Journal: Journal of Endocrinology

Article Title: Identification, localization and expression of LPXRFamide peptides, and melatonin-dependent induction of their precursor mRNA in the newt brain

doi: 10.1530/joe-10-0494

Figure Lengend Snippet: Figure 2 HPLC profile of the fGRP-immunoreactive material (IM) (A) and chromatograms of mass spectrometry (MALDI-TOF MS) of native nLPXRFa-1, -2, -3 and-4(B).TheIMloaded ontothe column was eluted withtwo-step gradients ofacetonitrile (20–27%/35 min; 27–47%/65 min) containing 0.1% trifluoroacetic acid at a flow rate of 0.5 ml/min, and fractioned every 2 min for 100 min. Aliquots of each fraction were evaporated to dryness, dissolved in distilled water and spotted onto a nitrocellulose membrane. The immunoreactive fractions which were eluted with 21, 24.5, 25.5 and 38% acetonitrile are indicated by the arrows a, b, c and d, respectively (A). The immunoreactive materials in the extract of newt brain using the antiserum against fGRP showed molecular ion peaks of 1056.31 m/z ([(MCH)]C) (i), 1352.32 m/z ([(MCH)]C) (ii), 1382.33 m/z ([(MCH)]C) (iii) and 1958.05 m/z ([(MCH)]C) (iv) by MALDI-TOF MS (B).

Article Snippet: The eluted fractions were concentrated and subjected to a reversed-phase HPLC column (ODS-80TM; Tosoh, Tokyo, Japan) with two-step gradients of acetonitrile (20–27%/35 min; 27–47%/65 min) containing 0.1% trifluoroacetic acid at a flow rate of 0.5 ml/min, and fractioned every 2 min for 100 min.

Techniques: Mass Spectrometry, Membrane

Journal: Journal of Biological Engineering

Article Title: Streamlined purification of ADDomer nanoparticles for scalable biomanufacturing

doi: 10.1186/s13036-025-00558-0

Figure Lengend Snippet: Sterile filtration optimisation and quality control analysis. ( A ) Coomassie stained SDS-PAGE gel for ADDomer samples from each of the three cassettes filtered through Supor (F1), PES (F2), PVDF (F3), RC (F4) or CA (F5) 0.22 μm units, compared to non-filtered control sample (load; Lo). ( B ) HPLC-SEC analysis of reference ADDomer sample (* , orange line) and ADDomer purified with the optimised process (blue line). ( C ) DLS [diameter (nm) vs. intensity (%)] with three replica readings performed (green, blue and orange lines). ( D ) Uranyl acetate negative-stained TEM micrographs. Scale bar represents 100 nm

Article Snippet: HPLC-SEC analysis was carried out at 0.7 mL/min, in TSKgel size exclusion G5000PWXL HPLC column (Tosoh Bioscience) using a HPLC-system equipped with ultraviolet and photodiode array detector (Vanquish HPLC, Thermo Fisher Scientific, USA).

Techniques: Sterility, Filtration, Control, Staining, SDS Page, Purification

Journal: ACS Infectious Diseases

Article Title: Switching Bond: Generation of New Antimicrobial Peptides via the Incorporation of an Intramolecular Isopeptide Bond

doi: 10.1021/acsinfecdis.1c00037

Figure Lengend Snippet: Resistance of peptides to trypsin digestion. Percentages intact of Amp1L, Amp1EP, MSI-78, and MSIEP peptides were determined by reversed-phase HPLC comparative to the peak areas acquired at t 0 (control at 0 min set to 100% for each peak).

Article Snippet: The supernatant (50 μL) was injected onto a reversed-phase HPLC (C 18 reverse phase, Bio-Rad analytical column, 250 × 4 mm, 300 Å pore size, 7 μm particle size).

Techniques: Control

Journal: ACS Infectious Diseases

Article Title: Switching Bond: Generation of New Antimicrobial Peptides via the Incorporation of an Intramolecular Isopeptide Bond

doi: 10.1021/acsinfecdis.1c00037

Figure Lengend Snippet: Amount of % Remaining Amp1L, Amp1EP, MSI-78, and MSIEP Peptides Assessed by RP-HPLC after Incubation with 20% (v/v) Human Plasma at Different Time Points

Article Snippet: The supernatant (50 μL) was injected onto a reversed-phase HPLC (C 18 reverse phase, Bio-Rad analytical column, 250 × 4 mm, 300 Å pore size, 7 μm particle size).

Techniques: Incubation, Clinical Proteomics