Patents by Inventor Maria Dimarchi
Maria Dimarchi has filed for patents to protect the following inventions. This listing includes patent applications that are pending as well as patents that have already been granted by the United States Patent and Trademark Office (USPTO).
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Patent number: 9447162Abstract: Modified glucagon peptides are disclosed having enhanced potency at the glucagon receptor relative to native glucagon. Further modification of the glucagon peptides by forming lactam bridges or the substitution of the terminal carboxylic acid with an amide group produces peptides exhibiting glucagon/GLP-1 receptor co-agonist activity. The solubility and stability of these high potency glucagon analogs can be further improved by modification of the polypeptides by pegylation, substitution of carboxy terminal amino acids, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 26 (GPSSGAPPPS), SEQ ID NO: 27 (KRNRNNIA) and SEQ ID NO: 28 (KRNR).Type: GrantFiled: November 7, 2014Date of Patent: September 20, 2016Assignee: Indiana University Research and Technology CorporationInventors: Jonathan Day, James Patterson, Joseph Chabenne, Maria DiMarchi, David L. Smiley, Richard D. DiMarchi
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Publication number: 20150126440Abstract: Modified glucagon peptides are disclosed having enhanced potency at the glucagon receptor relative to native glucagon. Further modification of the glucagon peptides by forming lactam bridges or the substitution of the terminal carboxylic acid with an amide group produces peptides exhibiting glucagon/GLP-1 receptor co-agonist activity. The solubility and stability of these high potency glucagon analogs can be further improved by modification of the polypeptides by pegylation, substitution of carboxy terminal amino acids, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 26 (GPSSGAPPPS), SEQ ID NO: 27 (KRNRNNIA) and SEQ ID NO: 28 (KRNR).Type: ApplicationFiled: November 7, 2014Publication date: May 7, 2015Inventors: Jonathan DAY, James PATTERSON, Joseph CHABENNE, Maria DiMARCHI, David L. SMILEY, Richard D. DiMARCHI
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Patent number: 8900593Abstract: Modified glucagon peptides are disclosed having enhanced potency at the glucagon receptor relative to native glucagon. Further modification of the glucagon peptides by forming lactam bridges or the substitution of the terminal carboxylic acid with an amide group produces peptides exhibiting glucagon/GLP-1 receptor co-agonist activity. The solubility and stability of these high potency glucagon analogs can be further improved by modification of the polypeptides by pegylation, substitution of carboxy terminal amino acids, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 26 (GPSSGAPPPS), SEQ ID NO: 27 (KRNRNNIA) and SEQ ID NO: 28 (KRNR).Type: GrantFiled: January 9, 2013Date of Patent: December 2, 2014Assignee: Indiana University Research and Technology CorporationInventors: Jonathan Day, James Patterson, Joseph Chabenne, Maria DiMarchi, David L. Smiley, Richard D. DiMarchi
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Patent number: 8669228Abstract: Modified glucagon peptides are disclosed having improved solubility while retaining glucagon agonist activity. The glycogen peptides have been modified by substitution of native amino acids with, and/or addition of, charged amino acids to the carboxy terminus of the peptide. The modified glucagon agonists can be further modified by pegylation, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 23, or both to further enhance the solubility of the glucagon agonist analogs.Type: GrantFiled: January 3, 2008Date of Patent: March 11, 2014Assignee: Indiana University Research and Technology CorporationInventors: Richard D. Dimarchi, Maria Dimarchi, Joseph Chabenne
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Patent number: 8546327Abstract: Modified glucagon peptides are disclosed having enhanced potency at the glucagon receptor relative to native glucagon. Further modification of the glucagon peptides by forming intramolecular bridges or the substitution of the terminal carboxylic acid with an amide group produces peptides exhibiting glucagon/GLP-1 receptor co-agonist activity. The solubility and stability of these high potency glucagon analogs can be further improved by modification of the polypeptides by pegylation, acylation, alkylation, substitution of carboxy terminal amino acids, C-terminal truncation, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 26 (GPSSGAPPPS), SEQ ID NO: 27 (KRNRNNIA) and SEQ ID NO: 28 (KRNR).Type: GrantFiled: June 16, 2009Date of Patent: October 1, 2013Assignee: Indiana University Research and Technology CorporationInventors: Richard D. Dimarchi, David L. Smiley, Maria Dimarchi, Joseph Chabenne, Jonathan Day, James Patterson, Brian Ward
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Patent number: 8454971Abstract: Modified glucagon peptides are disclosed having enhanced potency at the glucagon receptor relative to native glucagon. Further modification of the glucagon peptides by forming lactam bridges or the substitution of the terminal carboxylic acid with an amide group produces peptides exhibiting glucagon/GLP-1 receptor co-agonist activity. The solubility and stability of these high potency glucagon analogs can be further improved by modification of the polypeptides by pegylation, substitution of carboxy terminal amino acids, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 26 (GPSSGAPPPS), SEQ ID NO: 27 (K-RNRNNIA) and SEQ ID NO: 28 (KRNR).Type: GrantFiled: February 13, 2008Date of Patent: June 4, 2013Assignee: Indiana University Research and Technology CorporationInventors: Jonathan Day, James Patterson, Joseph Chabenne, Maria Dimarchi, David L. Smiley, Richard D. Dimarchi
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Patent number: 8450270Abstract: Modified glucagon peptides are disclosed having improved solubility and/or half-life while retaining glucagon agonist activity. The glycogen peptides have been modified by substitution of native amino acids with, and/or addition of, charged amino acids to the carboxy terminus of the peptide. The modified glucagon agonists can be further modified by pegylation, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 23, or both to further enhance the solubility of the glucagon agonist analogs.Type: GrantFiled: June 16, 2009Date of Patent: May 28, 2013Assignee: Indiana University Research and Technology CorporationInventors: Richard D. Dimarchi, David L. Smiley, Maria Dimarchi, Joseph Chabenne, Jonathan Day
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Publication number: 20120172295Abstract: Glucagon peptides with increased GIP activity are provided, optionally with GLP-I and/or glucagon activity. In some embodiments, C-terminally extended glucagon peptides comprising an amino acid sequence substantially similar to native glucagon are provided herein.Type: ApplicationFiled: June 16, 2010Publication date: July 5, 2012Applicant: Indiana University Research And Technology CorpInventors: Richard D. Dimarchi, David L. Smiley, Maria Dimarchi, Joseph Chabenne, Jonathan Day, James Patterson, Brian P. Ward, Tao Ma
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Publication number: 20110257092Abstract: Modified glucagon peptides are disclosed having enhanced potency at the glucagon receptor relative to native glucagon. Further modification of the glucagon peptides by forming intramolecular bridges or the substitution of the terminal carboxylic acid with an amide group produces peptides exhibiting glucagon/GLP-1 receptor co-agonist activity. The solubility and stability of these high potency glucagon analogs can be further improved by modification of the polypeptides by pegylation, acylation, alkylation, substitution of carboxy terminal amino acids, C-terminal truncation, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 26 (GPSSGAPPPS), SEQ ID NO: 27 (KRNRNNIA) and SEQ ID NO: 28 (KRNR).Type: ApplicationFiled: June 16, 2009Publication date: October 20, 2011Inventors: Richard D. Dimarchi, David l. Smiley, Maria Dimarchi, Joseph Chabenne, Jonathan Day, James Patterson, Brian Ward
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Publication number: 20110190200Abstract: Modified glucagon peptides are disclosed having improved solubility and/or half-life while retaining glucagon agonist activity. The glycogen peptides have been modified by substitution of native amino acids with, and/or addition of, charged amino acids to the carboxy terminus of the peptide. The modified glucagon agonists can be further modified by pegylation, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 23, or both to further enhance the solubility of the glucagon agonist analogs.Type: ApplicationFiled: June 16, 2009Publication date: August 4, 2011Inventors: Richard D. DiMarchi, David L. Smiley, Maria Dimarchi, Joseph Chabenne, Jonathan Day
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Publication number: 20100190701Abstract: Modified glucagon peptides are disclosed having enhanced potency at the glucagon receptor relative to native glucagon. Further modification of the glucagon peptides by forming lactam bridges or the substitution of the terminal carboxylic acid with an amide group produces peptides exhibiting glucagon/GLP-1 receptor co-agonist activity. The solubility and stability of these high potency glucagon analogs can be further improved by modification of the polypeptides by pegylation, substitution of carboxy terminal amino acids, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 26 (GPSSGAPPPS), SEQ ID NO: 27 (K-RNRNNIA) and SEQ ID NO: 28 (KRNR).Type: ApplicationFiled: February 13, 2008Publication date: July 29, 2010Inventors: Jonathan Day, James Patterson, Joseph Chabenne, Maria Dimarchi, David Smiely, Richard D. Dimarchi
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Publication number: 20100190699Abstract: Modified glucagon peptides are disclosed having improved solubility while retaining glucagon agonist activity. The glycogen peptides have been modified by substitution of native amino acids with, and/or addition of, charged amino acids to the carboxy terminus of the peptide. The modified glucagon agonists can be further modified by pegylation, or the addition of a carboxy terminal peptide selected from the group consisting of SEQ ID NO: 20, SEQ ID NO: 21, SEQ ID NO: 23, or both to further enhance the solubility of the glucagon agonist analogs.Type: ApplicationFiled: January 3, 2008Publication date: July 29, 2010Applicant: Indiana University Research and Technology CorporationInventors: Richard D. Dimarchi, Maria Dimarchi, Joseph Chabenne