Journal: Materials Today Bio

Article Title: Targeting FN1 to overcome gemcitabine resistance in gallbladder cancer: Mechanistic insights and an iRGD-modified PEG-PLGA nanoparticle delivery strategy

doi: 10.1016/j.mtbio.2026.102877

Figure Lengend Snippet: Preparation and characterization of iRGD-NPs (si-FN1). Note: (A) Schematic of iRGD-NPs (si-FN1) synthesis; (B-C) NP size distribution curve and size statistics for iRGD-NPs (si-FN1); (D) ζ-potential of iRGD-NPs (si-FN1); (E) Representative TEM image of iRGD-NPs (si-FN1), Scale bars = 500 nm; (F) RNA agarose gel electrophoresis assessing the EE% of si-FN1; (G) Agarose gel electrophoresis testing the stability of Free si-FN1 and iRGD-NPs (si-FN1) under RNase treatment; (H) Agarose gel electrophoresis testing the stability of Free si-FN1 and iRGD-NPs (si-FN1) incubated at ambient temperature in 25% FBS for 0, 2, 6, and 24 h, followed by treatment with heparin (1000 I.U./mL) for 1 h; (I) DLS measurement of particle size changes of iRGD-NPs (si-FN1) incubated at ambient temperature in 25% FBS for 0, 2, 6, 24, 48, and 72 h; (J) PDI values of the nanoparticle formulations determined by DLS; (K) Characterization of nanoparticle chemical functional groups using Fourier transform infrared spectroscopy. Experiments were repeated three times.

Article Snippet: The NPs (si-FN1) were then conjugated with iRGD peptides (HY-P0122, MCE, USA) through the interaction of the Mal group in Mal–PEG–PLGA with thiol groups in the iRGD peptide for 24 h. The molar ratio of NPs (si-FN1) to iRGD used for binding was 4:1.

Techniques: Agarose Gel Electrophoresis, Incubation, Functional Assay, Fourier Transform Infrared Spectroscopy, Spectroscopy

Journal: Materials Today Bio

Article Title: Targeting FN1 to overcome gemcitabine resistance in gallbladder cancer: Mechanistic insights and an iRGD-modified PEG-PLGA nanoparticle delivery strategy

doi: 10.1016/j.mtbio.2026.102877

Figure Lengend Snippet: In vivo biodistribution and in vitro cellular uptake of iRGD-NPs (si-FN1). Note: (A) Schematic of the in vivo biodistribution testing experiment of iRGD-NPs (si-FN1) in nude mice with subcutaneous xenografts; (B) IVIS images of xenograft-bearing mice at 0, 4, 8, 12, and 24 h after injection with Cy5.5-labeled iRGD-NPs (si-FN1) and NPs (si-FN1); (C) Representative IVIS images of xenograft tissues and various organs from mice 24 h after injection with Cy5.5-labeled iRGD-NPs (si-FN1) and NPs (si-FN1), ∗ indicates p < 0.05; (D) Schematic of the in vitro cellular uptake experiment for iRGD-NPs (si-FN1); (E-F) Immunofluorescence staining (E) and FCM (F) assessing the uptake of iRGD-NPs (si-FN1) by GBC-SD/GEM and NOZ/GEM cells, Scale bars = 25 μm; (G) 3D tumor spheroid model assessing the tumor-penetration capability conferred by iRGD modification (Scale bars = 500 μm). experiments repeated three times. Each group consists of 3 nude mice.

Article Snippet: The NPs (si-FN1) were then conjugated with iRGD peptides (HY-P0122, MCE, USA) through the interaction of the Mal group in Mal–PEG–PLGA with thiol groups in the iRGD peptide for 24 h. The molar ratio of NPs (si-FN1) to iRGD used for binding was 4:1.

Techniques: In Vivo, In Vitro, Injection, Labeling, Immunofluorescence, Staining, Modification

Journal: Materials Today Bio

Article Title: Targeting FN1 to overcome gemcitabine resistance in gallbladder cancer: Mechanistic insights and an iRGD-modified PEG-PLGA nanoparticle delivery strategy

doi: 10.1016/j.mtbio.2026.102877

Figure Lengend Snippet: Impact of NPs delivering si-FN1 on drug resistance and immune cell infiltration in GBC-SD/GEM cells. Note: (A) Schematic of the experimental setup for studying the impact of NPs delivering si-FN1 on GBC GEM resistance; (B-C) RT-qPCR (B) and Western Blot (C) analysis of FN1 and PI3K pathway protein expression in GBC-SD/GEM cells treated with NPs (si-FN1) and iRGD-NPs (si-FN1); (D) CCK-8 assay assessing the viability changes in GBC-SD/GEM cells after treatment with NPs (si-FN1) and iRGD-NPs (si-FN1); (E) Clonogenic assay evaluating colony formation in various groups of GBC-SD/GEM and NOZ/GEM cells; (F) FCM analysis of apoptosis in GBC-SD/GEM cells across different groups; (G) FCM analysis of Tregs levels in CD4 + T cells after co-culture with GBC-SD/GEM cells; (H) FCM analysis of M2 and M1 macrophage levels in THP-1 cells after co-culture with GBC-SD/GEM cells; (I) RT-qPCR analysis of IL-10 or CSF-1 expression in CD4 + T or THP-1 cells co-cultured with GBC-SD/GEM cells. ∗ indicates p < 0.05 compared to the NPs (si-NC) group, # indicates p < 0.05 compared to the NPs (si-FN1) group, experiments repeated three times.

Article Snippet: The NPs (si-FN1) were then conjugated with iRGD peptides (HY-P0122, MCE, USA) through the interaction of the Mal group in Mal–PEG–PLGA with thiol groups in the iRGD peptide for 24 h. The molar ratio of NPs (si-FN1) to iRGD used for binding was 4:1.

Techniques: Quantitative RT-PCR, Western Blot, Expressing, CCK-8 Assay, Clonogenic Assay, Co-Culture Assay, Cell Culture

Journal: Materials Today Bio

Article Title: Targeting FN1 to overcome gemcitabine resistance in gallbladder cancer: Mechanistic insights and an iRGD-modified PEG-PLGA nanoparticle delivery strategy

doi: 10.1016/j.mtbio.2026.102877

Figure Lengend Snippet: Impact of NPs delivering si-FN1 on tumorigenesis and the immunosuppressive environment in GBC-SD/GEM cells. Note: (A) Schematic of the in vivo therapeutic efficacy experiment for iRGD-NPs (si-FN1); (B-C) RT-qPCR (B) and Western Blot (C) analysis of FN1 and PI3K pathway protein expression in xenograft tissues from various mouse groups; (D) Post-dissection images of xenograft tumors from different mouse groups; (E) IVIS monitoring of tumor growth in xenograft mice from weeks 1 to 5; (F) Tumor weight statistics of different mouse groups at week 5; (G-H) Immunohistochemistry and TUNEL staining assessing Ki67 protein expression and apoptosis in tumor tissues from various mouse groups (Scale bars = 50 μm); (I) FCM analysis of Tregs infiltration levels in GBC-SD/GEM cell xenograft tissues from different mouse groups; (J) FCM analysis of M2 and M1 macrophage infiltration levels in GBC-SD/GEM cell xenograft tissues from various mouse groups; (K) RT-qPCR analysis of the expression of immunosuppressive factors in GBC-SD/GEM cell xenograft tissues from different mouse groups. ∗ indicates p < 0.05 compared to the NPs (si-NC) + GEM group, # indicates p < 0.05 compared to the NPs (si-FN1) + GEM group, each group consisting of 6 mice.

Article Snippet: The NPs (si-FN1) were then conjugated with iRGD peptides (HY-P0122, MCE, USA) through the interaction of the Mal group in Mal–PEG–PLGA with thiol groups in the iRGD peptide for 24 h. The molar ratio of NPs (si-FN1) to iRGD used for binding was 4:1.

Techniques: In Vivo, Drug discovery, Quantitative RT-PCR, Western Blot, Expressing, Dissection, Immunohistochemistry, TUNEL Assay, Staining

Journal: Molecular Medicine Reports

Article Title: Prenatal lipopolysaccharide exposure programs cardiac fibrosis via dysregulating of connexin 43 in offspring rats

doi: 10.3892/mmr.2026.13830

Figure Lengend Snippet: BW of offspring rats from 1-day to 16-week-old (A). Heart damages in offspring at the age of 8 and 16 weeks, including the ratios (B) LVW/BW, (C) HW/BW and (D) NT-proBNP level in serum. Concentration of Ang II in (E) left ventricle and (F) serum. Data are presented as mean ± SD. n=10 in each group (A-C) and n=7 in each group (D-F). *P<0.05, **P<0.01 vs Con. BW, body weight; HW, heart weight; LVW, left ventricular weight; NT-proBNP, N-terminal pro-brain natriuretic peptide; Ang II, angiotensin II; Con, control; LPS, lipopolysaccharide.

Article Snippet: Serum concentrations of N-terminal pro-BNP (NT-proBNP; cat. no. E-EL-R3023) and Ang II, along with myocardial tissue levels of Ang II (cat. no. E-EL-R1430c), were quantified using commercial ELISA kits (Elabscience Biotechnology Co., Ltd.) following manufacturer protocols.

Techniques: Concentration Assay, Control

Journal: bioRxiv

Article Title: BLAST: A blue light-assisted secretion toolkit tunable by reversible protein-protein interactions

doi: 10.64898/2026.03.30.715452

Figure Lengend Snippet: Secretion of therapeutic proteins with a-BLAST and d-BLAST. (a) The human preproinsulin (preproINS) construct contains a signal peptide, B-chain (yellow), C-peptide (dark gray), and A-chain (yellow), with engineered Furin cleavage sites flanking the C-peptide for maturation. To facilitate efficient processing within the Golgi apparatus, Furin protease was co-transfected with the BLAST modules. (b) Kinetic profiling of light-induced insulin secretion. Summary graphs of secreted C-peptide levels, quantified by ELISA, as a proxy for insulin secretion from a-BLAST (left) and d-BLAST (right). Both systems exhibited significant, time-dependent insulin release starting from 2 h of illumination (8.2-fold for a-BLAST, 8.4-fold for d-BLAST), reaching maximal induction at 24 h (13.8-fold for a-BLAST, 19.3-fold for d-BLAST). (c) Plasmid configurations for IL-12 secretion. Schematic of the heterodimeric cytokine IL-12-a-BLAST (left) and d-BLAST-IL-12 (right) constructs. (d) Kinetic profiling of light-induced IL-12 secretion. Summary graphs showing IL-12 secretion levels measured by ELISA. Significant secretion was observed starting at 3 h for a-BLAST (2.5-fold) and 2 h for d-BLAST (2.2-fold). At the 24 h time point, d-BLAST (4.7-fold) demonstrated a slightly higher dynamic range compared to a-BLAST (4.5-fold). Open circles represent individual measurements from three biologically independent samples. Data are presented as means ± S.D. Statistical significance was assessed using one-way ANOVA followed by Tukey’s multiple comparisons test (ns = not significant, * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001).

Article Snippet: Secreted human C-peptide levels in the supernatant were quantified using a Human C-peptide ELISA Kit (R&D Systems; Catalog #DICP00).

Techniques: Construct, Transfection, Enzyme-linked Immunosorbent Assay, Plasmid Preparation

Journal: bioRxiv

Article Title: BLAST: A blue light-assisted secretion toolkit tunable by reversible protein-protein interactions

doi: 10.64898/2026.03.30.715452

Figure Lengend Snippet: Secretion of therapeutic proteins with a-BLAST and d-BLAST. (a) The human preproinsulin (preproINS) construct contains a signal peptide, B-chain (yellow), C-peptide (dark gray), and A-chain (yellow), with engineered Furin cleavage sites flanking the C-peptide for maturation. To facilitate efficient processing within the Golgi apparatus, Furin protease was co-transfected with the BLAST modules. (b) Kinetic profiling of light-induced insulin secretion. Summary graphs of secreted C-peptide levels, quantified by ELISA, as a proxy for insulin secretion from a-BLAST (left) and d-BLAST (right). Both systems exhibited significant, time-dependent insulin release starting from 2 h of illumination (8.2-fold for a-BLAST, 8.4-fold for d-BLAST), reaching maximal induction at 24 h (13.8-fold for a-BLAST, 19.3-fold for d-BLAST). (c) Plasmid configurations for IL-12 secretion. Schematic of the heterodimeric cytokine IL-12-a-BLAST (left) and d-BLAST-IL-12 (right) constructs. (d) Kinetic profiling of light-induced IL-12 secretion. Summary graphs showing IL-12 secretion levels measured by ELISA. Significant secretion was observed starting at 3 h for a-BLAST (2.5-fold) and 2 h for d-BLAST (2.2-fold). At the 24 h time point, d-BLAST (4.7-fold) demonstrated a slightly higher dynamic range compared to a-BLAST (4.5-fold). Open circles represent individual measurements from three biologically independent samples. Data are presented as means ± S.D. Statistical significance was assessed using one-way ANOVA followed by Tukey’s multiple comparisons test (ns = not significant, * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001).

Article Snippet: Secreted human C-peptide levels in the supernatant were quantified using a Human C-peptide ELISA Kit (R&D Systems; Catalog #DICP00).

Techniques: Construct, Transfection, Enzyme-linked Immunosorbent Assay, Plasmid Preparation