Assembly behavior, structural characterization and rheological properties of legume proteins based amyloid fibrils

Li, Ting; Wang, Li; Zhang, Xinxia; Geng, Han; Xue, Wei; Chen, Zhengxing

doi:10.1016/j.foodhyd.2020.106396

Cited by 85 publications

(33 citation statements)

References 46 publications

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“…Hu et al [64] also observed that ultrasound treatment did not modify the protein SDS-PAGE profiles of SPI at varying intensities and time. As heating time increased, the polypeptide components of SPI with molecular weights of about 80, 75 and 50 kDa were gradually hydrolyzed into low molecular weight peptide, which agreed with the results of Li et al [56] . During the initial stage of heating, the α'α subunits were gradually degraded and completely disappeared at 2 h of heating, which may be related to the increase of H 0 .…”

Section: Resultssupporting

confidence: 90%

“…The nanofibrils structure can affect the rheological properties of proteins, where viscosity represents fluid resistance to flow and is related to molecular interactions [56] . The apparent viscosity of USPIN was shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

“…6 b, the changes in tertiary conformations of USPIN were compared using near-UV CD spectroscopy. The dichroism bands at around 255–270 nm, 275–285 nm and 285–310 nm are the characteristics of Phe, Tyr and Trp residues of the proteins, respectively [56] . The Phe and Tyr dichroism intensity of USPIN and SPIN decreased with increasing heating time, that might be due to protein structural unfolding and polypeptide hydrolysis [34] .…”

Section: Resultsmentioning

confidence: 99%

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Effect mechanism of ultrasound pretreatment on fibrillation Kinetics, physicochemical properties and structure characteristics of soy protein isolate nanofibrils

2021

Ultrasonics Sonochemistry

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Highlights Ultrasound can increase the formation rate of soy protein isolate nanofibrils. Ultrasound-pretreated soy protein isolate nanofibrils has a smaller particle size. Ultrasound can increase β-sheet contents of SPI nanofibrils, promoting the nanofibrils formation. Ultrasound can promote protein unfolding and exposing more binding sites.

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Section: Resultssupporting

confidence: 90%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Effect mechanism of ultrasound pretreatment on fibrillation Kinetics, physicochemical properties and structure characteristics of soy protein isolate nanofibrils

2021

Ultrasonics Sonochemistry

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“…The morphology of the treated samples was determined as described previously [30] . A drop of a sample (2 µg/mL) was placed on a newly cut mica sheet and dried at room temperature for 2 h. The samples were tested in the AFM tapping mode with a silicon cantilever probe (5 N/M), and each image was analyzed using Nanoscope Analysis at three different regions.…”

Section: Methodsmentioning

confidence: 99%

Ultrasonication promotes extraction of antioxidant peptides from oxhide gelatin by modifying collagen molecule structure

Gao

Wang

et al. 2021

Ultrasonics Sonochemistry

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“…Recently, fibrils have been obtained from legume proteins instead of animal proteins such as whey or egg proteins. This could constitute another approach to coat material for cell support [81].…”

Section: Amyloid Fibrillar Coatingsmentioning

confidence: 99%

Amine-Rich Coatings to Potentially Promote Cell Adhesion, Proliferation and Differentiation, and Reduce Microbial Colonization: Strategies for Generation and Characterization

Martocq

Douglas

2021

Coatings

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Biomaterial surface modification represents an important approach to obtain a better integration of the material in surrounding tissues. Different techniques are focused on improving cell support as well as avoiding efficiently the development of infections, such as by modifying the biomaterial surface with amine groups (–NH2). Previous studies showed that –NH2 groups could promote cell adhesion and proliferation. Moreover, these chemical functionalities may be used to facilitate the attachment of molecules such as proteins or to endow antimicrobial properties. This mini-review gives an overview of different techniques which have been used to obtain amine-rich coatings such as plasma methods and adsorption of biomolecules. In fact, different plasma treatment methods are commonly used with ammonia gas or by polymerization of precursors such as allylamine, as well as coatings of proteins (for example, collagen) or polymers containing –NH2 groups (for example, polyethyleneimine). Moreover, this mini-review will present the methods used to characterize such coatings and, in particular, quantify the –NH2 groups present on the surface by using dyes or chemical derivatization methods.

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Assembly behavior, structural characterization and rheological properties of legume proteins based amyloid fibrils

Cited by 85 publications

References 46 publications

Effect mechanism of ultrasound pretreatment on fibrillation Kinetics, physicochemical properties and structure characteristics of soy protein isolate nanofibrils

Effect mechanism of ultrasound pretreatment on fibrillation Kinetics, physicochemical properties and structure characteristics of soy protein isolate nanofibrils

Ultrasonication promotes extraction of antioxidant peptides from oxhide gelatin by modifying collagen molecule structure

Amine-Rich Coatings to Potentially Promote Cell Adhesion, Proliferation and Differentiation, and Reduce Microbial Colonization: Strategies for Generation and Characterization

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