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

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.

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.

Bioinspired Phosphatase-like Mimic Built from the Self-Assembly of De Novo Designed Helical Short Peptides

ACS Catalysis ◽  
2021 ◽  
pp. 5839-5849
Author(s):  
Yutong Wang ◽  
Lijun Yang ◽  
Mengfan Wang ◽  
Jiaxing Zhang ◽  
Wei Qi ◽  
...  
Keyword(s):  
Self Assembly ◽  
De Novo ◽  
The Self ◽  
Short Peptides

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

2019 ◽  
Author(s):  
Deepika Mathur ◽  
Harpreet Kaur ◽  
Anjali Dhall ◽  
Neelam Sharma ◽  
Gajendra P. S. Raghava
Keyword(s):  
Amino Acids ◽  
Self Assembly ◽  
Aromatic Amino Acids ◽  
The Self ◽  
Single Amino Acid ◽  
Short Peptides ◽  
Experimental Conditions ◽  
Surface Receptors ◽  
Self Assembling ◽  
Comprehensive Information

AbstractBackgroundNanostructures generated by self-assembly of peptides yield nanomaterial that has many therapeutic applications, including drug delivery and biomedical engineering, due to their low cytotoxicity and higher uptake by targeted cells owing to their high affinity and specificity towards cell surface receptors. Despite the promising implications of this rapidly expanding field, there is no dedicated resource to study peptide nanostructures.ResultThis study endeavours to create a dedicated repository of short peptides, which may prove to be the best models to study ordered nanostructures formed by peptide self-assembly. SAPdb has a repertoire of 1,049 entries of experimentally validated nanostructures formed by the self-assembling of small peptides. It includes 701 entries are of dipeptides, 328 entries belong to tripeptides, and 20 entries of single amino acid with some conjugated partners. Each entry encompasses comprehensive information about the peptide such as chemical modifications in the peptide sequences, the type of nanostructure formed, and experimental conditions like pH, temperature, and solvent required for the self-assembly of the peptide, etc. Further, our analysis has shown that the occurrence of aromatic amino acids favours the formation of self-assembling nanostructures, as indicated by a large number of entries in SAPdb contain aromatics amino acids. Besides, we have observed that these peptides form different nanostructures under different experimental conditions. SAPdb provides this comprehensive information in a hassle-free tabulated manner at a glance. User-friendly browsing, searching, and analysis modules are integrated for easy retrieval and comparison of data and examination of properties. We anticipate SAPdb to be a valuable repository for researchers engaged in the burgeoning arena of nanobiotechnology.AvailabilityThe database can be accessed on the web at https://webs.iiitd.edu.in/raghava/sapdb.

Mechanistic process understanding of the self-assembling behaviour of asymmetric bolaamphiphilic short-peptides and their templating for silica and titania nanomaterials

Nanoscale ◽  
2021 ◽  
Author(s):  
Shengjie Wang ◽  
Fangyuan Liu ◽  
Ning Ma ◽  
Yanpeng Li ◽  
Qian Jing ◽  
...  
Keyword(s):  
Self Assembly ◽  
Functional Materials ◽  
The Self ◽  
Short Peptides ◽  
Biological Functions ◽  
Self Assembling ◽  
Process Understanding ◽  
Silica And Titania

Investigation of self-assembly of peptides is critical important to clarify certain biophysical phenomenon, fulfill some biological functions, and construct functional materials. However, it is still a challenge to precisely predict...

The Nature of Rapidly Extracted Phycocyanin from the Blue-Green Alga Plectonema Boryanum

1971 ◽  
Vol 29 ◽  
pp. 366-367
Author(s):  
M. Kessel ◽  
R. MacColl
Keyword(s):  
Self Assembly ◽  
Analytical Ultracentrifugation ◽  
Uranyl Acetate ◽  
The Self ◽  
Major Protein ◽  
Subunit Structure ◽  
Blue Green Alga ◽  
Thin Sections ◽  
Blue Green Algae ◽  
Cacodylate Buffer

The major protein of the blue-green algae is the biliprotein, C-phycocyanin (Amax = 620 nm), which is presumed to exist in the cell in the form of distinct aggregates called phycobilisomes. The self-assembly of C-phycocyanin from monomer to hexamer has been extensively studied, but the proposed next step in the assembly of a phycobilisome, the formation of 19s subunits, is completely unknown. We have used electron microscopy and analytical ultracentrifugation in combination with a method for rapid and gentle extraction of phycocyanin to study its subunit structure and assembly.To establish the existence of phycobilisomes, cells of P. boryanum in the log phase of growth, growing at a light intensity of 200 foot candles, were fixed in 2% glutaraldehyde in 0.1M cacodylate buffer, pH 7.0, for 3 hours at 4°C. The cells were post-fixed in 1% OsO4 in the same buffer overnight. Material was stained for 1 hour in uranyl acetate (1%), dehydrated and embedded in araldite and examined in thin sections.

Interrelationship of the cellular distribution and secretion of regular structure (RS) protein in Bacillus licheniformis nm 105

1992 ◽  
Vol 50 (1) ◽  
pp. 712-713
Author(s):  
Xiaorong Zhu ◽  
Richard McVeigh ◽  
Bijan K. Ghosh
Keyword(s):  
Alkaline Phosphatase ◽  
Bacillus Licheniformis ◽  
Self Assembly ◽  
Gel Electrophoresis ◽  
Culture Supernatant ◽  
Regular Structure ◽  
The Self ◽  
Cellular Distribution ◽  
Structural Protein ◽  
Laboratory Cultures

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.

Nanoscale Self-Assembly Using Ion and Electron Beam Techniques: A Rapid Review

MRS Advances ◽  
2020 ◽  
Vol 5 (64) ◽  
pp. 3507-3520
Author(s):  
Chunhui Dai ◽  
Kriti Agarwal ◽  
Jeong-Hyun Cho
Keyword(s):  
Electron Beam ◽  
Self Assembly ◽  
Ion Beam ◽  
Three Dimensional ◽  
The Self ◽  
Stress Generation ◽  
Rapid Review ◽  
High Yield ◽  
3D Nanostructures ◽  
Self Assembled

AbstractNanoscale self-assembly, as a technique to transform two-dimensional (2D) planar patterns into three-dimensional (3D) nanoscale architectures, has achieved tremendous success in the past decade. However, an assembly process at nanoscale is easily affected by small unavoidable variations in sample conditions and reaction environment, resulting in a low yield. Recently, in-situ monitored self-assembly based on ion and electron irradiation has stood out as a promising candidate to overcome this limitation. The usage of ion and electron beam allows stress generation and real-time observation simultaneously, which significantly enhances the controllability of self-assembly. This enables the realization of various complex 3D nanostructures with a high yield. The additional dimension of the self-assembled 3D nanostructures opens the possibility to explore novel properties that cannot be demonstrated in 2D planar patterns. Here, we present a rapid review on the recent achievements and challenges in nanoscale self-assembly using electron and ion beam techniques, followed by a discussion of the novel optical properties achieved in the self-assembled 3D nanostructures.

Bottom-up Evolution from Disks to High-Genus Polymersomes

2018 ◽  
Author(s):  
Claudia Contini ◽  
Russell Pearson ◽  
Linge Wang ◽  
Lea Messager ◽  
Jens Gaitzsch ◽  
...  
Keyword(s):  
Self Assembly ◽  
The Self ◽  
Amphiphilic Copolymers ◽  
Chain Entanglement ◽  
Bottom Up ◽  
New Approach ◽  
High Genus ◽  
Transmission Electron ◽  
Minimal Radius ◽  
Stop Flow

<div><div><div><p>We report the design of polymersomes using a bottom-up approach where the self-assembly of amphiphilic copolymers poly(2-(methacryloyloxy) ethyl phosphorylcholine)–poly(2-(diisopropylamino) ethyl methacrylate) (PMPC-PDPA) into membranes is tuned using pH and temperature. We study this process in detail using transmission electron microscopy (TEM), nuclear magnetic resonance (NMR) spectroscopy, dynamic light scattering (DLS), and stop-flow ab- sorbance disclosing the molecular and supramolecular anatomy of each structure observed. We report a clear evolution from disk micelles to vesicle to high-genus vesicles where each passage is controlled by pH switch or temperature. We show that the process can be rationalised adapting membrane physics theories disclosing important scaling principles that allow the estimation of the vesiculation minimal radius as well as chain entanglement and coupling. This allows us to propose a new approach to generate nanoscale vesicles with genus from 0 to 70 which have been very elusive and difficult to control so far.</p></div></div></div>

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