Effect of electrical field on polypeptide phase behavior involving a conformationally coupled anisotropic–isotropic transition

Chen, Tao; Lin, Shaoliang; Lin, Jiaping; Zhang, Liangshun

doi:10.1016/j.polymer.2007.02.001

Cited by 10 publications

(4 citation statements)

References 42 publications

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“…The thermodynamic equilibrium of protein could shift to its denatured state under strong exogenous stimulations. − Several theoretical and experimental works have been carried out to detect the effect of the exogenous perturbation on protein folding and unfolding processes such as temperature, − pressure, − pH changes, and laser excitation . Currently, an active research field is to study the effect of external electric fields acting on proteins. ,,,,,,− It has been experimentally confirmed that microwave radiation could alter protein conformation without bulk heating . The fact that the change of protein conformation can alter the function of protein has been verified by theoretical , and experimental works using amyloid, whose formation of fibrils would result in diseases such as Alzheimer’s disease, cystic fibrosis, and variant Creutzfeldt–Jakob disease.…”

Section: Introductionmentioning

confidence: 99%

Effect of Strong Electric Field on the Conformational Integrity of Insulin

Wang

et al. 2014

J. Phys. Chem. A

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A series of molecular dynamics (MD) simulations up to 1 μs for bovine insulin monomer in different external electric fields were carried out to study the effect of external electric field on conformational integrity of insulin. Our results show that the secondary structure of insulin is kept intact under the external electric field strength below 0.15 V/nm, but disruption of secondary structure is observed at 0.25 V/nm or higher electric field strength. Although the starting time of secondary structure disruption of insulin is not clearly correlated with the strength of the external electric field ranging between 0.15 and 0.60 V/nm, long time MD simulations demonstrate that the cumulative effect of exposure time under the electric field is a major cause for the damage of insulin's secondary structure. In addition, the strength of the external electric field has a significant impact on the lifetime of hydrogen bonds when it is higher than 0.60 V/nm. The fast evolution of some hydrogen bonds of bovine insulin in the presence of the 1.0 V/nm electric field shows that different microwaves could either speed up protein folding or destroy the secondary structure of globular proteins deponding on the intensity of the external electric field.

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Section: Introductionmentioning

confidence: 99%

Effect of Strong Electric Field on the Conformational Integrity of Insulin

Wang

et al. 2014

J. Phys. Chem. A

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“…Among the variety of self-assembled nanostructures, the polymeric micelles formed by block copolymers consisting of polypeptide segments and solvophilic polymer chains have received much interest for their great potential applications [15][16][17][18][19][20][21][22][23][24][25][26][27][28][29][30][31] . Cho et al have reported the formation of polymeric micelles composed of poly(γ-benzyl L-glutamate) and poly(ethylene oxide) in aqueous medium and the drug delivery system based on the core-shell nanoparticles with PBLG as the hydrophobic inner core and PEO as the hydrophilic outer shell 17 .…”

Section: Introductionmentioning

confidence: 99%

Micellization Behavior Comparision of Polypeptide Graft Copolymer and Block-Graft Copolymer in Ethanol

Zhu

2010

J. Chil. Chem. Soc.

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Poly(ethylene glycol)-block-poly(γ-benzyl L-glutamate)-graft-poly(ethylene glycol) (PEG-b-PBLG-g-PEG) copolymer and poly(γ-benzyl L-glutamate)-graftpoly(ethylene glycol) (PBLG-graft-PEG) copolymer were synthesized by the ester exchange reaction of PEG chain with PBLG-block-PEG copolymer and PBLG homopolymer, respectively. The micellization behaviors of PEG-b-PBLG-g-PEG and PBLG-graft-PEG in ethanol were investigated by transmission electron microscopy (TEM) and viscometry. Effects of both the introduction of PBLG homopolymer and the change of testing temperature on the critical aggregation concentration (CAC) of the two polypeptide copolymers in ethanol were mainly studied. Nuclear magnetic resonance (NMR) spectroscopy and fourier transform infrared spectroscopy (FTIR) were used to research the chain conformations of polypeptide segments of the two polypeptide copolymers in solvent and in the solid state, respectively.

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“…1,19 In the grafting reaction, the mole ratio of mPEG to PBLG segments is (20)(21)(22)(23)(24)(25)(26)(27)(28)(29)(30):1, the weight ratio of catalyst to PBLG segments is 5:1, PBLG/ dichloroethane is 1 g/200 mL, and the reaction temperature is controlled between 55 -60 °C with a precision of ±0.1 °C. The pure PEG-b-PBLG-g-PEG copolymer was obtained by dialysis.…”

Section: Syntheses Of Polypeptide Homopolymer and Copolymersmentioning

confidence: 99%

“…[1][2][3][4][5][6][7][8][9][10][11][12] Because of the unique structures and properties, synthesized polypeptides and their copolymers have been investigated widely in the fields of protein simulation, macromolecular conformational study, catalysis, drug delivery, nanoreactors etc. [13][14][15][16][17][18][19][20][21][22][23] Recently, much interest has been focused on the self-association behavior of the copolymers composed of hydrophobic polypeptide segments and hydrophilic polymer chains. 1,[7][8][9][10][11][12][13] Cho et al 9 have reported the formation of polymeric micelles composed of poly(γ-benzyl L-glutamate) and poly(ethylene oxide) in aqueous medium and the drug delivery system based on the core-shell nanoparticles with PBLG as the hydrophobic inner core and PEO as the hydrophilic outer shell.…”

Section: Introductionmentioning

confidence: 99%

Effects of reaction conditions on the grafting percentage of poly(ethylene glycol)-block-poly(γ-benzyl L-glutamate)-graft-poly(ethylene glycol) copolymer

Zhu

Wang

Liu

2010

J. Braz. Chem. Soc.

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a cadeia PEG. A estrutura e propriedades do copolímero PEG-b-PBLG-g-PEG foram investigadas por spetroscopia no infravermelho (FT-IR), microscopia de força atômica (AFM), microscopia eletrônica de varredura (SEM) e calorimetria diferencial de varredura (DSC). Foram investigados os efeitos de temperatura de reação, tempo de reação, e extensão da cadeia dos segmentos PBLG na porcentagem de enxerto do copolímero PEG-b-PBLGg-PEG. Os resultados experimentais demonstraram que a porcentagem de enxerto do copolímero PEG-b-PBLG-g-PEG aumentarou com o aumento do tempo e temperatura de reação, enquanto que o aumento do comprimento da cadeia de segmentos PBLG no copolímero bloco diminuiu a porcentagem de enxerto.In the present work, poly(ethylene glycol)-block-poly(γ-benzyl L-glutamate)-graftpoly(ethylene glycol) (PEG-b-PBLG-g-PEG) copolymer was synthesized by the ester exchange reaction of PEG-block-PBLG copolymer with PEG chain. Structure and properties of PEG-b-PBLG-g-PEG copolymer were investigated by fourier transform infrared spectroscopy (FT-IR), atomic force microscopy (AFM), scanning electron microscopy (SEM), and differential scanning calorimeter (DSC). The effects of reaction temperature, reaction time, and the chain length of PBLG segments on the grafting percentage of PEG-b-PBLG-g-PEG copolymer were studied. Experimental results demonstrated that the grafting percentage of PEG-b-PBLG-g-PEG copolymer increased with the increase of both reaction temperature and reaction time, while the increase of the chain length of PBLG segments in block copolymer decreased the grafting percentage.

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Effect of electrical field on polypeptide phase behavior involving a conformationally coupled anisotropic–isotropic transition

Cited by 10 publications

References 42 publications

Effect of Strong Electric Field on the Conformational Integrity of Insulin

Effect of Strong Electric Field on the Conformational Integrity of Insulin

Micellization Behavior Comparision of Polypeptide Graft Copolymer and Block-Graft Copolymer in Ethanol

Effects of reaction conditions on the grafting percentage of poly(ethylene glycol)-block-poly(γ-benzyl L-glutamate)-graft-poly(ethylene glycol) copolymer

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