scholarly journals Self-Assembling Multidomain Peptides: Design and Characterization of Neutral Peptide-Based Materials with pH and Ionic Strength Independent Self-Assembly

2018 ◽  
Vol 5 (2) ◽  
pp. 977-985 ◽  
Author(s):  
Tania L. Lopez-Silva ◽  
David G. Leach ◽  
I-Che Li ◽  
Xinran Wang ◽  
Jeffrey D. Hartgerink
Inorganics ◽  
2019 ◽  
Vol 7 (7) ◽  
pp. 91 ◽  
Author(s):  
Marta Gozzi ◽  
Benedikt Schwarze ◽  
Peter Coburger ◽  
Evamarie Hey-Hawkins

3,1,2-Ruthenadicarbadodecaborane complexes bearing the [C2B9H11]2− (dicarbollide) ligand are robust scaffolds, with exceptional thermal and chemical stability. Our previous work has shown that these complexes possess promising anti-tumor activities in vitro, and tend to form aggregates (or self-assemblies) in aqueous solutions. Here, we report on the synthesis and characterization of four ruthenium(II) complexes of the type [3-(η6-arene)-1,2-R2-3,1,2-RuC2B9H9], bearing either non-polar (R = Me (2–4)) or polar (R = CO2Me (7)) substituents at the cluster carbon atoms. The behavior in aqueous solution of complexes 2, 7 and the parent unsubstituted [3-(η6-p-cymene)-3,1,2-RuC2B9H11] (8) was investigated via UV-Vis spectroscopy, mass spectrometry and nanoparticle tracking analysis (NTA). All complexes showed spontaneous formation of self-assemblies (108–109 particles mL−1), at low micromolar concentration, with high polydispersity. For perspective applications in medicine, there is thus a strong need for further characterization of the spontaneous self-assembly behavior in aqueous solutions for the class of neutral metallacarboranes, with the ultimate scope of finding the optimal conditions for exploiting this self-assembling behavior for improved biological performance.


Author(s):  
Sjors Bakels ◽  
Sebastiaan Porskamp ◽  
Anouk Rijs

The spontaneous aggregation of proteins and peptides is widely studied due to its relation to neurodegenerative diseases. To understand the underlying principles of peptide aggregation, elucidation of structure and structural changes upon their formation is key. This level of detail can be obtained by studying the peptide self-assembly in the gas phase. Structural characterization of aggregates is mainly done on charged species, as adding charges is an intrinsic part of the technique to bring molecules into the gas phase. Studying neutral peptide aggregates will complement the existing picture. These studies are restricted to dimers due to experimental limitations. Here, we present advances in laser desorption molecular beam spectroscopy to form neutral peptide aggregates in the gas phase consisting of up to fourteen monomeric peptides. The combination with IR-UV spectroscopy allowed us to select each aggregate by size and subsequently characterize its structure.


2019 ◽  
Author(s):  
Sjors Bakels ◽  
Sebastiaan Porskamp ◽  
Anouk Rijs

The spontaneous aggregation of proteins and peptides is widely studied due to its relation to neurodegenerative diseases. To understand the underlying principles of peptide aggregation, elucidation of structure and structural changes upon their formation is key. This level of detail can be obtained by studying the peptide self-assembly in the gas phase. Structural characterization of aggregates is mainly done on charged species, as adding charges is an intrinsic part of the technique to bring molecules into the gas phase. Studying neutral peptide aggregates will complement the existing picture. These studies are restricted to dimers due to experimental limitations. Here, we present advances in laser desorption molecular beam spectroscopy to form neutral peptide aggregates in the gas phase consisting of up to fourteen monomeric peptides. The combination with IR-UV spectroscopy allowed us to select each aggregate by size and subsequently characterize its structure.


Soft Matter ◽  
2013 ◽  
Vol 9 (42) ◽  
pp. 10025-10030 ◽  
Author(s):  
Isja de Feijter ◽  
Pol Besenius ◽  
Lorenzo Albertazzi ◽  
E. W. Meijer ◽  
Anja R. A. Palmans ◽  
...  

Increasing the ionic strength of solutions of self-assembling discotic amphiphiles results in the coexistence of small and large supramolecular aggregates.


2011 ◽  
Vol 1316 ◽  
Author(s):  
Mounir El-Bakkari ◽  
Rachel L. Beingessner ◽  
Aws Alshamsan ◽  
Jae-Young Cho ◽  
Hicham Fenniri

ABSTRACTDiscrete nanoscale tubular architectures have received significant attention during the past decade because of their potential role in electronic and photonic devices, sensors, liquid crystals, artificial channel systems and biomedical engineering [1-2]. Our research group has reported the synthesis and characterization of the bicyclic G∧C motif, a self complementary DNA base analogue, which undergoes hierarchical self-assembly to form Rosette Nanotubes (RNTs) [3]. The stability of this system depends however, on functional group density (sterics) and net charge (electrostatics) on the RNT surface [5c]. To this end, we have synthesized several G∧C modules bearing oligopeptides with different lengths and net charge and investigated their self-assembling properties.


2016 ◽  
Vol 20 (08n11) ◽  
pp. 1272-1276 ◽  
Author(s):  
Rosalba Randazzo ◽  
Andrea Savoldelli ◽  
D. Andrea Cristaldi ◽  
Alessandra Cunsolo ◽  
Massimiliano Gaeta ◽  
...  

Hierarchical self-assembly of porphyrins is an intrigue research field, which can lead to the design of functional materials. Porphyrin derivatives self-assembling under hierarchical control allows to understand the principles governing molecular recognition processes, as demonstrated for meso-tetrakis(4-phosphonatophenyl)porphyne (H2TPPP) whose polyprotic nature is responsible for a pH-dependent hierarchical aggregation. Herein, self-assembly of meso-tris(4-phosphonatophenyl)corrole (TPPC) in aqueous solution has been spectroscopically studied and compared to that of TPPP. The corrole aggregation does not follow the hierarchical rules that govern the porphyrin counterpart due to the accessibility of the core of the macrocycle to protons, promoted by the reduced number of involved intermolecular H-bonds.


2011 ◽  
Vol 1301 ◽  
Author(s):  
Min Dai ◽  
Jennifer S. Haghpanah ◽  
Carlo Yuvienco ◽  
Jin Kim Montclare

ABSTRACTWe describe the biosynthesis and characterization of protein materials comprised of two distinct self-assembling domains (SADs): elastin (E) found in tissue for its elastic properties and cartilage oligomeric matrix protein coiled-coil (COMPcc, C) predominantly locatedin joint and in bones. Based on earlier studies on protein block polymers comprised these two SADs, orientation and number of blocks play a crucial role in the overall stimuli-responsive supramolecular assembly behavior. Here we fabricate a range of EnC and CEn block polymers in which the E domain is systematically truncated to explore the effects of the E domain on the overall physicochemical behavior.


Nanoscale ◽  
2015 ◽  
Vol 7 (34) ◽  
pp. 14358-14367 ◽  
Author(s):  
Daniele Passeri ◽  
Emanuela Tamburri ◽  
Maria Letizia Terranova ◽  
Marco Rossi

Nanomechanical characterization of micrometric fibers of polyaniline (PANI) doped with nanodiamond (ND) particles resulting from the self-assembling of PANI/ND nano-fibrils has been performed using torsional harmonics atomic force microscopy.


2014 ◽  
Vol 915-916 ◽  
pp. 891-894
Author(s):  
Ge Yang ◽  
Ke Shuai Lu ◽  
Xue Yan Su

The present paper describes the preparation and characterization of novel biodegradable nanoparticles based on self-assembly of poly-γ-glutamic acid (γ-PGA). The nanosystems were stable inaqueous media at low pH conditions. Solubility of the systems was determined by turbidity measurements. Surface charge and mobility were measured electrophoretically. It was found that the size and size distribution of the nanosystems depends on the concentrations of γ-PGA solutions and their ratio as well as on the pH of the mixture and the order of addition. The average hydrodynamic diameters were between 150 and 330 nm. These biodegradable,self-assembling stable nanocomplexes might be useful for several biomedical applications.


2012 ◽  
Vol 9 (1) ◽  
pp. 43 ◽  
Author(s):  
Hueyling Tan

Molecular self-assembly is ubiquitous in nature and has emerged as a new approach to produce new materials in chemistry, engineering, nanotechnology, polymer science and materials. Molecular self-assembly has been attracting increasing interest from the scientific community in recent years due to its importance in understanding biology and a variety of diseases at the molecular level. In the last few years, considerable advances have been made in the use ofpeptides as building blocks to produce biological materials for wide range of applications, including fabricating novel supra-molecular structures and scaffolding for tissue repair. The study ofbiological self-assembly systems represents a significant advancement in molecular engineering and is a rapidly growing scientific and engineering field that crosses the boundaries ofexisting disciplines. Many self-assembling systems are rangefrom bi- andtri-block copolymers to DNA structures as well as simple and complex proteins andpeptides. The ultimate goal is to harness molecular self-assembly such that design andcontrol ofbottom-up processes is achieved thereby enabling exploitation of structures developed at the meso- and macro-scopic scale for the purposes oflife and non-life science applications. Such aspirations can be achievedthrough understanding thefundamental principles behind the selforganisation and self-synthesis processes exhibited by biological systems.


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