Aromatic identity, electronic substitution, and sequence in amphiphilic tripeptide self-assembly

Soft Matter ◽  
2018 ◽  
Vol 14 (45) ◽  
pp. 9168-9174 ◽  
Author(s):  
Jugal Kishore Sahoo ◽  
Calvin Nazareth ◽  
Michael A. VandenBerg ◽  
Matthew J. Webber
Keyword(s):  
Self Assembly ◽  
Short Peptides ◽  
Design Rules ◽  
Sequence Variations

The design rules for self-assembly of short peptides are assessed using a combination of chemical and sequence variations.

Tuning the Self-Assembly of Short Peptides via Sequence Variations

Langmuir ◽  
2013 ◽  
Vol 29 (44) ◽  
pp. 13457-13464 ◽  
Author(s):  
Yurong Zhao ◽  
Jiqian Wang ◽  
Li Deng ◽  
Peng Zhou ◽  
Shengjie Wang ◽  
...  
Keyword(s):  
Self Assembly ◽  
The Self ◽  
Short Peptides ◽  
Sequence Variations

scholarly journals SAPdb: A database of short peptides and the corresponding nanostructures formed by self-assembly

2021 ◽  
pp. 104391
Author(s):  
Deepika Mathur ◽  
Harpreet Kaur ◽  
Anjali Dhall ◽  
Neelam Sharma ◽  
Gajendra P.S. Raghava
Keyword(s):  
Self Assembly ◽  
Short Peptides

scholarly journals Organic/Inorganic hydrogels by simultaneous self-assembly and mineralization of aromatic short-peptides

2022 ◽  
Author(s):  
Mari C. Mañas-Torres ◽  
Gloria Belén Ramírez-Rodríguez ◽  
Jose I. Garcia-Peiro ◽  
Belen Parra-Torrejón ◽  
Juan Manuel Cuerva ◽  
...  
Keyword(s):  
Self Assembly ◽  
Short Peptides ◽  
Self Assembled

Self-assembled peptides and proteins have turned out to be excellent templates for the growth of inorganic minerals trying to emulate natural biomineralization processes. Doing this, researchers have developed complex sophisticate...

Peptide α-helices for synthetic nanostructures

2007 ◽  
Vol 35 (3) ◽  
pp. 487-491 ◽  
Author(s):  
M.G. Ryadnov
Keyword(s):  
Self Assembly ◽  
De Novo ◽  
Three Dimensional ◽  
Functional Materials ◽  
Protein Assemblies ◽  
Helical Peptides ◽  
Design Rules ◽  
Natural Protein ◽  
Self Assembling ◽  
Recent Developments

Supramolecular structures arising from a broad range of chemical archetypes are of great technological promise. Defining such structures at the nanoscale is crucial to access principally new types of functional materials for applications in bionanotechnology. In this vein, biomolecular self-assembly has emerged as an efficient approach for building synthetic nanostructures from the bottom up. The approach predominantly employs the spontaneous folding of biopolymers to monodisperse three-dimensional shapes that assemble into hierarchically defined mesoscale composites. An immediate interest here is the extraction of reliable rules that link the chemistry of biopolymers to the mechanisms of their assembly. Once established these can be further harnessed in designing supramolecular objects de novo. Different biopolymer classes compile a rich repertoire of assembly motifs to facilitate the synthesis of otherwise inaccessible nanostructures. Among those are peptide α-helices, ubiquitous folding elements of natural protein assemblies. These are particularly appealing candidates for prescriptive supramolecular engineering, as their well-established and conservative design rules give unmatched predictability and rationale. Recent developments of self-assembling systems based on helical peptides, including fibrous systems, nanoscale linkers and reactors will be highlighted herein.

scholarly journals Biocatalysis of d,l-Peptide Nanofibrillar Hydrogel

Molecules ◽  
2020 ◽  
Vol 25 (13) ◽  
pp. 2995 ◽  
Author(s):  
Tiziano Carlomagno ◽  
Maria C. Cringoli ◽  
Slavko Kralj ◽  
Marina Kurbasic ◽  
Paolo Fornasiero ◽  
...  
Keyword(s):  
Self Assembly ◽  
Solid Phase ◽  
Building Blocks ◽  
Cd Spectroscopy ◽  
Tem Analysis ◽  
Design Rules ◽  
Self Assembling ◽  
Transmission Electron ◽  
Oscillatory Rheometry ◽  
The Many

Self-assembling peptides are attracting wide interest as biodegradable building blocks to achieve functional nanomaterials that do not persist in the environment. Amongst the many applications, biocatalysis is gaining momentum, although a clear structure-to-activity relationship is still lacking. This work applied emerging design rules to the heterochiral octapeptide sequence His–Leu–DLeu–Ile–His–Leu–DLeu–Ile for self-assembly into nanofibrils that, at higher concentration, give rise to a supramolecular hydrogel for the mimicry of esterase-like activity. The peptide was synthesized by solid-phase and purified by HPLC, while its identity was confirmed by 1H-NMR and electrospray ionization (ESI)-MS. The hydrogel formed by this peptide was studied with oscillatory rheometry, and the supramolecular behavior of the peptide was investigated with transmission electron microscopy (TEM) analysis, circular dichroism (CD) spectroscopy, thioflavin T amyloid fluorescence assay, and attenuated total reflectance (ATR) Fourier-transform infrared (FT-IR) spectroscopy. The biocatalytic activity was studied by monitoring the hydrolysis of p-nitrophenyl acetate (pNPA) at neutral pH, and the reaction kinetics followed an apparent Michaelis–Menten model, for which a Lineweaver–Burk plot was produced to determine its enzymatic parameters for a comparison with the literature. Finally, LC–MS analysis was conducted on a series of experiments to evaluate the extent of, if any, undesired peptide acetylation at the N-terminus. In conclusion, we provide new insights that allow gaining a clearer picture of self-assembling peptide design rules for biocatalysis.

Phosphobisaromatic motifs enable rapid enzymatic self-assembly and hydrogelation of short peptides

Soft Matter ◽  
2021 ◽  
Author(s):  
Meihui Yi ◽  
Jiaqi Guo ◽  
Hongjian He ◽  
Weiyi Tan ◽  
Nya Harmon ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Self Assembly ◽  
Soft Materials ◽  
Short Peptides

Enzyme-instructed self-assembly (EISA) and hydrogelation is a versatile approach for generating soft materials. Most of the substrates for alkaline phosphatase catalysed EISA utilizes phosphotyrosine (pTyr) as the enzymatic trigger for...

Polyoxometalate-Driven Self-Assembly of Short Peptides into Multivalent Nanofibers with Enhanced Antibacterial Activity

2016 ◽  
Vol 128 (7) ◽  
pp. 2638-2641 ◽  
Author(s):  
Jingfang Li ◽  
Zhijun Chen ◽  
Mengcheng Zhou ◽  
Jiangbo Jing ◽  
Wen Li ◽  
...  
Keyword(s):  
Antibacterial Activity ◽  
Self Assembly ◽  
Short Peptides
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