20240033318. PEPTIDYL INHIBITORS OF CALCINEURIN-NFAT INTERACTION simplified abstract (Ohio State Innovation Foundation)

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PEPTIDYL INHIBITORS OF CALCINEURIN-NFAT INTERACTION

Organization Name

Ohio State Innovation Foundation

Inventor(s)

Dehua Pei of Columbus OH (US)

John W. Christman of Columbus OH (US)

Manjula Karpurapu of Columbus OH (US)

Patrick G. Dougherty of Columbus OH (US)

PEPTIDYL INHIBITORS OF CALCINEURIN-NFAT INTERACTION - A simplified explanation of the abstract

This abstract first appeared for US patent application 20240033318 titled 'PEPTIDYL INHIBITORS OF CALCINEURIN-NFAT INTERACTION

Simplified Explanation

The patent application describes peptides and peptide conjugates that inhibit the interaction between CN (calcineurin) and NFAT (nuclear factor of activated T-cells). These peptides contain CN binding motifs (CNBMs) and a hydrophobic, non-peptidic moiety (RH) that interacts with a hydrophobic pocket on a CN protein. The peptides also contain a sequence of amino acids (AAU1-AAU2-AAU3-AAU4-AAU5-AAU6), where each AAU is optional and independently represents an amino acid. The RH or the AAU sequence can be conjugated to the N- or C-terminus of the CNBM.

  • Peptides and peptide conjugates are described that inhibit the interaction between CN and NFAT.
  • The peptides contain CN binding motifs (CNBMs) and a hydrophobic, non-peptidic moiety (RH).
  • The RH interacts with a hydrophobic pocket on a CN protein.
  • The peptides also contain a sequence of optional amino acids (AAU1-AAU2-AAU3-AAU4-AAU5-AAU6).
  • The RH or the AAU sequence can be conjugated to the N- or C-terminus of the CNBM.

Potential applications of this technology:

  • Development of therapeutic agents for diseases involving CN-NFAT interaction, such as autoimmune disorders and certain cancers.
  • Modulation of immune responses and inflammation.
  • Treatment of neurodegenerative diseases.

Problems solved by this technology:

  • Inhibition of the CN-NFAT interaction, which can contribute to the development and progression of various diseases.
  • Targeted disruption of specific protein-protein interactions involved in disease pathways.

Benefits of this technology:

  • Provides a novel approach to modulating CN-NFAT interaction.
  • Offers potential for the development of more specific and effective therapeutic agents.
  • Allows for targeted disruption of disease-related protein-protein interactions.


Original Abstract Submitted

described are peptides and peptide conjugates comprising cn binding motifs (cnbm) which inhibit the cn-nfat interaction. in some embodiments, the peptides comprise: (i) cnbm; (ii) a hydrophobic, non-peptidic moiety (rh) which interacts with the hydrophobic pocket on a cn protein; (iii) a sequence -aau1-aau2-aau3-aau4-aau5-aau6-, wherein each of aau2, aau3, aau4, aau5, and aau6, is, independently, optional, and each of aau1, aau2, aau3, aau4, aau5, and aau6 when present is independently an amino acid as defined herein; or (iv) combinations thereof. in some embodiments, rh is conjugated to the n- or c-terminus of the cnbm. in some embodiments, the sequence -aau1-aau2-aau3-aau4-aau5-aau6- is conjugated to the n- or c terminus of the cnbm. in some embodiments, the peptides comprise: cnbm and rh. in some embodiments. in some embodiments, the peptides comprise: cnbm and aau1-aau2-aau3-aau4-aau5-aau6-. in some embodiments, the peptides of the disclosure cnbm and rh.

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