Fluorescent isotope‐coded affinity tag 2: Peptide labeling and affinity capture

Rivera‐Monroy, Zuly Jenny; Bonn, Guenther K.; Guttman, András

doi:10.1002/elps.200800830

Cited by 10 publications

(3 citation statements)

References 29 publications

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“…12 The purity and efficiency of rhodamine labeling were investigated via high-performance liquid chromatography by monitoring the absorbance at 230 nm and fluorescence at 560 nm.…”

mentioning

confidence: 99%

Identification of a cell-penetrating peptide domain from human beta-defensin 3 and characterization of its anti-inflammatory activity

Lee¹,

Suh²,

Kim³

et al. 2015

IJN

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Human beta-defensins (hBDs) are crucial factors of intrinsic immunity that function in the immunologic response to a variety of invading enveloped viruses, bacteria, and fungi. hBDs can cause membrane depolarization and cell lysis due to their highly cationic nature. These molecules participate in antimicrobial defenses and the control of adaptive and innate immunity in every mammalian species and are produced by various cell types. The C-terminal 15-mer peptide within hBD3, designated as hBD3-3, was selected for study due to its cell- and skin-penetrating activity, which can induce anti-inflammatory activity in lipopolysaccharide-treated RAW 264.7 macrophages. hBD3-3 penetrated both the outer membrane of the cells and mouse skin within a short treatment period. Two other peptide fragments showed poorer penetration activity compared to hBD3-3. hBD3-3 inhibited the lipopolysaccharide-induced production of inducible nitric oxide synthase, nitric oxide, and secretory cytokines, such as interleukin-6 and tumor necrosis factor in a concentration-dependent manner. Moreover, hBD3-3 reduced the interstitial infiltration of polymorphonuclear leukocytes in a lung inflammation model. Further investigation also revealed that hBD3-3 downregulated nuclear factor kappa B-dependent inflammation by directly suppressing the degradation of phosphorylated-IκBα and by downregulating active nuclear factor kappa B p65. Our findings indicate that hBD3-3 may be conjugated with drugs of interest to ensure their proper translocation to sites, such as the cytoplasm or nucleus, as hBD3-3 has the ability to be used as a carrier, and suggest a potential approach to effectively treat inflammatory diseases.

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“…12 The purity and efficiency of rhodamine labeling were investigated via high-performance liquid chromatography by monitoring the absorbance at 230 nm and fluorescence at 560 nm.…”

mentioning

confidence: 99%

Identification of a cell-penetrating peptide domain from human beta-defensin 3 and characterization of its anti-inflammatory activity

Lee¹,

Suh²,

Kim³

et al. 2015

IJN

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“…The Michael addition reaction between the thiol group (cysteine) and the maleimido group (click chemistry) is frequently used to label proteins; 22 however, this reaction has been little used to functionalize porous polymeric materials. 23 Therefore, it was decided to first study the reaction in solution, in order to determine the optimal experimental conditions for the reaction over the monolith's surface.…”

Section: Resultsmentioning

confidence: 99%

Obtaining an immunoaffinity monolithic material: poly(GMA-co-EDMA) functionalized with an HPV-derived peptide using a thiol–maleimide reaction

et al. 2021

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“…AGP has four cysteine residues forming two disulfide bonds (www.uniprot.org/uniprot/P02763). Reduction of these bonds has been accomplished using TCEP, a mild reducing agent not frequently used in proteomics []. Since TCEP does not possess a thiol group, generally it does not need to be eliminated from the reaction mixture prior to the derivatization reaction.…”

Section: Resultsmentioning

confidence: 99%

Analysis of alpha‐1‐acid glycoprotein isoforms using CE‐LIF with fluorescent thiol derivatization

et al. 2012

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The analysis of glycoprotein isoforms is of high interest in the biomedical field and clinical chemistry. Many studies have demonstrated that some glycoprotein isoforms could serve as biomarkers for several major diseases, such as cancers and vascular diseases, among others. Capillary zone electrophoresis (CZE) is a well‐established technique to separate glycoprotein isoforms, however, it suffers from limited sensitivity when UV‐Vis detection is used. On the other hand, with laser‐induced fluorescence (LIF) detection, derivatization reaction to render the proteins fluorescent can destroy the resolution of the isoforms. In this work, a derivatization procedure through the thiol groups of glycoproteins using either 5‐(iodoacetamide) fluorescein (5‐IAF) or BODIPY iodoacetamide is presented with the model protein of alpha‐1‐acid glycoprotein (AGP). The derivatization process presented enabled high‐resolution analysis of AGP isoforms by CZE‐LIF. The derivatization procedure was successfully applied to label AGP from samples of serum and secretome of artery tissue, enabling the separation of the AGP isoforms by CE‐LIF in natural samples at different concentration levels.

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Fluorescent isotope‐coded affinity tag 2: Peptide labeling and affinity capture

Cited by 10 publications

References 29 publications

Identification of a cell-penetrating peptide domain from human beta-defensin 3 and characterization of its anti-inflammatory activity

Identification of a cell-penetrating peptide domain from human beta-defensin 3 and characterization of its anti-inflammatory activity

Obtaining an immunoaffinity monolithic material: poly(GMA-co-EDMA) functionalized with an HPV-derived peptide using a thiol–maleimide reaction

Analysis of alpha‐1‐acid glycoprotein isoforms using CE‐LIF with fluorescent thiol derivatization

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