Aggregation behavior of N-carboxyethylchitosan in aqueous solution: effects of pH, polymer concentration, and presence of a gemini surfactant

Peng, Baoliang; Hao, Yongliang; Kang, Hongzhang; Han, Xia; Peng, Changjun; Liu, Honglai

doi:10.1016/j.carres.2009.10.018

Cited by 14 publications

(4 citation statements)

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“…These zeta potential measurements provided the direct information on the charge density of the solution and electrostatic interactions among charged segments. Theoretically, a polymer solution would be unstable and aggregate when the | | < 30 mV [34]. There were enough protonated imidazole and deprotonated carboxylic groups coexisted, where the | | was closed to zero near the pI.…”

Section: Electrophoretic Mobility and The Determination Of Isoelectrimentioning

confidence: 98%

Synthesis of a novel zwitterionic biodegradable poly (α,β-l-aspartic acid) derivative with some l-histidine side-residues and its resistance to non-specific protein adsorption

Wang

et al. 2011

Colloids and Surfaces B: Biointerfaces

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Section: Electrophoretic Mobility and The Determination Of Isoelectrimentioning

confidence: 98%

Synthesis of a novel zwitterionic biodegradable poly (α,β-l-aspartic acid) derivative with some l-histidine side-residues and its resistance to non-specific protein adsorption

Wang

et al. 2011

Colloids and Surfaces B: Biointerfaces

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“…Rate constant (k X 10 different functional groups will be changed, influencing assembly (Peng et al, 2010). Fig.…”

Section: Factorsmentioning

confidence: 99%

Effect of concentration, pH and ionic strength on the kinetic self-assembly of acid-soluble collagen from walleye pollock (Theragra chalcogramma) skin

Yan

Zhao

et al. 2012

Food Hydrocolloids

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“…The pH value of protein solution has a great influence on the aggregation behavior of protein molecules because the pH could change the charge of different functional groups. 40 When the pH was nearby the isoelectric point of walleye pollock ( Theragra chalcogramma ) skin collagen, the aggregation degree of collagen was enhanced. 41 Because the isoelectric point of the acylated collagen was 4.93, 21 the pH values in the region from 4.0 to 9.0 were selected to investigate the fluorescence intensity of the acylated collagen solution and the intensity data are shown in Table II.…”

Section: Resultsmentioning

confidence: 99%

Aggregation Behavior of Acylated Pepsin-Solubilized Collagen Based on Fluorescence Spectrum Technology

et al. 2020

Appl Spectrosc

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The aggregation behavior of collagen-based materials plays an important role in their processing because it could affect their physicochemical properties. Based on the intrinsic fluorescence characteristic of tyrosine, fluorescence spectrum technology was used to investigate the aggregation state of the acylated collagen molecules in aqueous solution. The results showed that the aggregate degree of the acylated collagen was higher than that of the native collagen due to the hydrophobic interaction. With the increase of concentrations of the acylated collagen or at NaCl higher than 40 mmol/L, the aggregate degree of the acylated collagen molecules increased. When the pH was close to the isoelectric point of the acylated collagen, the hydrophobic interaction and the hydrogen bond helped to increase the aggregation degree. However, with the increase of temperature (10–70 ℃), the aggregation state of the acylated collagen decreased gradually due to the quenching, the molecular collision, and the broken of hydrogen bonds. Furthermore, two-dimensional correlation spectroscopy (2D-COS) showed that the response order was 360 > 305 nm at various acylated collagen and NaCl (>40 mmol/L) concentrations, while the response order was 305 > 360 nm when the pH value was increased from 5.0 to 9.0. Temperature-dependent 2D-COS showed there were four bands that occurred and the response order was listed as follows: 293 > 305 > 360 > 420 nm. In brief, the results might provide an important guide for molding processes of the acylated collagen.

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Aggregation behavior of N-carboxyethylchitosan in aqueous solution: effects of pH, polymer concentration, and presence of a gemini surfactant

Cited by 14 publications

References 50 publications

Synthesis of a novel zwitterionic biodegradable poly (α,β-l-aspartic acid) derivative with some l-histidine side-residues and its resistance to non-specific protein adsorption

Synthesis of a novel zwitterionic biodegradable poly (α,β-l-aspartic acid) derivative with some l-histidine side-residues and its resistance to non-specific protein adsorption

Effect of concentration, pH and ionic strength on the kinetic self-assembly of acid-soluble collagen from walleye pollock (Theragra chalcogramma) skin

Aggregation Behavior of Acylated Pepsin-Solubilized Collagen Based on Fluorescence Spectrum Technology

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