A Matrix-Assisted Laser Desorption/Ionization Compatible Reagent for Tagging Tryptophan Residues

Li, Chunyan; Gawandi, Vijay; Protos, Adam N.; Phillips, Robert S.; Amster, I. Jonathan

doi:10.1255/ejms.814

Cited by 5 publications

(4 citation statements)

References 23 publications

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“…Compounds like 2-nitro-and 2,4-dinitrophenylsulfenylchloride reacting at the 2-position of the indole group can be used for studying active sites of enzymes (13). Applications in the field of proteomics, including relative quantification studies employing stable isotope-labeled analogues, were reported (14)(15)(16); N-bromosuccinimide is a derivatizing reagent used for similar applications (17). Another method, selectively targeting the indole nitrogen, uses rhodium carbenoids for the derivatization of tryptophan residues in proteins as recently reported by Antos et al (18).…”

Section: Introductionmentioning

confidence: 99%

Reaction of the Indole Group with Malondialdehyde: Application for the Derivatization of Tryptophan Residues in Peptides

et al. 2007

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A method for the selective modification of tryptophan residues based on the reaction of malondialdehyde with the indole nitrogen of the tryptophan side chain at acidic conditions is presented. The condensation reaction is quantitative and leads to a substituted acrolein moiety with a remaining reactive aldehyde group. As is shown, this group can be further converted to a hydrazone using hydrazide compounds, but if hydrazine or phenylhydrazine are used, release of the free indole group is observed upon cleavage of the substitution. Alternatively, secondary amines such as pyrrolidine may also act as cleavage reagents. This general reaction scheme has been adapted and optimized for the derivatization of tryptophan-containing peptides and small N-heterocyclic compounds. It serves as the basis of a reversible tagging scheme for Trp-peptides or molecules of interest carrying indole structures as it allows the specific attachment and removal of a reactive group that may be used for a variety of purposes such as affinity tagging.

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Section: Introductionmentioning

confidence: 99%

Reaction of the Indole Group with Malondialdehyde: Application for the Derivatization of Tryptophan Residues in Peptides

et al. 2007

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“…In addition, 3D cultures are less costly and labor-intensive than animal studies and should be prioritized at a preliminary stage. Experimental data show that the pattern of gene expression, mRNA splicing, intracellular signaling, cytoskeletal organization and secretion profile of cells grown in 3D cultures more closely resemble what is observed in vivo than when grown in two-dimensional (2D) cultures 84-88 .…”

Section: Challenges and Perspectives For The P19arf + Ifn{\tf="greek_mentioning

confidence: 82%

Perspectives for cancer immunotherapy mediated by p19Arf plus interferon-beta gene transfer

Strauss¹,

Silva²,

Vieira³

et al. 2018

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While cancer immunotherapy has gained much deserved attention in recent years, many areas regarding the optimization of such modalities remain unexplored, including the development of novel approaches and the strategic combination of therapies that target multiple aspects of the cancer-immunity cycle. Our own work involves the use of gene transfer technology to promote cell death and immune stimulation. Such immunogenic cell death, mediated by the combined transfer of the alternate reading frame (p14ARF in humans and p19Arf in mice) and the interferon-β cDNA in our case, was shown to promote an antitumor immune response in mouse models of melanoma and lung carcinoma. With these encouraging results, we are now setting out on the road toward translational and preclinical development of our novel immunotherapeutic approach. Here, we outline the perspectives and challenges that we face, including the use of human tumor and immune cells to verify the response seen in mouse models and the incorporation of clinically relevant models, such as patient-derived xenografts and spontaneous tumors in animals. In addition, we seek to combine our immunotherapeutic approach with other treatments, such as chemotherapy or checkpoint blockade, with the goal of reducing dosage and increasing efficacy. The success of any translational research requires the cooperation of a multidisciplinary team of professionals involved in laboratory and clinical research, a relationship that is fostered at the Cancer Institute of Sao Paulo.

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“…[25][26] 2-(Trifluoromethyl)benzenesulfenyl chloride as an alternative tagging reagent has been introduced by Amster and coworkers. 27 Several other (more or less) selective tryptophan modification agents are known, like N-bromosuccinimide, 28 2-hydroxy-5-nitrobenzyl bromide, 29 or rhodium carbenoids, 30 but they have not been applied to proteomic samples. A kit for the enrichment of tryptophan containing peptides has been made commercially available, 31 but to our knowledge, no application has been described in the literature.…”

Section: Introductionmentioning

confidence: 99%

“…To isolate the tagged peptides, the increased hydrophobicity upon modification of tryptophan residues was utilized. Recently, an improved enrichment strategy using a phenyl column and the application to biological samples have been described. − 2-(Trifluoromethyl)benzenesulfenyl chloride as an alternative tagging reagent has been introduced by Amster and co-workers . Several other (more or less) selective tryptophan modification agents are known, like N -bromosuccinimide, 2-hydroxy-5-nitrobenzyl bromide, or rhodium carbenoids, but they have not been applied to proteomic samples.…”

Section: Introductionmentioning

confidence: 99%

Selective Enrichment of Tryptophan-Containing Peptides from Protein Digests Employing a Reversible Derivatization with Malondialdehyde and Solid-Phase Capture on Hydrazide Beads

2007

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A method for the selective enrichment of tryptophan-containing peptides from complex peptide mixtures such as protein digests is presented. It is based on the reversible reaction of tryptophan with malondialdehyde and trapping of the derivatized Trp-peptides on hydrazide beads via the free aldehyde group of the modified peptides. The peptides are subsequently recovered in their native form by specific cleavage reactions for further (mass spectrometric) analysis. The method was optimized and evaluated using a tryptic digest of a mixture of 10 model proteins, demonstrating a significant reduction in sample complexity while still allowing the identification of all proteins. The applicability of the tryptophan-specific enrichment procedure to complex biological samples is demonstrated for a total yeast cell lysate. Analysis of the processed fraction by 1D-LC-MS/MS confirms the specificity of the enrichment procedure, as more than 85% of the peptides recovered from the enrichment step contained tryptophan. The reduction in sample complexity also resulted in the identification of additional proteins in comparison to the untreated lysate.

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A Matrix-Assisted Laser Desorption/Ionization Compatible Reagent for Tagging Tryptophan Residues

Cited by 5 publications

References 23 publications

Reaction of the Indole Group with Malondialdehyde: Application for the Derivatization of Tryptophan Residues in Peptides

Reaction of the Indole Group with Malondialdehyde: Application for the Derivatization of Tryptophan Residues in Peptides

Perspectives for cancer immunotherapy mediated by p19Arf plus interferon-beta gene transfer

Selective Enrichment of Tryptophan-Containing Peptides from Protein Digests Employing a Reversible Derivatization with Malondialdehyde and Solid-Phase Capture on Hydrazide Beads

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