Journal: Foods

Article Title: Development and Characterization of Quinoa Peptide Nanoparticles as Carriers for Bioactive Food Ingredient Encapsulation

doi: 10.3390/foods15091589

Figure Lengend Snippet: ( A ) Particle size and PDI of quinoa peptide nanoparticles (QPNPs). ( B ) Zeta potentials of QPNPs. ( C ) Transmission electron microscopy (TEM) images of QPNPs, scale bar: 100 nm. Chy-QPNPs, Try-QPNPs, and Alc-QPNPs refer to QPNPs prepared by controllable enzymolysis of α-chymotrypsin, trypsin, and Alcalase 2.4L, respectively. Different letters on columns mean significantly different ( p < 0.05).

Article Snippet: The morphologies of QPNPs and CAPE-loaded QPNPs (CAPE-QPNPs) were observed using a transmission electron microscope (JEM-2100, JEOL Ltd., Tokyo, Japan) according to a previously reported method [ ] with some modifications.

Techniques: Transmission Assay, Electron Microscopy

Journal: Foods

Article Title: Development and Characterization of Quinoa Peptide Nanoparticles as Carriers for Bioactive Food Ingredient Encapsulation

doi: 10.3390/foods15091589

Figure Lengend Snippet: ( A ) Surface tension of quinoa peptide nanoparticles (QPNPs). ( B ) Fourier transform infrared spectroscopy (FT-IR) of QPNPs. ( C ) Effect of different denaturants on the particle size of QPNPs, 1: deionized water; 2: SDS; 3: DTT; 4: Urea; 5: SDS + DTT; 6: DTT + Urea; 7: SDS + Urea; 8: SDS + DTT +Urea. Different letters on columns mean significantly different ( p < 0.05). Chy-QPNPs, Try-QPNPs, and Alc-QPNPs refer to QPNPs prepared by controllable enzymolysis of α-chymotrypsin, trypsin, and Alcalase 2.4L, respectively.

Article Snippet: The morphologies of QPNPs and CAPE-loaded QPNPs (CAPE-QPNPs) were observed using a transmission electron microscope (JEM-2100, JEOL Ltd., Tokyo, Japan) according to a previously reported method [ ] with some modifications.

Techniques: Fourier Transform Infrared Spectroscopy, Spectroscopy

Journal: Foods

Article Title: Development and Characterization of Quinoa Peptide Nanoparticles as Carriers for Bioactive Food Ingredient Encapsulation

doi: 10.3390/foods15091589

Figure Lengend Snippet: ( A ) Particle size distribution of CAPE-loaded QPNPs (CAPE-QPNPs) (Inset: TEM images of CAPE-QPNPs), the different colors represent three independent replicate experiments. ( B ) Fourier transform infrared spectroscopy (FT-IR) of CAPE, QPNPs, and CAPE-QPNPs. ( C ) Secondary structure proportion of QPNPs and CAPE-QPNPs, * p < 0.05, ** p < 0.01.

Article Snippet: The morphologies of QPNPs and CAPE-loaded QPNPs (CAPE-QPNPs) were observed using a transmission electron microscope (JEM-2100, JEOL Ltd., Tokyo, Japan) according to a previously reported method [ ] with some modifications.

Techniques: Fourier Transform Infrared Spectroscopy, Spectroscopy

Journal: Foods

Article Title: Development and Characterization of Quinoa Peptide Nanoparticles as Carriers for Bioactive Food Ingredient Encapsulation

doi: 10.3390/foods15091589

Figure Lengend Snippet: ( A ) Effect of temperatures on the remaining amount of CAPE in CAPE-loaded QPNPs (CAPE-QPNPs), * p < 0.05, ** p < 0.01, *** p < 0.001. ( B ) Effect of irradiation on the remaining amount of CAPE in CAPE-QPNPs. ( C ) Effect of storage time on the particle size of CAPE-QPNPs at 4 °C and 25 °C. ( D ) Effect of storage time on the remaining amount of CAPE in CAPE-QPNPs at 4 °C and 25 °C.

Article Snippet: The morphologies of QPNPs and CAPE-loaded QPNPs (CAPE-QPNPs) were observed using a transmission electron microscope (JEM-2100, JEOL Ltd., Tokyo, Japan) according to a previously reported method [ ] with some modifications.

Techniques: Irradiation

Journal: Foods

Article Title: Development and Characterization of Quinoa Peptide Nanoparticles as Carriers for Bioactive Food Ingredient Encapsulation

doi: 10.3390/foods15091589

Figure Lengend Snippet: In vitro release profile of CAPE-loaded QPNPs (CAPE-QPNPs) in simulated gastric fluid (SGF) and intestinal fluid (SIF). The dotted lines indicate the transition from SGF to SIF and the end of the intestinal digestion phase, respectively.

Article Snippet: The morphologies of QPNPs and CAPE-loaded QPNPs (CAPE-QPNPs) were observed using a transmission electron microscope (JEM-2100, JEOL Ltd., Tokyo, Japan) according to a previously reported method [ ] with some modifications.

Techniques: In Vitro

Journal: Advanced Materials (Deerfield Beach, Fla.)

Article Title: Label‐Free SERS Fingerprinting of Neuroprotein Conformational Dynamics in Human Saliva

doi: 10.1002/adma.202513500

Figure Lengend Snippet: Development of GME method. SEM images of a) AuS@CuO substrate and b) AuS@CuO after GME in the presence of target analytes, c) HR‐TEM and TEM (inset) images of the AuNS on the AuS@CuO in the presence of target analytes, d) elemental mapping on the TEM image area, e) SERS enhancement in GME development, f) real‐time time monitoring of SERS signal changes at 1600 cm −1 and g) time‐resolved spectral evolution during GME, and h) SERS activity of GME for 4‐aminothiophenol and benzoic acid detection on the AuS and AuS@CuO substrate.

Article Snippet: Surface morphology images were characterized by FE‐SEM (JSM‐6700, JEOL) and the cross‐section images and grain structures were characterized by HR‐TEM (JEM‐2200FS with Image Cs‐corrector, JEOL).

Techniques: Activity Assay

Journal: Advanced Materials (Deerfield Beach, Fla.)

Article Title: Label‐Free SERS Fingerprinting of Neuroprotein Conformational Dynamics in Human Saliva

doi: 10.1002/adma.202513500

Figure Lengend Snippet: Material and optical characterization of GME in the presence of protein. a) SEM image of AuS@CuO after GME, b) HR‐TEM image of the AuS‐CuO‐AuNS interfaces area, c) schematic illustration of GME mechanism for protein detection, d) elemental mapping of the corresponding HR‐TEM image area, e) E‐field distribution of GME, f) UV–vis absorbance spectra of AuS@CuO before and after GME in both presence and absence of protein, g) SERS enhancement of GME method for protein detection (scale bar refers to SERS intensity), h) SERS performance of the GME method at various cyt c concentrations, i) signal uniformity test with 100 different points, j) reproducibility test with 5 independent test for each batch, k) stability test of GME at various storage time.

Article Snippet: Surface morphology images were characterized by FE‐SEM (JSM‐6700, JEOL) and the cross‐section images and grain structures were characterized by HR‐TEM (JEM‐2200FS with Image Cs‐corrector, JEOL).

Techniques:

Journal: ACS Materials Au

Article Title: Facet-Specific Liquid-Phase Exfoliation of an Ionic 1D Crystal, (NbSe 4 ) 3 I, into Ultrathin Nanoribbons

doi: 10.1021/acsmaterialsau.5c00143

Figure Lengend Snippet: Nanoscale morphology and structure of exfoliated (NbSe 4 ) 3 I nanocrystals. (A) Atomic resolution C S -corrected HAADF-STEM image of (NbSe 4 ) 3 I acquired from nanoribbons exfoliated from bulk needles in THF (left) and the corresponding simulated image (right). (B) SAED patterns of (NbSe 4 ) 3 I acquired from nanoribbons exfoliated from bulk needles in THF along the [110] (left) and [100] (right) zone axes. (C) Wide-field TEM image of (NbSe 4 ) 3 I nanoribbons from the exfoliation of bulk needles in THF. (D) HRTEM image of the resulting nanoribbons from the exfoliation of bulk needles in THF. (E) FFT of the micrograph in part D. (F) Wide-field TEM image of (NbSe 4 ) 3 I nanoribbons from the exfoliation of bulk flakes in chloroform. (G) HRTEM image of the resulting nanoribbons from the exfoliation of bulk flakes in chloroform. (H) FFT of the micrograph in G. (I) Wide-field TEM image of nonuniform (NbSe 4 ) 3 I nanocrystals from the exfoliation of powdered samples in water. (J) HRTEM image of the resulting nanocrystals from the exfoliation of powdered samples in water. (K) FFT of the micrograph in J.

Article Snippet: Aberration-corrected HAADF-STEM was performed on a JEOL JEM-ARM300F instrument operated at 300 kV.

Techniques:

Journal: Scientific reports

Article Title: Circulatory extracellular vesicle derived miR-195-5p promotes cellular apoptosis and suppresses cell proliferation in the buffalo endometrial primary cell culture.

doi: 10.1038/s41598-023-43530-y

Figure Lengend Snippet: Figure 1. Characterization of extracellular vesicles. (A) Intensity-based Size distribution of buffalo blood plasma-derived EVs, as assessed by the Zetasizer nano zs particle sizer. Each curve shows means ± SD from three replicates in a representative experiment out of the three performed with similar results. (B) Nanoparticle Tracking Analysis (NTA) on the buffalo blood plasma-derived small EVs under 100× dilutions. FTLA size per concentration graph, taken as five replicates (C) graph represents the averaged FTLA size per concentration (particles/ml) (D) Transmission Electron Microscopy (TEM). TEM image of EVs derived from buffalo blood plasma. EVs were negatively stained with 1% phosphotungstic acid after removing the extra moisture. (Magnification-250000×, Scale bar—50 nm, 120 kV) (E) Identification of the CD9, CD63 and TSG101 EV-specific protein markers by the western blot analysis of isolated pooled EVs samples from the blood plasma of Murrah buffalo. Full blots are shown in Supplementary Fig. S3A–C.

Article Snippet: TEM examination was performed using JEM1400 FLASH transmission electron microscope (JEOL USA Inc, Peabody, MA, United States) at 120 kV and viewed under 250,000× magnification with highly sensitive olympus sCMOS camera at the TEM facility of Advanced Technology Platform Centre (ATPC), Regional Centre for Biotechnology, Faridabad.

Techniques: Clinical Proteomics, Derivative Assay, Concentration Assay, Transmission Assay, Electron Microscopy, Staining, Western Blot, Isolation