The Experts below are selected from a list of 207 Experts worldwide ranked by ideXlab platform
Thomas Reinard - One of the best experts on this subject based on the ideXlab platform.
-
Production of a single-chain variable fragment antibody against fumonisin B1.
Journal of Agricultural and Food Chemistry, 2005Co-Authors: Björn Lauer, Ilka Ottleben, Hans-jörg Jacobsen, Thomas ReinardAbstract:The selection of synthetic antibody fragments from large phage libraries has become a common method for the generation of specific antibodies. The technique is particularly valuable when antibodies against small, non-immunogenic molecules (Haptens) or highly toxic substances have to be produced. In addition, Haptens are usually coupled to protein carriers, bearing the risk that the free Hapten is not detectable. Here, a single variable chain antibody (scFv) against the highly toxic mycotoxin fumonisin B1 has been produced. The Hapten was coupled via a linker to biotin. Using this conjugate and a naive scFv library, it was possible to circumvent both the necessity of immunization and the risk of a disguised Hapten. The scFv obtained after three panning rounds was found to bind specifically to both free fumonisin B1 and fumonisin−biotin conjugate. Also fumonisin B2 was bound by the scFv. Modeling of both scFv and fumonisin B1 molecule revealed a good fitting of structures. The antibody obtained can potentia...
-
Production of a single-chain variable fragment antibody against fumonisin B1
Journal of Agricultural and Food Chemistry, 2005Co-Authors: Björn Lauer, Ilka Ottleben, Hans-jörg Jacobsen, Thomas ReinardAbstract:The selection of synthetic antibody fragments from large phage libraries has become a common method for the generation of specific antibodies. The technique is particularly valuable when antibodies against small, non-immunogenic molecules (Haptens) or highly toxic substances have to be produced. In addition, Haptens are usually coupled to protein carriers, bearing the risk that the free Hapten is not detectable. Here, a single variable chain antibody (scFv) against the highly toxic mycotoxin fumonisin B1 has been produced. The Hapten was coupled via a linker to biotin. Using this conjugate and a naive scFv library, it was possible to circumvent both the necessity of immunization and the risk of a disguised Hapten. The scFv obtained after three panning rounds was found to bind specifically to both free fumonisin B1 and fumonisin-biotin conjugate. Also fumonisin B2 was bound by the scFv. Modeling of both scFv and fumonisin B1 molecule revealed a good fitting of structures. The antibody obtained can potentially be used for developing a rapid and affordable immunoassay for detection of food contamination and can be applied in immunoaffinity chromatography, usually carried out prior to HPLC analysis of mycotoxin-contaminated food and feed.
Björn Lauer - One of the best experts on this subject based on the ideXlab platform.
-
Production of a single-chain variable fragment antibody against fumonisin B1.
Journal of Agricultural and Food Chemistry, 2005Co-Authors: Björn Lauer, Ilka Ottleben, Hans-jörg Jacobsen, Thomas ReinardAbstract:The selection of synthetic antibody fragments from large phage libraries has become a common method for the generation of specific antibodies. The technique is particularly valuable when antibodies against small, non-immunogenic molecules (Haptens) or highly toxic substances have to be produced. In addition, Haptens are usually coupled to protein carriers, bearing the risk that the free Hapten is not detectable. Here, a single variable chain antibody (scFv) against the highly toxic mycotoxin fumonisin B1 has been produced. The Hapten was coupled via a linker to biotin. Using this conjugate and a naive scFv library, it was possible to circumvent both the necessity of immunization and the risk of a disguised Hapten. The scFv obtained after three panning rounds was found to bind specifically to both free fumonisin B1 and fumonisin−biotin conjugate. Also fumonisin B2 was bound by the scFv. Modeling of both scFv and fumonisin B1 molecule revealed a good fitting of structures. The antibody obtained can potentia...
-
Production of a single-chain variable fragment antibody against fumonisin B1
Journal of Agricultural and Food Chemistry, 2005Co-Authors: Björn Lauer, Ilka Ottleben, Hans-jörg Jacobsen, Thomas ReinardAbstract:The selection of synthetic antibody fragments from large phage libraries has become a common method for the generation of specific antibodies. The technique is particularly valuable when antibodies against small, non-immunogenic molecules (Haptens) or highly toxic substances have to be produced. In addition, Haptens are usually coupled to protein carriers, bearing the risk that the free Hapten is not detectable. Here, a single variable chain antibody (scFv) against the highly toxic mycotoxin fumonisin B1 has been produced. The Hapten was coupled via a linker to biotin. Using this conjugate and a naive scFv library, it was possible to circumvent both the necessity of immunization and the risk of a disguised Hapten. The scFv obtained after three panning rounds was found to bind specifically to both free fumonisin B1 and fumonisin-biotin conjugate. Also fumonisin B2 was bound by the scFv. Modeling of both scFv and fumonisin B1 molecule revealed a good fitting of structures. The antibody obtained can potentially be used for developing a rapid and affordable immunoassay for detection of food contamination and can be applied in immunoaffinity chromatography, usually carried out prior to HPLC analysis of mycotoxin-contaminated food and feed.
Hans-jörg Jacobsen - One of the best experts on this subject based on the ideXlab platform.
-
Production of a single-chain variable fragment antibody against fumonisin B1.
Journal of Agricultural and Food Chemistry, 2005Co-Authors: Björn Lauer, Ilka Ottleben, Hans-jörg Jacobsen, Thomas ReinardAbstract:The selection of synthetic antibody fragments from large phage libraries has become a common method for the generation of specific antibodies. The technique is particularly valuable when antibodies against small, non-immunogenic molecules (Haptens) or highly toxic substances have to be produced. In addition, Haptens are usually coupled to protein carriers, bearing the risk that the free Hapten is not detectable. Here, a single variable chain antibody (scFv) against the highly toxic mycotoxin fumonisin B1 has been produced. The Hapten was coupled via a linker to biotin. Using this conjugate and a naive scFv library, it was possible to circumvent both the necessity of immunization and the risk of a disguised Hapten. The scFv obtained after three panning rounds was found to bind specifically to both free fumonisin B1 and fumonisin−biotin conjugate. Also fumonisin B2 was bound by the scFv. Modeling of both scFv and fumonisin B1 molecule revealed a good fitting of structures. The antibody obtained can potentia...
-
Production of a single-chain variable fragment antibody against fumonisin B1
Journal of Agricultural and Food Chemistry, 2005Co-Authors: Björn Lauer, Ilka Ottleben, Hans-jörg Jacobsen, Thomas ReinardAbstract:The selection of synthetic antibody fragments from large phage libraries has become a common method for the generation of specific antibodies. The technique is particularly valuable when antibodies against small, non-immunogenic molecules (Haptens) or highly toxic substances have to be produced. In addition, Haptens are usually coupled to protein carriers, bearing the risk that the free Hapten is not detectable. Here, a single variable chain antibody (scFv) against the highly toxic mycotoxin fumonisin B1 has been produced. The Hapten was coupled via a linker to biotin. Using this conjugate and a naive scFv library, it was possible to circumvent both the necessity of immunization and the risk of a disguised Hapten. The scFv obtained after three panning rounds was found to bind specifically to both free fumonisin B1 and fumonisin-biotin conjugate. Also fumonisin B2 was bound by the scFv. Modeling of both scFv and fumonisin B1 molecule revealed a good fitting of structures. The antibody obtained can potentially be used for developing a rapid and affordable immunoassay for detection of food contamination and can be applied in immunoaffinity chromatography, usually carried out prior to HPLC analysis of mycotoxin-contaminated food and feed.
Ilka Ottleben - One of the best experts on this subject based on the ideXlab platform.
-
Production of a single-chain variable fragment antibody against fumonisin B1.
Journal of Agricultural and Food Chemistry, 2005Co-Authors: Björn Lauer, Ilka Ottleben, Hans-jörg Jacobsen, Thomas ReinardAbstract:The selection of synthetic antibody fragments from large phage libraries has become a common method for the generation of specific antibodies. The technique is particularly valuable when antibodies against small, non-immunogenic molecules (Haptens) or highly toxic substances have to be produced. In addition, Haptens are usually coupled to protein carriers, bearing the risk that the free Hapten is not detectable. Here, a single variable chain antibody (scFv) against the highly toxic mycotoxin fumonisin B1 has been produced. The Hapten was coupled via a linker to biotin. Using this conjugate and a naive scFv library, it was possible to circumvent both the necessity of immunization and the risk of a disguised Hapten. The scFv obtained after three panning rounds was found to bind specifically to both free fumonisin B1 and fumonisin−biotin conjugate. Also fumonisin B2 was bound by the scFv. Modeling of both scFv and fumonisin B1 molecule revealed a good fitting of structures. The antibody obtained can potentia...
-
Production of a single-chain variable fragment antibody against fumonisin B1
Journal of Agricultural and Food Chemistry, 2005Co-Authors: Björn Lauer, Ilka Ottleben, Hans-jörg Jacobsen, Thomas ReinardAbstract:The selection of synthetic antibody fragments from large phage libraries has become a common method for the generation of specific antibodies. The technique is particularly valuable when antibodies against small, non-immunogenic molecules (Haptens) or highly toxic substances have to be produced. In addition, Haptens are usually coupled to protein carriers, bearing the risk that the free Hapten is not detectable. Here, a single variable chain antibody (scFv) against the highly toxic mycotoxin fumonisin B1 has been produced. The Hapten was coupled via a linker to biotin. Using this conjugate and a naive scFv library, it was possible to circumvent both the necessity of immunization and the risk of a disguised Hapten. The scFv obtained after three panning rounds was found to bind specifically to both free fumonisin B1 and fumonisin-biotin conjugate. Also fumonisin B2 was bound by the scFv. Modeling of both scFv and fumonisin B1 molecule revealed a good fitting of structures. The antibody obtained can potentially be used for developing a rapid and affordable immunoassay for detection of food contamination and can be applied in immunoaffinity chromatography, usually carried out prior to HPLC analysis of mycotoxin-contaminated food and feed.
Kim D Janda - One of the best experts on this subject based on the ideXlab platform.
-
Probing the effects of Hapten stability on cocaine vaccine immunogenicity.
Molecular pharmaceutics, 2013Co-Authors: Xiaoqing Cai, Timothy W. Whitfield, Amira Y. Moreno, Yanabel Grant, Mark S. Hixon, George F. Koob, Kim D JandaAbstract:Judicious Hapten design has been shown to be of importance when trying to generate a viable vaccine against a drug of abuse. Hapten design has typically been predicated upon faithfully emulating the unique chemical architecture that each drug presents. However, the need for drug–Hapten congruency may also compromise vaccine immunogenicity if the drug–Hapten conjugate possesses chemical epitope instability. There has been no systematic study on the impact of Hapten stability as it relates to vaccine immunogenicity. As a starting point, we have probed the stability of a series of cocaine Haptens through varying several of its structural elements, including functionality at the C2-position, the nature of the linker, and its site of attachment. Accordingly, a hydrolytic stability profile of four cocaine Haptens (GNNA, GNNS, GNE, and GNC) was produced, and these results were compared through each Hapten’s immunological properties, which were generated via active vaccination. From this group of four, three of t...
-
liposomes containing monophosphoryl lipid a a potent adjuvant system for inducing antibodies to heroin Hapten analogs
Vaccine, 2013Co-Authors: Gary R. Matyas, Kenner C. Rice, Malliga R. Iyer, Arthur E. Jacobson, Alexander V Mayorov, Kejun Cheng, Zoltan Beck, Kim D JandaAbstract:In order to create an effective immunization approach for a potential vaccine to heroin, liposomes containing monophosphoryl lipid A [L(MPLA)] were tested as an adjuvant system to induce antibodies to heroin Hapten analogs. Four synthetic Haptens and two immunization strategies were employed. In the first strategy, a hydrophobic 23 amino acid immunogenic peptide derived from the membrane proximal external region of gp41 from HIV-1 envelope protein was embedded as a carrier in the outer surface of L(MPLA), to which was conjugated a 15 amino acid universal T cell epitope and a terminal heroin Hapten analog. In the second strategy, tetanus toxoid (TT) carrier protein was decorated with Haptens by conjugation, and the Hapten-conjugated protein was mixed with L(MPLA). After immunization of mice, each of the immunization strategies was effective for induction of IgG anti-Hapten antibodies. The first immunization strategy induced a mean end-point IgG titer against one of two Haptens tested of approximately 12,800; however, no detectable antibodies were induced against the liposome-associated HIV-1 carrier peptide. In the second immunization strategy, depending on the Hapten used for decorating the TT, end-point IgG titers ranged from 100,000 to 6,500,000. In this strategy, in which Hapten was conjugated to the TT, end-point IgG titers of 400,000 to the TT carrier were observed with each conjugate. However, upon mixing unconjugated TT with L(MPLA), anti-TT titers of 6,500,000 were observed. We conclude that L(MPLA) serves as a potent adjuvant for inducing antibodies to candidate heroin Haptens. However, antibodies to the carrier peptide or protein were partly or completed inhibited by the presence of conjugated Hapten.
-
modulating cocaine vaccine potency through Hapten fluorination
Journal of the American Chemical Society, 2013Co-Authors: Xiaoqing Cai, Kyoji Tsuchikama, Kim D JandaAbstract:Cocaine addiction is a long-lasting relapsing illness characterized by cycles of abuse, abstinence, and reinstatement, and antibody-based therapies could be a powerful therapeutic approach. Herein, we explored the possibility of using halogenated cocaine Haptens to enhance the immunological properties of anti-cocaine vaccines. Three fluorine-containing cocaine Haptens (GNF, GNCF and GN5F) and one chlorine-containing cocaine Hapten (GNCl) were designed and synthesized, based upon the chemical scaffold of the only Hapten that has reached clinical trials, succinyl norcocaine (SNC). Hapten GNF was found to retain potent cocaine affinity, and also elicit antibodies in a higher concentration than the parent structure SNC. Our data suggests that not only could strategic Hapten fluorination be useful for improving upon the current cocaine vaccine undergoing clinical trials, but it may also be a valuable new approach, with application to any of the vaccines being developed for the treatment of drugs of abuse.
