scholarly journals Molecular Determinants for the Self-Assembly of Elastin Peptides

2014 ◽  
Vol 2014 ◽  
pp. 1-4
Author(s):  
Brigida Bochicchio ◽  
Maria Rosaria Armenante ◽  
Maria Antonietta Crudele ◽  
Antonietta Pepe
Keyword(s):  
Molecular Structure ◽  
Mechanical Properties ◽  
Self Assembly ◽  
Terminal Region ◽  
The Self ◽  
Experimental Conditions ◽  
Self Assembling ◽  
Terminal Fragment ◽  
Aggregation Pattern ◽  
Molecular Determinants

Elastin and elastin-related peptides have great potential in the biomaterial field, because of their peculiar mechanical properties and spontaneous self-assembling behavior. Depending on their sequences and under appropriate experimental conditions, they are able to self-assemble in different fiber morphologies, including amyloid-like fibers. In this work, we will review recent data on elastin peptides derived from exon 30-coded domain of human tropoelastin. This domain has been shown to be fundamental for the correct assembly of elastin. However, the N-terminal region forms amyloid-like fibers, while the C-terminal fragment forms elastin-like fibers. A rationale for the varied aggregation pattern has been sought in the molecular structure of the peptides. Minimal differences in the sequences, adopting alternative conformations, are shown to be responsible for the observed data.

Biologically-Based Self-Assembling Hydrogels

2002 ◽  
Vol 724 ◽  
Author(s):  
Brandon L. Seal ◽  
Alyssa Panitch
Keyword(s):  
Mechanical Properties ◽  
Self Assembly ◽  
Binding Pocket ◽  
The Self ◽  
Star Polymer ◽  
Factor Xiiia ◽  
Polymer Mixtures ◽  
Poly Ethylene Glycol ◽  
Self Assembling ◽  
Poly Ethylene

AbstractWe have developed polymers, which borrowing from biology, assemble into networks. The self-assembly regions of fibrinogen were cloned to form a scaffolding that either interacts with fibrin or assembles independently. Peptides consisting of a binding pocket (BP), ligand (L), and/or a Factor XIIIa substrate were synthesized and conjugated to methacroylated dextran or acrylated poly(ethylene glycol). Peptide-conjugated dextran was added to polymerizing fibrin, and the resulting hydrogels were evaluated rheologically. These conjugates significantly affected the mechanical properties of fibrin while the addition of unconjugated dextran did not. The BP and L peptides were conjugated to PEG star polymer. Mixtures of conjugated PEG-BP and PEG-L were found to assemble. This work shows that peptides directing assembly can be designed using motifs found in proteins. The peptides in this study not only alter the mechanical properties of fibrin, but also allow a mechanism for creating a self-assembling network.

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.

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.

Self-assembling behaviour of a modified aromatic amino acid in competitive medium

Soft Matter ◽  
2020 ◽  
Vol 16 (28) ◽  
pp. 6599-6607 ◽  
Author(s):  
Pijush Singh ◽  
Souvik Misra ◽  
Nayim Sepay ◽  
Sanjoy Mondal ◽  
Debes Ray ◽  
...  
Keyword(s):  
Amino Acid ◽  
Self Assembly ◽  
Aromatic Amino Acid ◽  
Photophysical Properties ◽  
Solvent Mixture ◽  
The Self ◽  
Solvent Ratio ◽  
Self Assembling

The self-assembly and photophysical properties of 4-nitrophenylalanine (4NP) are changed with the alteration of solvent and final self-assembly state of 4NP in competitive solvent mixture and are dictated by the solvent ratio.

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>

Z-E isomerization of azobenzene based amphiphilic poly(urethane-urea)s: Influence on the dynamic mechanical properties and the effect of the self-assembly in solution on the isomerization kinetics

2020 ◽  
Vol 127 ◽  
pp. 109583
Author(s):  
Germana Maria Santos Paiva ◽  
Luís Gustavo Teixeira Alves Duarte ◽  
Marcelo Meira Faleiros ◽  
Teresa Dib Zambon Atvars ◽  
Maria Isabel Felisberti
Keyword(s):  
Mechanical Properties ◽  
Self Assembly ◽  
Dynamic Mechanical Properties ◽  
The Self ◽  
Dynamic Mechanical

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.

scholarly journals Self-assembly study of type I collagen extracted from male Wistar Hannover rat tail tendons

2020 ◽  
Vol 24 (1) ◽  
Author(s):  
Jeimmy González-Masís ◽  
Jorge M. Cubero-Sesin ◽  
Simón Guerrero ◽  
Sara González-Camacho ◽  
Yendry Regina Corrales-Ureña ◽  
...  
Keyword(s):  
Regenerative Medicine ◽  
Self Assembly ◽  
Type I Collagen ◽  
Ph Effect ◽  
The Self ◽  
Titration Calorimetry ◽  
Type I ◽  
Self Assembling ◽  
Functional Features ◽  
Rat Tail

Abstract Background Collagen, the most abundant protein in the animal kingdom, represents a promising biomaterial for regenerative medicine applications due to its structural diversity and self-assembling complexity. Despite collagen’s widely known structural and functional features, the thermodynamics behind its fibrillogenic self-assembling process is still to be fully understood. In this work we report on a series of spectroscopic, mechanical, morphological and thermodynamic characterizations of high purity type I collagen (with a D-pattern of 65 nm) extracted from Wistar Hannover rat tail. Our herein reported results can be of help to elucidate differences in self-assembly states of proteins using ITC to improve the design of energy responsive and dynamic materials for applications in tissue engineering and regenerative medicine. Methods Herein we report the systematic study on the self-assembling fibrillogenesis mechanism of type I collagen, we provide morphological and thermodynamic evidence associated to different self-assembly events using ITC titrations. We provide thorough characterization of the effect of pH, effect of salts and protein conformation on self-assembled collagen samples via several complementary biophysical techniques, including circular dichroism (CD), Fourier Transform infrared spectroscopy (FTIR), differential scanning calorimetry (DSC), atomic force microscopy (AFM), scanning electron microscopy (SEM), dynamic mechanical thermal analysis (DMTA) and thermogravimetric analysis (TGA). Results Emphasis was made on the use of isothermal titration calorimetry (ITC) for the thermodynamic monitoring of fibrillogenesis stages of the protein. An overall self-assembly enthalpy value of 3.27 ± 0.85 J/mol was found. Different stages of the self-assembly mechanism were identified, initial stages take place at pH values lower than the protein isoelectric point (pI), however, higher energy release events were recorded at collagen’s pI. Denatured collagen employed as a control exhibited higher energy absorption at its pI, suggesting different energy exchange mechanisms as a consequence of different aggregation routes. Graphical abstract

scholarly journals 2-Deoxyglucose-Modified Folate Derivative: Self-Assembling Nanoparticle Able to Load Cisplatin

Molecules ◽  
2019 ◽  
Vol 24 (6) ◽  
pp. 1084 ◽  
Author(s):  
Shaoming Jin ◽  
Zhongyao Du ◽  
Pengjie Wang ◽  
Huiyuan Guo ◽  
Hao Zhang ◽  
...  
Keyword(s):  
Folic Acid ◽  
Self Assembly ◽  
Water Solubility ◽  
Pure Water ◽  
The Self ◽  
Molar Ratio ◽  
Antineoplastic Drugs ◽  
Self Assembling ◽  
Bonding Interaction ◽  
Nano Drug Delivery

Folic acid has been widely introduced into nano-drug delivery systems to give nanoparticle-targeted characteristics. However, the poor water solubility of folic acid may hinder the exploitation of its ability to load antineoplastic drugs. In the present study, we designed a new folate derivative (FA-2-DG) synthesized from folic acid and 2-Deoxyglucose (2-DG). The aim of this study was to evaluate the self-assembly characteristics of FA-2-DG, and its ability of loading cisplatin. The critical micelle concentration was 7.94 × 10−6 mol L−1. Fourier transform infrared spectroscopy indicated that hydrogen bonding interaction is a main driving force for the self–assembly of FA-2-DG. The particle was stable in pure water or 0.5% bovine serum albumin dispersions. By forming a coordination bond, the particles assembled from FA-2-DG can load cisplatin. The loading efficiency was maximal when the molar ratio of FA-2-DG to cisplatin was 2:1.

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