous formation of β-sheet secondary structures. Lastly, we demonstrated that this hydrogel has antioxidant activity. Altogether, our findings address multiple challenges associated with the development of naturally occurring food peptide-based hydrogels, offering a new tool to both fine tune the mechanical properties and tailor the antioxidant activities, providing new research directions across food chemistry, biochemistry, and bioengineering.

scholarly journals Self-Assembly of a Dentinogenic Peptide Hydrogel

ACS Omega ◽  
2018 ◽  
Vol 3 (6) ◽  
pp. 5980-5987 ◽  
Author(s):  
Peter K. Nguyen ◽  
William Gao ◽  
Saloni D. Patel ◽  
Zain Siddiqui ◽  
Saul Weiner ◽  
...  
Keyword(s):  
Self Assembly ◽  
Peptide Hydrogel

RADA16: A Self-Assembly Peptide Hydrogel for the Application in Tissue Regeneration

2014 ◽  
Vol 4 (12) ◽  
pp. 1019-1029 ◽  
Author(s):  
Qingyuan Meng ◽  
Shenglian Yao ◽  
Xiumei Wang ◽  
Yingying Chen
Keyword(s):  
Tissue Regeneration ◽  
Self Assembly ◽  
Peptide Hydrogel

scholarly journals Hierarchical supramolecular hydrogels: self-assembly by peptides and photo-controlled release via host–guest interaction

2017 ◽  
Vol 53 (92) ◽  
pp. 12450-12453 ◽  
Author(s):  
Chih-Wei Chu ◽  
Bart Jan Ravoo
Keyword(s):  
Controlled Release ◽  
Self Assembly ◽  
Peptide Hydrogel ◽  
Guest Chemistry

Using photoresponsive host–guest chemistry, three different payloads can be photo-released successively from the same peptide hydrogel.

scholarly journals A Rapid Self-Assembly Peptide Hydrogel for Recruitment and Activation of Immune Cells

Molecules ◽  
2022 ◽  
Vol 27 (2) ◽  
pp. 419
Author(s):  
Ruyue Luo ◽  
Yuan Wan ◽  
Xinyi Luo ◽  
Guicen Liu ◽  
Zhaoxu Li ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Dendritic Cells ◽  
Self Assembly ◽  
Immune Cell ◽  
Three Dimensional ◽  
Hydrophobic Surface ◽  
Inhibitory Effect ◽  
Blue Staining ◽  
Peptide Hydrogel

Self-assembly peptide nanotechnology has attracted much attention due to its regular and orderly structure and diverse functions. Most of the existing self-assembly peptides can form aggregates with specific structures only under specific conditions and their assembly time is relatively long. They have good biocompatibility but no immunogenicity. To optimize it, a self-assembly peptide named DRF3 was designed. It contains a hydrophilic and hydrophobic surface, using two N-terminal arginines, leucine, and two c-terminal aspartate and glutamic acid. Meanwhile, the c-terminal of the peptide was amidated, so that peptide segments were interconnected to increase diversity. Its characterization, biocompatibility, controlled release effect on antigen, immune cell recruitment ability, and antitumor properties were examined here. Congo red/aniline blue staining revealed that peptide hydrogel DRF3 could be immediately gelled in PBS. The stable β-sheet secondary structure of DRF3 was confirmed by circular dichroism spectrum and IR spectra. The observation results of cryo-scanning electron microscopy, transmission electron microscopy, and atomic force microscopy demonstrated that DRF3 formed nanotubule-like and vesicular structures in PBS, and these structures interlaced with each other to form ordered three-dimensional nanofiber structures. Meanwhile, DRF3 showed excellent biocompatibility, could sustainably and slowly release antigens, recruit dendritic cells and promote the maturation of dendritic cells (DCs) in vitro. In addition, DRF3 has a strong inhibitory effect on clear renal cell carcinoma (786-0). These results provide a reliable basis for the application of peptide hydrogels in biomedical and preclinical trials.

Self-Assembly of an Antiangiogenic Nanofibrous Peptide Hydrogel

2018 ◽  
Vol 1 (3) ◽  
pp. 865-870 ◽  
Author(s):  
Peter K. Nguyen ◽  
Biplab Sarkar ◽  
Zain Siddiqui ◽  
Michael McGowan ◽  
Patricia Iglesias-Montoro ◽  
...  
Keyword(s):  
Self Assembly ◽  
Peptide Hydrogel

scholarly journals Kinetic and energetic insights in the dissipative non-equilibrium operation of an autonomous light-powered supramolecular pump

2021 ◽  
Author(s):  
Stefano Corrà ◽  
Marina Tranfik Bakic ◽  
Jessica Groppi ◽  
Massimo Baroncini ◽  
Serena Silvi ◽  
...  
Keyword(s):  
Self Assembly ◽  
Physicochemical Characterization ◽  
Theoretical Models ◽  
External Source ◽  
Light Energy ◽  
Artificial System ◽  
Depth Study ◽  
First Time ◽  
Non Equilibrium

Natural and artificial autonomous molecular machines operate by constantly dissipating energy coming from an external source to maintain a non-equilibrium state. The in-depth study of these dissipative states is highly challenging as they exist only as long as energy is provided. Here we report on the detailed physicochemical characterization of the dissipative operation of a supramolecular pump transducing light energy into chemical energy by shifting the equilibrium of self-assembly reactions. The composition of the system under light irradiation was followed in real-time by 1H NMR and parameters such as the dissipation and the energy storage at the steady state were extracted for four different irradiation intensities. For the first time in an artificial system, we quantitatively probed the relationship between the light energy input and the deviation of the dissipative state from thermodynamic equilibrium. Our results also provide a testing ground for newly developed theoretical models.

Self-Assembly Processes Were Essential for Life’s Origin

2019 ◽  
Author(s):  
David W. Deamer
Keyword(s):  
Lipid Bilayers ◽  
Self Assembly ◽  
Directed Assembly ◽  
Living Cells ◽  
Light Energy ◽  
Ion Concentration ◽  
Future Research ◽  
Lipid Bilayer Membranes ◽  
Bilayer Membranes ◽  
Transmembrane Channels

In the absence of self-assembly processes, life as we know it would be impossible. This chapter begins by introducing self-assembly then focuses on the primary functions of membranes in living cells, most of which depend on highly evolved proteins embedded in lipid bilayers. These serve to capture light energy in photosynthesis and produce ion concentration gradients from which osmotic energy can be transduced into chemical energy. Although lipid bilayer membranes provide a permeability barrier, they cannot be absolutely impermeable because intracellular metabolic functions depend on external sources of nutrients. Therefore, another set of embedded proteins evolved to form transmembrane channels that allow selective permeation of certain solutes. The earliest life did not have proteins available, so in their absence what was the primary function of membranous compartments in prebiotic conditions? There are three possibilities. First, the compartments would allow encapsulated polymers to remain together as random mixtures called protocells. Second, populations of protocells that vary in composition would be subject to selective processes and the first steps of evolution. Even though any given protocell would be only transiently stable, certain mixtures of polymers would tend to stabilize the surrounding membrane. Such an encapsulated mixture would persist longer than the majority that would be dispersed and recycled, and these more robust protocells would tend to emerge as a kind of species. Last and perhaps most important, there had to be a point in early evolution at which light energy began to be captured by membranous structures, just as it is today. Bilayer membranes are not necessarily composed solely of amphiphilic molecules. They can also contain other nonpolar compounds that happen to be pigments capable of capturing light energy. This possibility is almost entirely unexplored, but the experiments are obvious and would be a fruitful focus for future research. Questions to be addressed: What is meant by self-assembly? Why is self-assembly important for the origin of life? What compounds can undergo self-assembly processes? How can mixtures of monomers and lipids assemble into protocells? We tend to think of living cells in terms of directed assembly.

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