Patents by Inventor John M. Tomich
John M. Tomich 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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Publication number: 20220183277Abstract: Described herein are linear peptides for creation of colloidal particles and micelles for delivery of active agents. The colloidal particles facilitate encapsulation and delivery of hydrophobic and/or poorly water soluble active agents within the particle hydrophobic core. The compositions are suitable for delivery of active agents to plants and animals.Type: ApplicationFiled: March 20, 2020Publication date: June 16, 2022Inventors: John M. Tomich, Sheila de Mello Barros, Susan K. Whitaker, Pinakin Sukthankar
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Patent number: 11252957Abstract: Described herein are nucleic acid-peptide capsule complexes or nanoparticles comprising pre-formed peptide capsules and nucleic acids bound the exterior surface of the capsule, such that the wrap around the capsule membrane. The peptide capsules comprise bilayer membrane defining a liquid-receiving interior space and comprises a plurality of branched, amphipathic peptides. Method of making and using such complexes for delivering nucleic acids in vivo and in vitro are also described.Type: GrantFiled: August 31, 2017Date of Patent: February 22, 2022Assignee: Kansas State University Research FoundationInventors: John M. Tomich, Gerald Reeck, Luz Adriana Avila Flores, Raman Chandrasekar
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Patent number: 10961547Abstract: Described are nanoparticulates comprising a metallic nanoparticle core and a peptide coating or shell encapsulating the nanoparticle core and being covalently bonded thereto. The coating is formed from a plurality of branched, amphipathic peptides, each comprising a polar/positively charged C-terminal segment, a branch point, and two hydrophobic N-terminal segments extending from the branch point. Methods of forming and using the nanoparticulates are also described. When a plurality of first and second peptides are added sequentially to the nanoparticle core, the peptides they self-assemble to form an interlocking peptide network bilayer where the respective hydrophobic segments of the peptides form beta-sheet structures in which the opposed sequences interlock to form a zipper-like structure in three dimensions.Type: GrantFiled: November 4, 2015Date of Patent: March 30, 2021Assignee: Kansas State University Research FoundationInventors: John M. Tomich, Pinakin R. Sukthankar
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Publication number: 20190246632Abstract: Described herein are nucleic acid-peptide capsule complexes or nanoparticles comprising pre-formed peptide capsules and nucleic acids bound the exterior surface of the capsule, such that the wrap around the capsule membrane. The peptide capsules comprise bilayer membrane defining a liquid-receiving interior space and comprises a plurality of branched, amphipathic peptides. Method of making and using such complexes for delivering nucleic acids in vivo and in vitro are also described.Type: ApplicationFiled: August 31, 2017Publication date: August 15, 2019Inventors: John M. Tomich, Gerald Reeck, Luz Adriana Avila Flores, Raman Chandrasekar
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Publication number: 20170232116Abstract: Described are nanoparticulates comprising a metallic nanoparticle core and a peptide coating or shell encapsulating the nanoparticle core and being covalently bonded thereto. The coating is formed from a plurality of branched, amphipathic peptides, each comprising a polar/positively charged C-terminal segment, a branch point, and two hydrophobic N-terminal segments extending from the branch point. Methods of forming and using the nanoparticulates are also described. When a plurality of first and second peptides are added sequentially to the nanoparticle core, the peptides they self-assemble to form an interlocking peptide network bilayer where the respective hydrophobic segments of the peptides form beta-sheet structures in which the opposed sequences interlock to form a zipper-like structure in three dimensions.Type: ApplicationFiled: November 4, 2015Publication date: August 17, 2017Inventors: John M. Tomich, Pinakin R. Sukthankar
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Patent number: 8895502Abstract: Therapeutic peptides (and peptoids) for preventing or inhibiting tissue damage associated with ischemia and/or reperfusion are provided, along with peptides (and peptoids) for preventing or inhibiting cancerous tissue growth. The peptides are derived from ?2-glycoprotein I. Pharmaceutical and veterinary compositions comprising the peptides are also provided. Methods of using the peptides to prevent or inhibit tissue damage associated with ischemia and/or reperfusion and/or to prevent or inhibit tissue damage or the growth of cancerous tissue are also provided.Type: GrantFiled: March 1, 2013Date of Patent: November 25, 2014Assignee: Kansas State University Research FoundationInventors: Sherry Fleming, John M. Tomich
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Patent number: 8883967Abstract: The present invention provides branched amphipathic peptides and vesicles formed thereof. The peptides comprise a polar/positively charged C-terminal segment, a branch point, and two hydrophobic N-terminal segments extending from the branch point. The vesicles are formed using a plurality of first and second peptides, wherein the first peptide has a different chain length from the second peptide. When a plurality of the first and second peptides are mixed together, they self-assemble to form small spheres defined by a membrane consisting of an interlocking peptide network bilayer and having a liquid-receiving interior space (i.e., hollow core). In the bi-layer, the respective hydrophobic segments of the peptides form beta-sheet structures having a hydrogen bond-stabilized, anti-parallel orientation in which the opposed sequences interlock to form a zipper-like structure in three dimensions. Thus, the peptide assembly (i.e.Type: GrantFiled: March 26, 2010Date of Patent: November 11, 2014Assignee: Kansas State University Research FoundationInventors: John M. Tomich, Takeo Iwamoto, Yasuaki Hiromasa, Sushanth Gudlur
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Patent number: 8163870Abstract: The present invention provides a family of peptides based upon the M2GlyR sequence. These peptides are derivatives of the M2GlyR sequence and can be modified at their ends to include a plurality of polar amino acid residues to enhance their solubility. Particularly preferred derivatives include portions of the M2GlyR sequence which are palindromic to another portion of the peptide or to the M2GlyR sequence itself. Preferably these portions are at least 7 amino acid residues in length. Peptides embraced by the present invention are characterized by having greater effects on the transepithelial electrical resistance of cells at lower concentrations. Peptides of the present invention have been shown to increase Isc in MDCK epithelial cell monolayers with half maximal effects observed at or below 30 ?M, a nearly 10-fold improvement over any peptide previously characterized in the M2GlyR family.Type: GrantFiled: June 14, 2004Date of Patent: April 24, 2012Assignee: Kansas State University Research FoundationInventors: John M. Tomich, Iwamoto Takeo, James R. Broughman, Bruce D. Schultz
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Publication number: 20120021020Abstract: The present invention provides branched amphipathic peptides and vesicles formed thereof. The peptides comprise a polar/positively charged C-terminal segment, a branch point, and two hydrophobic N -terminal segments extending from the branch point. The vesicles are formed using a plurality of first and second peptides, wherein the first peptide has a different chain length from the second peptide. When a plurality of the first and second peptides are mixed together, they self-assemble to form small spheres defined by a membrane consisting of an interlocking peptide network bilayer and having a liquid-receiving interior space (i.e., hollow core). In the bi-layer, the respective hydrophobic segments of the peptides form beta-sheet structures having a hydrogen bond-stabilized, anti-parallel orientation in which the opposed sequences interlock to form a zipper-like structure in three dimensions. Thus, the peptide assembly (i.e.Type: ApplicationFiled: March 26, 2010Publication date: January 26, 2012Applicant: KANSAS STATE UNIVERSITY RESEARCH FOUNDATIONInventors: John M. Tomich, Takeo Iwamoto, Yasuaki Hiromasa, Sushanth Gudlur
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Patent number: 7829661Abstract: The present invention provides a family of peptides based upon the M2GlyR sequence. These peptides are derivatives of the M2GlyR sequence and can be modified at their ends to include a plurality of polar amino acid residues to enhance their solubility. Particularly preferred derivatives include portions of the M2GlyR sequence which are palindromic to another portion of the peptide or to the M2GlyR sequence itself. Preferably these portions are at least 7 amino acid residues in length. Peptides embraced by the present invention are characterized by having greater effects on the transepithelial electrical resistance of cells at lower concentrations. Peptides of the present invention have been shown to increase Isc in MDCK epithelial cell monolayers with half maximal effects observed at or below 30 ?M, a nearly 10-fold improvement over any peptide previously characterized in the M2GlyR family.Type: GrantFiled: June 14, 2004Date of Patent: November 9, 2010Assignee: Kansas State University Research FoundationInventors: John M. Tomich, Iwamoto Takeo, James R. Broughman, Bruce D. Schultz
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Patent number: 7592341Abstract: Improved methods and preparations are provided for ocular administration of therapeutic drugs. The preparations include respective quantities of a drug and a peptide which enhances transport of the drug across ocular tissues. The drug and peptide components may be separately administered or used as a mixture. The preferred peptide is NC-1059 (SEQ. ID NO. 1).Type: GrantFiled: December 15, 2005Date of Patent: September 22, 2009Assignee: Kansas State University Research FoundationInventors: John M. Tomich, Takeo Iwamoto
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Publication number: 20080207623Abstract: Improved methods and preparations are provided for ocular administration of therapeutic drugs. The preparations include respective quantities of a drug and a peptide which enhances transport of the drug across ocular tissues. The drug and peptide components may be separately administered or used as a mixture. The preferred peptide is NC-1059 (Seq. ID No. 1).Type: ApplicationFiled: December 15, 2005Publication date: August 28, 2008Inventors: John M. Tomich, Takeo Iwamoto
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Patent number: 6750200Abstract: The present invention provides a family of peptides based upon the M2GlyR sequence. These peptides are derivatives of the M2GlyR sequence and can be modified at their ends to include a plurality of polar amino acid residues to enhance their solubility. Particularly preferred derivatives include portions of the M2GlyR sequence which are palindromic to another portion of the peptide or to the M2GlyR sequence itself. Preferably these portions are at least 7 amino acid residues in length. Peptides embraced by the present invention are characterized by having greater effects on the transepithelial electrical resistance of cells at lower concentrations. Peptides of the present invention have been shown to increase Isc in MDCK epithelial cell monolayers with half maximal effects observed at or below 30 &mgr;M, a nearly 10-fold improvement over any peptide previously characterized in the M2GlyR family.Type: GrantFiled: November 9, 2000Date of Patent: June 15, 2004Assignee: Kansas State University Research FoundationInventors: John M. Tomich, Takeo Iwamoto, James R. Broughman, Bruce D. Schultz
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Patent number: 6077826Abstract: The present invention is directed to multiple-peptide channel assemblies for transport of anions such as chloride ions through epithelial cells, synthetic peptides capable of forming such channel assemblies and methods for using channel assemblies in therapeutic contexts for altering the flux of water across epithelial cells. The channel assemblies are composed of a plurality of peptides that transport through the membrane of an epithelial cell and provide for alteration of the flux of water through the cell. The peptides are soluble in water to a level of at least 10 mM and exhibit at least about 50% helical content when dispersed in a 40% trifluoroethanol/60% water solution. The peptides ideally have the amino acid sequence ABC(X).sub.Type: GrantFiled: June 8, 1998Date of Patent: June 20, 2000Assignee: Kansas State University Research FoundationInventors: John M. Tomich, Takeo Iwamoto, Lawrence P. Sullivan
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Patent number: 5922840Abstract: Methods for making preparations of homogenous peptides are disclosed. In these methods, reversible alterations of the physicochemical properties of the peptides are exploited. In preferred embodiments, the methods include the following sequential steps: (1) exhaustive capping is carried out during solid-phase synthesis of a desired peptide; (2) a cleavable linker is attached to the peptide, (3) a polymer is added to the peptide either by condensation with preformed polymer or by in situ polymerization such that the linker is interposed between the polymer moiety and the peptide moiety of the resultant adduct; alternatively, steps (2) and (3) can be conducted simultaneously by attaching a combination polymer/linker to the peptide; (4) the polymer-peptide adduct is cleaved from the resin; (5) the polymer-peptide adduct is purified from undesired, nonadducted peptides; and (6) the polymer-peptide adduct is cleaved at the linker, and the desired peptide is purified from the polymer.Type: GrantFiled: July 23, 1996Date of Patent: July 13, 1999Assignee: Kansas State University Research FoundationInventors: John M. Tomich, Takeo Iwamoto