scholarly journals Viscoelastic Properties of Dilute Solutions of Random Coil Polymer and α-Helix Polymer

1966 ◽  
Vol 15 (153) ◽  
pp. 447-451
Author(s):  
Hidejiro TANAKA ◽  
Akio SAKANISHI ◽  
Motozo KANEKO ◽  
Jiro FURUICHI
Keyword(s):  
Viscoelastic Properties ◽  
Random Coil ◽  
Dilute Solutions ◽  
Α Helix

scholarly journals Astrocytes Are More Vulnerable than Neurons to Silicon Dioxide Nanoparticle Toxicity in Vitro

Toxics ◽  
2020 ◽  
Vol 8 (3) ◽  
pp. 51
Author(s):  
Jorge Humberto Limón-Pacheco ◽  
Natalie Jiménez-Barrios ◽  
Alejandro Déciga-Alcaraz ◽  
Adriana Martínez-Cuazitl ◽  
Mónica Maribel Mata-Miranda ◽  
...  
Keyword(s):  
Nucleic Acids ◽  
Silicon Dioxide ◽  
Culture Media ◽  
Brain Cell ◽  
Attenuated Total Reflection ◽  
Random Coil ◽  
Silicon Dioxide Nanoparticles ◽  
Neurotoxic Effects ◽  
Α Helix

Some studies have shown that silicon dioxide nanoparticles (SiO2-NPs) can reach different regions of the brain and cause toxicity; however, the consequences of SiO2-NPs exposure on the diverse brain cell lineages is limited. We aimed to investigate the neurotoxic effects of SiO2-NP (0–100 µg/mL) on rat astrocyte-rich cultures or neuron-rich cultures using scanning electron microscopy, Attenuated Total Reflection-Fourier Transform Infrared spectroscopy (ATR-FTIR), FTIR microspectroscopy mapping (IQ mapping), and cell viability tests. SiO2-NPs were amorphous particles and aggregated in saline and culture media. Both astrocytes and neurons treated with SiO2-NPs showed alterations in cell morphology and changes in the IR spectral regions corresponding to nucleic acids, proteins, and lipids. The analysis by the second derivative revealed a significant decrease in the signal of the amide I (α-helix, parallel β-strand, and random coil) at the concentration of 10 µg/mL in astrocytes but not in neurons. IQ mapping confirmed changes in nucleic acids, proteins, and lipids in astrocytes; cell death was higher in astrocytes than in neurons (10–100 µg/mL). We conclude that astrocytes were more vulnerable than neurons to SiO2-NPs toxicity. Therefore, the evaluation of human exposure to SiO2-NPs and possible neurotoxic effects must be followed up.

The Viscoelastic Properties of Dilute Solutions of Polystyrene in Toluene

1964 ◽  
Vol 68 (5) ◽  
pp. 1072-1078 ◽  
Author(s):  
G. Harrison ◽  
J. Lamb ◽  
A. J. Matheson
Keyword(s):  
Viscoelastic Properties ◽  
Dilute Solutions

Influence of Post-Treatment with Methanol Vapor on the Properties of SF/P(LLA-CL) Nanofibrous Scaffolds

2011 ◽  
Vol 236-238 ◽  
pp. 2221-2224
Author(s):  
Kui Hua Zhang ◽  
Xiu Mei Mo
Keyword(s):  
Electrospun Nanofibers ◽  
Random Coil ◽  
Methanol Vapor ◽  
Nanofibrous Scaffolds ◽  
Nanofibrous Structure ◽  
Α Helix ◽  
Β Sheet ◽  
Ideal Method ◽  
C Nmr

In order to improve water-resistant ability silk fibroin (SF) and SF/P(LLA-CL) blended nanofibrous scaffolds for tissue engineering applications, methanol vapor were used to treat electrospun nanofibers. SEM indicated SF and SF/ P(LLA-CL) scaffolds maintained nanofibrous structure after treated with methanol vapor and possessed good water-resistant ability. Characterization of 13C NMR clarified methanol vapor induced SF conformation from random coil or α- helix to β-sheet. Moreover, treated SF/ P (LLA-CL) nanofibrous scaffolds still kept good mechanical properties. Methanol vapor could be ideal method to treat SF and SF/ P(LLA-CL) nanofibrous scaffolds for biomedical applications.

Phospholipids modulate the biophysical properties and vasoactivity of PACAP-(1—38)

2002 ◽  
Vol 93 (4) ◽  
pp. 1377-1383 ◽  
Author(s):  
Takaya Tsueshita ◽  
Salil Gandhi ◽  
Hayat Önyüksel ◽  
Israel Rubinstein
Keyword(s):  
Conformational Transition ◽  
Critical Micellar Concentration ◽  
Random Coil ◽  
Cheek Pouch ◽  
Hamster Cheek Pouch ◽  
Pituitary Adenylate Cyclase ◽  
Peripheral Microcirculation ◽  
Α Helix

The purpose of this study was to elucidate the interactions between pituitary adenylate cyclase-activating peptide (PACAP)-(1—38) and phospholipids in vitro and to determine whether these phenomena modulate, in part, the vasorelaxant effects of the peptide in the intact peripheral microcirculation. We found that the critical micellar concentration of PACAP-(1—38) was 0.4–0.9 μM. PACAP-(1—38) significantly increased the surface tension of a dipalmitoylphosphatidylcholine monolayer and underwent conformational transition from predominantly random coil in saline to α-helix in the presence of distearoyl-phosphatidylethanolamine-polyethylene glycol (molecular mass of 2,000 Da) sterically stabilized phospholipid micelles (SSM) ( P < 0.05). Using intravital microscopy, we found that aqueous PACAP-(1—38) evoked significant concentration-dependent vasodilation in the intact hamster cheek pouch that was significantly potentiated when PACAP-(1—38) was associated with SSM ( P < 0.05). The vasorelaxant effects of aqueous PACAP-(1—38) were mediated predominantly by PACAP type 1 (PAC1) receptors, whereas those of PACAP-(1—38) in SSM predominantly by PACAP/vasoactive intestinal peptide type 1 and 2 (VPAC1/VPAC2) receptors. Collectively, these data indicate that PACAP-(1—38) self-associates and interacts avidly with phospholipids in vitro and that these phenomena amplify peptide vasoactivity in the intact peripheral microcirculation.

Electrochemistry of Alzheimer Disease Amyloid Beta Peptides

2018 ◽  
Vol 25 (33) ◽  
pp. 4066-4083 ◽  
Author(s):  
Ana-Maria Chiorcea-Paquim ◽  
Teodor Adrian Enache ◽  
Ana Maria Oliveira-Brett
Keyword(s):  
Amino Acid ◽  
Amyloid Beta ◽  
Biological Fluids ◽  
Electron Transfer Reaction ◽  
Random Coil ◽  
Sequence Length ◽  
Dependent Manner ◽  
Aβ Peptide ◽  
Aβ Peptides ◽  
Α Helix

Alzheimer’s disease (AD) is a widespread form of dementia that is estimated to affect 44.4 million people worldwide. AD pathology is closely related to the accumulation of amyloid beta (Aβ) peptides in fibrils and plagues, the small oligomeric intermediate species formed during the Aβ peptides aggregation presenting the highest neurotoxicity. This review discusses the recent advances on the Aβ peptides electrochemical characterization. The Aβ peptides oxidation at a glassy carbon electrode occurs in one or two steps, depending on the amino acid sequence, length and content. The first electron transfer reaction corresponds to the tyrosine Tyr10 amino acid residue oxidation, and the second to all three histidine (His6, His13 and His14) and one methionine (Met35) amino acid residues. The Aβ peptides aggregation and amyloid fibril formation are electrochemically detected via the electroactive amino acids oxidation peak currents decrease that occurs in a time dependent manner. The Aβ peptides redox behaviour is correlated with changes in the adsorption morphology from initially random coiled structures, corresponding to the Aβ peptide monomers in random coil or in α-helix conformations, to aggregates, protofibrils and two types of fibrils, corresponding to the Aβ peptides in a β-sheet configuration, observed by atomic force microscopy. Electrochemical studies of Aβ peptides aggregation, mediated by the interaction with metal ions, particularly zinc, copper and iron, and different methodologies concerning the detection of Aβ peptide biomarkers of AD in biological fluids, using electrochemical biosensors, are also discussed.

A Mass Spectrometry Investigation of the Conformational Changes in Adrenocorticotropic Hormones

2002 ◽  
Vol 8 (5) ◽  
pp. 381-387 ◽  
Author(s):  
Hui Lin ◽  
Chhabil Dass
Keyword(s):  
Mass Spectrometry ◽  
Conformational Changes ◽  
Aqueous Media ◽  
Charge State Distribution ◽  
Random Coil ◽  
Helical Conformation ◽  
Ionization Mass ◽  
Time Resolved ◽  
Esi Ms ◽  
Α Helix

Electrospray ionization-mass spectrometry (ESI-MS) was employed to study methanol-induced conformational changes in adrenocorticotrophic hormone (ACTH). ACTH, a 39–residue peptide, is a member of the proopiomelanocortin family of peptides. Charge-state distribution (CSD) and hydrogen–deuterium (H/D) exchange were used to monitor the conformational changes as a function of methanol concentration. The latter experiments were conducted via time-resolved ESI-MS in a continuous-flow apparatus. The CSD and the H/D exchange experimental data both reveal that ACTH exists, presumably in a random coil open structure in aqueous media, but assumes a more compact helical conformation with increased concentration of methanol. The H/D exchange experiments also reveal that 79% of ACTH is present as α-helix in mixed water-methanol solvent media.

scholarly journals Physicochemical Mechanism for the Lipid Membrane Binding of Polyarginine: The Favorable Enthalpy Change with Structural Transition from Random Coil to α-Helix

2012 ◽  
Vol 41 (10) ◽  
pp. 1374-1376 ◽  
Author(s):  
Yuki Takechi ◽  
Chiharu Mizuguchi ◽  
Masafumi Tanaka ◽  
Toru Kawakami ◽  
Saburo Aimoto ◽  
...  
Keyword(s):  
Structural Transition ◽  
Lipid Membrane ◽  
Membrane Binding ◽  
Enthalpy Change ◽  
Random Coil ◽  
Physicochemical Mechanism ◽  
Α Helix

scholarly journals Effect of Oxidation on Quality of Chiba Tofu Produced by Soy Isolate Protein When Subjected to Storage

Foods ◽  
2020 ◽  
Vol 9 (12) ◽  
pp. 1877
Author(s):  
Yue Xu ◽  
Zhongjiang Wang ◽  
Baokun Qi ◽  
Anqi Ran ◽  
Zengwang Guo ◽  
...  
Keyword(s):  
Loss Modulus ◽  
Structural Characteristics ◽  
Soy Protein Isolate ◽  
Protein Isolate ◽  
Sensory Properties ◽  
Random Coil ◽  
Carbonyl Content ◽  
New Type ◽  
Α Helix

Chiba tofu is a new type of vegetarian food prepared with soy protein isolate (SPI). According to factory feedback, the SPI stored in the factory storeroom in summer undergoes reactive oxidation, which changes the structure of SPI and further affects the quality of Chiba tofu. Consequently, the main objective of this study was to prepare Chiba tofu with SPI with different storage periods and evaluate the effect of different degrees of oxidation on structural characteristics of SPI and rheology, texture, microstructure and sensory properties of Chiba tofu. The carbonyl content and turbidity of SPI significantly increased, and the contents of free sulfhydryl (SH) and disulfide bond (S-S) simultaneously decreased with storage time. The oxidation changes the SPI conformation, leading to a transition of α-helix and β-turn to β-sheet and random coil during the storage periods. In the SDS–PAGE analysis, oxidation promoted the SPI molecules crosslinked and aggregated, which affected the quality of Chiba tofu. In short storage periods (0–12 days), SPI was relatively moderately oxidized when the carbonyl content was between 4.14 and 6.87 mmol/g. The storage and loss modulus of Chiba tofu both increased, the network was compact, and the hardness and springiness of Chiba tofu showed an increasing trend. Moreover, in longer storage periods (12–30 days), the SPI was relatively severely oxidized when the carbonyl content was between 7.24 and 9.14 mmol/g, which had an adverse effect on Chiba tofu rheological and texture properties, microstructure, and sensory properties. In sensory evaluation, Chiba tofu stored 12 days had the highest overall quality score than that stored on other days. This study is expected to provide an argument for the better industrial production of Chiba tofu.

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