A method of improving specific immune responses to small immunogens, haptens, has been developed by changing the linkage between the hapten and carrier being used for immunization. High affinity antibodies to the hapten cotinine have been produced using this method. Antibodies to a glycated protein have also been developed, utilizing an immunogen which is composed of a glycated peptide mimic of the glycated peptide sequence which is the target epitope, wherein the peptide mimic is constructed to conformationally mimic the conformation of the peptide in the native protein, the peptide mimic contains no charged groups or other immunodominant group, and the peptide mimic is connected to a spacer sequence equivalent to a peptide spacer of between one and thirty amino acids in length, which serves to position the peptide epitope in a conformation that approximates its conformation in the native protein. In a further embodiment the peptide mimic and spacer are linked to a carrier molecule.
Antibody To And Assay For Peptide Linked-Pyridinoline As Indicator Of Bone Resorption Level
Judith Fitzpatrick - Tenafly NJ Regina Lenda - Wesley Hills NY Zijian Zeng - Warren NJ
Assignee:
Serex, Inc. - Maywood NJ
International Classification:
C07D21172
US Classification:
546345
Abstract:
A monoclonal antibody, Serex A93, recognizes peptide linked pyridinoline in Type I bone collagen fragments and can be used to quantitate bone resorption. The hybridoma producing this antibody has been deposited with the American Type Culture Collection, Rockville, Md. , under accession number HB-12254. The epitope reactive with the antibody is stable to acid hydrolysis and therefore is not a linear peptide. The antibody recognizes pyridinoline in bound or conjugated form, but not in the free form found in urine. The antibody is useful in immunoassays for determining bone resorption, utilizing body fluids such as urine, saliva, blood, or sweat.
Method And Device For Detection Of Apo A, Apo B And The Ratio Thereof In Saliva
A method has been developed to detect the levels of apolipoproteins A-1 and B in saliva, which is correlated with the levels of HDL and LDL in serum, respectively. In unstimulated saliva, the ration of Apo A to Apo B is correlated with the ration of HDL to LDL in serum. Albumin can be used to normalize the sample for dilution. The high degree of correlation in combination with a simple, quick test that can be performed at the site of collection provides a cost effective, patient friendly means to monitor an individuals risk of heart disease. In the preferred embodiment, saliva production is stimulated by means such as breath mint or tart solution (such as lemon) and the effect of dilution controlled by reference to albumin.
Methods To Improve Immunogenicity Of Antigens And Specificity Of Antibodies
Judith Fitzpatrick - Englewood NJ, US Regina Lenda - Wesley Hills NY, US
Assignee:
Serex, Inc. - Maywood NJ
International Classification:
A61K 39/00 G01N 33/66 G01N 33/68 G01N 33/72
US Classification:
4241851, 4241841, 435 71
Abstract:
A method of improving specific immune responses to small immunogens, haptens, has been developed by changing the linkage between the hapten and carrier being used for immunization. High affinity antibodies to the hapten cotinine have been produced using this method. Antibodies to a glycated protein have also been developed, utilizing an immunogen which is composed of a glycated peptide mimic of the glycated peptide sequence which is the target epitope, wherein the peptide mimic is constructed to conformationally mimic the conformation of the peptide in the native protein, the peptide mimic contains no charged groups or other immunodominant group, and the peptide mimic is connected to a spacer sequence equivalent to a peptide spacer of between one and thirty amino acids in length, which serves to position the peptide epitope in a conformation that approximates its conformation in the native protein. In a further embodiment the peptide mimic and spacer are linked to a carrier molecule.
Judith Fitzpatrick - Englewood NJ, US Paul Averback - St. Laurent, CA Maggie Focht - Glen Rock NJ, US Riza Bibiano - Old Bridge NJ, US
Assignee:
Nymox Pharmaceutical Corporation - Quebec
International Classification:
C07K 14/435 C07K 5/04
US Classification:
530300, 530330
Abstract:
The invention is directed to preferred repeat sequences of Neural Thread Protein (NTP), peptides, mimetics, antibodies, and nucleic acids of the preferred sequences, and diagnostic and therapeutic methods of using such preferred NTP sequences.
Methods To Improve Immunogenicity Of Antigens And Specificity Of Antibodies
Judith Fitzpatrick - Englewood NJ, US Regina Lenda - Wesley Hills NY, US
Assignee:
Serex, Inc. - Maywood NJ
International Classification:
A61K 39/385
US Classification:
4241841
Abstract:
A method of improving specific immune response to small immunogens, haptens, has been developed by changing the linkage between the hapten and carrier being used for immunization. High affinity antibodies to cotinine have been produced using this method. Antibodies to a glycated protein have also been developed, utilizing an immunogen which is composed of a glycated peptide mimic of the glycated peptide sequence which is the target epitope, wherein the peptide mimic is constructed to conformationally mimic the conformation of the peptide in the native protein, the peptide mimic contains no charged groups or other immunodominant group, and is connected to a spacer sequence equivalent to a peptide spacer of between one and thirty amino acids in length, which serves to position the peptide epitope in a conformation that approximates its conformation in the native protein. In another embodiment, the peptide mimic and spacer are linked to a carrier molecule.
Methods To Improve Immunogenicity Of Antigens And Specificity Of Antibodies
Judith Fitzpatrick - Englewood NJ, US Regina Lenda - Wesley Hills NY, US
Assignee:
Serex, Inc. - Maywood NJ
International Classification:
G01N 33/531 A61K 38/03 C07K 17/02 C07K 16/44
US Classification:
436547, 435 71, 530345, 5303871
Abstract:
A method of improving specific immune responses to small immunogens, haptens, has been developed by changing the linkage between the hapten and carrier being used for immunization. Antibodies to a glycated protein have been developed, utilizing an immunogen which is composed of a glycated peptide mimic of the glycated peptide sequence which is the target epitope, wherein the peptide mimic is constructed to conformationally mimic the conformation of the peptide in the native protein, the peptide mimic contains no charged groups or other immunodominant group, and the peptide mimic is connected to a spacer sequence equivalent to a peptide spacer of between one and thirty amino acids in length, which serves to position the peptide epitope in a conformation that approximates its conformation in the native protein. In a further embodiment the peptide mimic and spacer are linked to a carrier molecule.
Methods To Improve Immunogenicity Of Antigens And Specificity Of Antibodies
Judith Fitzpatrick - Englewood NJ, US Regina Lenda - Wesley Hills NY, US
Assignee:
Serex, Inc.
International Classification:
C12P021/04 A61K039/00
US Classification:
424/184100, 435/070210
Abstract:
A method of improving specific immune responses to smal immunogens, haptens, has been developed by changing the linkage between the hapten and carrier being used for immunization. High affinity antibodies to the hapten cotinine have been produced using this method. Antibodies to a glycated protein have also been developed, utilizing an immunogen which is composed of a glycated peptide mimic of the glycated peptide sequence which is the target epitope, wherein the peptide mimic is constructed to conformationally mimic the conformation of the peptide in the native protein, the peptide mimic contains no charged groups or other immunodominant group, and the peptide mimic is connected to a spacer sequence equivalent to a peptide spacer of between one and thirty amino acids in length, which serves to position the peptide epitope in a conformation that approximates its conformation in the native protein. In a further embodiment the peptide mimic and spacer are linked to a carrier molecule. This method has been used to produce an antibody to the glycated protein HbAc, wherein the peptide mimic includes a valine modified by addition of a glucose molecule, an analog of Histidine which does not bear a charge in the immunizing structure, allows orientation of the peptide so that the immune response can be directed to the side of the peptide chain oriented oppositely to the ring, and is of a size that the conformation of the peptide mimics the conformation of the peptide in the native molecule, a leucine or an analog thereof which allows binding to an antibody preferentially recognizing Hb Ac such as 82D259, and a threonine or an analog thereof which allows binding to antibody number 82D259. In the example described below the histidine analog is 2-amino-3-flurylpropionyl, and the peptide is Fructosyl-Val-2-amino-3-furanylproprionic acid-Leu-Pro-Pro-Glu-Glu-Tyr-Tyr-Cys.
Medicine Doctors
Judith A Fitzpatrick, Leonia NJ - LPT (Licensed physical therapist)
Kathleen Redd, Gerard Dresser, Margaret Feetham, Geraldine Johnson, Laura Higgins, Theresa Ritchie, Anne Politano, Andrea Arnao, Gail Lach, Florence Charles, Yvonne Bonnie, Mary Shea