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Amino Groups

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Robert Scott Prosser – One of the best experts on this subject based on the ideXlab platform.

  • site specific labeling of protein lysine residues and n terminal Amino Groups with indoles and indole derivatives
    Bioconjugate Chemistry, 2015
    Co-Authors: Sacha Thierry Larda, Dmitry Pichugin, Robert Scott Prosser

    Abstract:

    Indoles and indole-derivatives can be used to site-specifically label proteins on lysine and N-terminal Amino Groups under mild, nondenaturing reaction conditions. Hen egg white lysozyme (HEWL) and α-lactalbumin were labeled with indole, fluoroindole, or fluoroindole-2-carboxylate via electrophilic aromatic substitutions to lysine side chain Ne- and N-terminal Amino imines, formed in situ in the presence of formaldehyde. The reaction is highly site-selective, easily controlled by temperature, and does not eliminate the native charge of the protein, unlike many other common lysine-specific labeling strategies. 19F NMR was used to monitor reaction progression, and in the case of HEWL, unique resonances for each labeled side chain could be resolved. We demonstrate that the indole tags are highly selective for primary Amino Groups. 19F NMR demonstrates that each lysine exhibits a different rate of conjugation to indoles making it possible to employ these tags as a means of probing surface topology by NMR or m…

Wolfgang E. S. Unger – One of the best experts on this subject based on the ideXlab platform.

  • determination of accessible Amino Groups on surfaces by chemical derivatization with 3 5 bis trifluoromethyl phenyl isothiocyanate and xps nexafs analysis
    Analytical and Bioanalytical Chemistry, 2010
    Co-Authors: Nora Graf, Andreas Lippitz, Thomas Gross, Falko Pippig, Andreas Hollander, Wolfgang E. S. Unger

    Abstract:

    The determination of Amino Groups on surfaces capable of binding biomolecules is important for the understanding and optimization of technologically relevant coupling processes. In this study, three different types of Amino-functionalized model surfaces, Amino thiolate on Au, Amino siloxane on Si, and polyethylene (PE) foils and films reacted with 1,2-diAminoethane (DAE) were derivatized with 3,5-bis(trifluoromethyl)phenyl isothiocyanate. Subsequently, these samples were analyzed by chemical derivatization X-ray photoelectron spectroscopy (CD-XPS) and near-edge X-ray absorption fine structure spectroscopy (NEXAFS). The determination of Amino Groups by this analytical approach allows gaining insight into the availability of Groups on surfaces that can actually serve as attachment sites for biomolecules in technical applications. In the case of the Amino thiolate on Au, almost 90% of the expected Amino Groups were detected by CD-XPS. Investigation of the Amino siloxane films revealed lower yields for the derivatization reaction in the order of 30%. The lowered reaction yields are thought to be due to interactions between the Amino siloxane’s Amino and silanol Groups or the underlying substrate, making them inaccessible to the derivatization agent. The aminated PE samples are characterized by a complex surface chemistry and structure, and reaction yields of the derivatization reaction cannot be unequivocally derived. However, 1–3% of the total carbon atoms in the surface layer were found to be bound to Amino Groups accessible to the derivatization agent. It can be concluded that, depending on the detailed character of the investigated Amino-terminated surface, the amount of Amino Groups accessible to CD-XPS can be substantially lower than the total amount of Amino Groups present at the surface.

  • Determination of accessible Amino Groups on surfaces by chemical derivatization with 3,5-bis(trifluoromethyl)phenyl isothiocyanate and XPS/NEXAFS analysis
    Analytical and Bioanalytical Chemistry, 2009
    Co-Authors: Nora Graf, Andreas Lippitz, Thomas Gross, Falko Pippig, Andreas Hollander, Wolfgang E. S. Unger

    Abstract:

    The determination of Amino Groups on surfaces capable of binding biomolecules is important for the understanding and optimization of technologically relevant coupling processes. In this study, three different types of Amino-functionalized model surfaces, Amino thiolate on Au, Amino siloxane on Si, and polyethylene (PE) foils and films reacted with 1,2-diAminoethane (DAE) were derivatized with 3,5-bis(trifluoromethyl)phenyl isothiocyanate. Subsequently, these samples were analyzed by chemical derivatization X-ray photoelectron spectroscopy (CD-XPS) and near-edge X-ray absorption fine structure spectroscopy (NEXAFS). The determination of Amino Groups by this analytical approach allows gaining insight into the availability of Groups on surfaces that can actually serve as attachment sites for biomolecules in technical applications. In the case of the Amino thiolate on Au, almost 90% of the expected Amino Groups were detected by CD-XPS. Investigation of the Amino siloxane films revealed lower yields for the derivatization reaction in the order of 30%. The lowered reaction yields are thought to be due to interactions between the Amino siloxane’s Amino and silanol Groups or the underlying substrate, making them inaccessible to the derivatization agent. The aminated PE samples are characterized by a complex surface chemistry and structure, and reaction yields of the derivatization reaction cannot be unequivocally derived. However, 1–3% of the total carbon atoms in the surface layer were found to be bound to Amino Groups accessible to the derivatization agent. It can be concluded that, depending on the detailed character of the investigated Amino-terminated surface, the amount of Amino Groups accessible to CD-XPS can be substantially lower than the total amount of Amino Groups present at the surface.

Sacha Thierry Larda – One of the best experts on this subject based on the ideXlab platform.

  • site specific labeling of protein lysine residues and n terminal Amino Groups with indoles and indole derivatives
    Bioconjugate Chemistry, 2015
    Co-Authors: Sacha Thierry Larda, Dmitry Pichugin, Robert Scott Prosser

    Abstract:

    Indoles and indole-derivatives can be used to site-specifically label proteins on lysine and N-terminal Amino Groups under mild, nondenaturing reaction conditions. Hen egg white lysozyme (HEWL) and α-lactalbumin were labeled with indole, fluoroindole, or fluoroindole-2-carboxylate via electrophilic aromatic substitutions to lysine side chain Ne- and N-terminal Amino imines, formed in situ in the presence of formaldehyde. The reaction is highly site-selective, easily controlled by temperature, and does not eliminate the native charge of the protein, unlike many other common lysine-specific labeling strategies. 19F NMR was used to monitor reaction progression, and in the case of HEWL, unique resonances for each labeled side chain could be resolved. We demonstrate that the indole tags are highly selective for primary Amino Groups. 19F NMR demonstrates that each lysine exhibits a different rate of conjugation to indoles making it possible to employ these tags as a means of probing surface topology by NMR or m…