Nanoparticle Surface Specific Adsorption of Zein and Its Self-assembled Behavior of Nanocubes Formation in Relation to On–Off SERS: Understanding Morphology Control of Protein Aggregates

Navdeep,; Banipal, Tarlok S.; Kaur, Gurinder; Bakshi, Mandeep Singh

doi:10.1021/acs.jafc.5b05495

Cited by 24 publications

(13 citation statements)

References 54 publications

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“…This is the region (pH 5–9) where color transformation from light gray to light yellow-brown occurs, which eventually converts into dark brown. At pH 2.55 (acetic acid reaction medium, see Experimental Section), zein coated NPs exist in self-aggregated state (Figure ), which is prompted by the fusogenic behavior of zein due to the screening of surface negative charge (zein is solubilized in aqueous SDS). Increase in the pH reduces the charge screening and increases the Columbic repulsions with the result that NPs start to disperse and show increasing absorbance.…”

Section: Resultsmentioning

confidence: 99%

pH Responsive Bioactive Lead Sulfide Nanomaterials: Protein Induced Morphology Control, Bioapplicability, and Bioextraction of Nanomaterials

Mahal¹,

Tandon²,

Khullar³

et al. 2016

ACS Sustainable Chem. Eng.

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Precise morphologies of pH responsive bioactive lead sulfide nanoparticles (PbS NPs) were synthesized by using industrially and environmentally important proteins like zein and lysozyme (Lys), and a bioactive polymer diethylaminoethyl dextran chloride (DEAE). Though, proteins are not known morphology control agents, zein demonstrated a fine crystal growth control of PbS NPs better than Lys as well as DEAE, and even better than conventional surfactants known for their shape control behavior. Proteins and DEAE coated NPs thus obtained were highly pH responsive in terms of a color change from light gray (at low pH) to dark brown (at high pH). Bioapplicability of coated NPs was done by subjecting them to hemolysis. Both Lys and DEAE coated NPs did not induce any significant hemolysis and demonstrated their good compatibility and usability in systemic circulation. For their industrial scale uses, different extraction methods were proposed by using other industrially important biomolecules and ionic liquids. Alginic acid and xanthan gum were excellent complexing agents for an instant extraction of Lys and DEAE coated NPs from aqueous phase. Ionic liquid exhibited excellent extraction ability in both organic as well as aqueous phases.

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Section: Resultsmentioning

confidence: 99%

pH Responsive Bioactive Lead Sulfide Nanomaterials: Protein Induced Morphology Control, Bioapplicability, and Bioextraction of Nanomaterials

Mahal¹,

Tandon²,

Khullar³

et al. 2016

ACS Sustainable Chem. Eng.

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“…The mixture was shaken thoroughly for some time and kept in a thermostat bath at constant 80 °C for 24 h. Zein initiated the reduction and converted Ag(I) into Ag(0) with final pink to purple or yellow-brown color. 11 As soon as the Ag nucleating centers were created, zein stabilized them by surface adsorption and limiting growth proceeded to form tiny Ag NPs. The following reaction is expected to take place within first few hours of the reaction.…”

Section: Methodsmentioning

confidence: 99%

“…It triggers protein–protein interactions through seeding that leads to the onset of self-aggregation. 11−14 This complex process is little understood and requires a proper mechanistic approach to understand. It is particularly more prevalent in predominantly water-insoluble or hydrophobic proteins which contain high proportions of nonpolar amino acids.…”

Section: Introductionmentioning

confidence: 99%

Ag Nanometallic Surfaces for Self-Assembled Ordered Morphologies of Zein

Gurtu

Bakshi

2018

ACS Omega

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Nanometallic surfaces of Ag nanoparticles (NPs) catalyzed the self-aggregation behavior of zein in different ordered morphologies such as cubes, rectangles, and bars. This was studied in a ternary in situ reaction (AgNO 3 + zein + water), where zein performed the reduction as well as stabilization of Ag NPs. This reaction produced small Ag NPs of less than 10 nm predominantly bound with {111} crystal planes, which attracted the surface adsorption of zein. Surface-adsorbed zein initiated the protein seeding and converted the tertiary structure of protein into open β-pleated structure with aqueous exposed hydrophobic domains. A layered deposition of β-pleats on different crystal planes of Ag NPs derived them to nearly monodispersed cubic morphologies. The mechanistic aspects of self-aggregation of zein in the presence of nanometallic surfaces hold possible scenarios for simple and straightforward routes of protein crystallization.

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“…Glutenin is a heterogeneous mixture of a number of different high and low molecular mass subunits connected through disulfide bonds with strong hydrophobic interactions and hence constitutes up to 47% of the total protein contents . The presence of glutenin makes gluten highly hydrophobic, and hence it cannot be easily solubilized in water but is readily soluble in aqueous micellar solution. − Surfactant molecules in the aqueous phase interact with the hydrophobic domains of protein through their hydrocarbon chains while their polar head groups provide essential polarity for aqueous solubilization . Aqueous solubilized wheat protein is an excellent candidate for nanometallic surface adsorption and its subsequent applications in materials chemistry.…”

Section: Introductionmentioning

confidence: 99%

Role of Gluten in Surface Chemistry: Nanometallic Bioconjugation of Hard, Medium, and Soft Wheat Protein

Mandial¹,

Khullar²,

Gupta³

et al. 2019

J. Agric. Food Chem.

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Hard, medium, and soft wheat proteins, based on gluten content, were studied for their important roles in nanometallic surface chemistry. In situ synthesis of Au nanoparticles (NPs) was followed to determine the surface adsorption behavior of wheat protein based on the gluten contents. A greater amount of gluten contents facilitated the nucleation to produce Au NPs. X-ray photoelectron spectroscopy (XPS) surface analysis clearly showed the surface adsorption of protein on nanometallic surfaces which was almost equally prevalent for the hard, medium, and soft wheat proteins. Wheat protein conjugated NPs were highly susceptible to phase transfer from aqueous to organic phase that was entirely related to the amount of gluten contents. The presence of higher gluten content in hard wheat protein readily enabled the hard wheat protein conjugated NPs to move across the aqueous−organic interface followed by medium and soft wheat protein conjugated NPs. Sodium dodecyl sulfate−polyacrylamide gel electrophoresis (SDS page) analysis allowed us to determine molar masses of nanometallic surface adsorbed protein fractions. Only two protein fractions of high molar masses (74 and 85 kDa) from SDS solubilized hard, medium, and soft wheat proteins preferred to adsorb on nanometallic surfaces out of more than 15 protein fractions of pure wheat protein. This made the surface adsorption of wheat protein highly selective and closely related to gluten content. Cetyltrimethylammonium bromide (CTAB) solubilized wheat protein conjugated NPs demonstrated their strong antimicrobial activities against both Gram negative and Gram positive bacteria making them suitable for their applications in food industry.

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Nanoparticle Surface Specific Adsorption of Zein and Its Self-assembled Behavior of Nanocubes Formation in Relation to On–Off SERS: Understanding Morphology Control of Protein Aggregates

Cited by 24 publications

References 54 publications

pH Responsive Bioactive Lead Sulfide Nanomaterials: Protein Induced Morphology Control, Bioapplicability, and Bioextraction of Nanomaterials

pH Responsive Bioactive Lead Sulfide Nanomaterials: Protein Induced Morphology Control, Bioapplicability, and Bioextraction of Nanomaterials

Ag Nanometallic Surfaces for Self-Assembled Ordered Morphologies of Zein

Role of Gluten in Surface Chemistry: Nanometallic Bioconjugation of Hard, Medium, and Soft Wheat Protein

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