18468151. CYCLIC PEPTIDYL INHIBITORS OF CAL-PDZ BINDING DOMAIN simplified abstract (OHIO STATE INNOVATION FOUNDATION)
Contents
- 1 CYCLIC PEPTIDYL INHIBITORS OF CAL-PDZ BINDING DOMAIN
- 1.1 Organization Name
- 1.2 Inventor(s)
- 1.3 CYCLIC PEPTIDYL INHIBITORS OF CAL-PDZ BINDING DOMAIN - A simplified explanation of the abstract
- 1.4 Simplified Explanation
- 1.5 Potential Applications
- 1.6 Problems Solved
- 1.7 Benefits
- 1.8 Potential Commercial Applications
- 1.9 Possible Prior Art
- 1.10 Original Abstract Submitted
CYCLIC PEPTIDYL INHIBITORS OF CAL-PDZ BINDING DOMAIN
Organization Name
OHIO STATE INNOVATION FOUNDATION
Inventor(s)
Patrick G. Dougherty of Columbus OH (US)
CYCLIC PEPTIDYL INHIBITORS OF CAL-PDZ BINDING DOMAIN - A simplified explanation of the abstract
This abstract first appeared for US patent application 18468151 titled 'CYCLIC PEPTIDYL INHIBITORS OF CAL-PDZ BINDING DOMAIN
Simplified Explanation
The patent application describes peptides that consist of a cyclic cell-penetrating peptide sequence (cCPP) and a CAL-PDZ binding sequence, with the CAL-PDZ binding sequence conjugated to the cCPP. The peptides may also include a physiologically cleavable group that is reduced after entering the cell, converting the peptide into a linear form. The cCPP sequence not only facilitates the cytosolic delivery of the CAL-PDZ binding sequence but also enhances the binding of the CAL-PDZ binding sequence to the CAL-PDZ binding domain and improves its selectivity for the CAL-PDZ domain over other PDZ binding domains.
- Peptides consist of cCPP and CAL-PDZ binding sequence
- CAL-PDZ binding sequence is conjugated to cCPP
- Peptides may include a physiologically cleavable group
- Cleavable group is reduced after cell entry, converting peptide into linear form
- cCPP sequence enhances cytosolic delivery of CAL-PDZ binding sequence
- cCPP sequence improves binding of CAL-PDZ binding sequence to CAL-PDZ binding domain
- cCPP sequence enhances selectivity of CAL-PDZ binding sequence for CAL-PDZ domain
Potential Applications
The technology could be applied in drug delivery systems, targeted therapy, and molecular biology research.
Problems Solved
The technology addresses the challenge of efficiently delivering therapeutic agents into cells and improving the specificity of binding interactions between molecules.
Benefits
The technology offers enhanced cellular uptake of therapeutic compounds, increased binding affinity to target proteins, and improved selectivity for specific protein domains.
Potential Commercial Applications
The technology could be utilized in pharmaceuticals, biotechnology, and research institutions for developing novel therapeutics and studying protein-protein interactions.
Possible Prior Art
Prior research may exist on cell-penetrating peptides, CAL-PDZ binding sequences, and methods for enhancing protein binding interactions. Further investigation is needed to determine the novelty of the current invention.
Unanswered Questions
How does the physiologically cleavable group impact the overall stability and efficacy of the peptides in cellular environments?
The physiologically cleavable group plays a crucial role in converting the cyclic peptide into a linear form after cell entry. However, the specific mechanisms by which this cleavage process affects the stability and efficacy of the peptides in cellular environments are not fully elucidated. Further studies are needed to investigate the impact of different cleavable groups on the overall performance of the peptides.
What are the potential off-target effects of the cCPP sequence on cellular processes and signaling pathways?
While the cCPP sequence enhances the cellular uptake and delivery of the CAL-PDZ binding sequence, its interactions with other cellular components and signaling pathways could lead to unintended off-target effects. Understanding the specificity of the cCPP sequence and its potential interactions with intracellular molecules is essential for evaluating the safety and efficacy of the peptides in therapeutic applications.
Original Abstract Submitted
Described herein, in various embodiments, are peptides comprising: (i) a cyclic cell-penetrating peptide sequence (cCPP) and (ii) a CAL-PDZ binding sequence, which is conjugated, directly or indirectly, to an N-terminus of an amino acid in the cCPP, to a C-terminus of an amino acid on the cCPP, or on a side chain of an amino acid in the cCPP. In other embodiments, the peptides further comprise a physiologically cleavable group, wherein after entering the cell, the physiologically cleavable group is reduced, thereby providing a linear peptide. Without being bound by theory, the inventors discovered that the amino acid sequence in the cCPP, which facilities cytosolic delivery of the CAL-PDZ binding sequence also, surprisingly and unexpectedly, synergistically improves binding of CAL-PDZ binding sequence to the CAL-PDZ binding domain. Additionally, the cCPP sequence may also improve selectivity of the CAL-PDZ binding sequence for the CAL-PDZ domain relative to other PDZ binding domains.
