PAGE TITLE
Overview
PAGE SUMMARY
Developed by Dr. Timothy Cunningham at Drexel University, this innovation is a peptide‑based platform that activates Heat Shock Protein 70 (HSP70) to restore the body’s natural protein quality control systems.
The technology comprises a family of short, bioengineered peptides, most notably CHEC 9, CHEC 7, and the optimized cyclic variant cycloSKEc7 (cSKE7), derived from naturally occurring protein fragments that help regulate cellular stress responses. These peptides work by activating Heat Shock Protein 70 (HSP70), a key “protein quality control” factor in the body that identifies and repairs or removes damaged proteins. In many age related and metabolic conditions, proteins become chemically modified (for example, by excess blood sugar byproducts), causing them to misfold and clump into toxic aggregates known as amyloids that impair normal cell function. The CHEC peptides act as small molecule regulators of HSP70, enhancing its ability to break apart these aggregates and restore protein function.
Earlier versions of the Drexel inventor’s peptides demonstrated anti inflammatory and cell protective effects through this mechanism, while the next generation cSKE7 has been rationally redesigned to improve stability, solubility, and therapeutic practicality. In human plasma models of metabolic stress, these peptides have been shown to disperse existing protein aggregates, inhibit new aggregate formation at very low concentrations, and recover key enzymatic and antioxidant functions, ultimately reducing oxidative stress and inflammation. Together, these properties position this proof-of-concept platform as a novel approach to treating diseases driven by protein damage and aggregation, including metabolic disorders, neurodegenerative conditions, and aging related decline, by restoring the body’s natural protein maintenance systems rather than targeting a single disease pathway.
Supported by early stage preclinical studies in human plasma and related models, the technology is positioned for translational development in treating protein aggregation–driven diseases.
ADVANTAGES
TITLE:Key Advantages
First-in-class mechanism leveraging HSP70 stimulation to directly disperse amyloid and protein aggregates, addressing root causes of proteostasis failure.
Demonstrated nanomolar potency and specificity, enabling effective disaggregation activity at low therapeutic doses.
Capability to reduce oxidative stress and inflammatory markers concomitantly, thereby offering multi-modal therapeutic effects.
Enhanced chemical stability and improved aqueous solubility support formulation development and therapeutic applicability.
Derived from a human endogenous protein, which may support a low immunogenicity profile.
Preclinical studies support translational relevance and therapeutic viability across human plasma and neural models.
Problem Solved
TITLE:Problems Solved
Mitigates accumulation of toxic protein aggregates in blood and neural tissues that contribute to metabolic and neurodegenerative diseases.
Addresses oxidative stress and inflammatory cascades triggered by protein misfolding, which exacerbate cellular damage and disease progression.
Overcomes limitations of current treatments that primarily provide symptomatic relief without targeting aggregate clearance.
Offers a novel therapeutic approach to reduce complications associated with hyperglycemia and aging-related cellular decline.
Supports restoration of enzymatic function and redox balance impaired in metabolic disorder pathologies.
APPLICATIONS
TITLE: Market Applications
Therapeutic intervention in metabolic disorders such as diabetes by mitigating protein aggregation-associated complications.
Treatment of age-related diseases including Alzheimer's, Parkinson's, and other neurodegenerative conditions characterized by proteinopathy.
Life extension therapies aimed at enhancing healthy lifespan through improved systemic proteostasis and reduction of cellular stress markers.
Potential adjunctive treatment in oxidative stress-related organ dysfunctions affecting heart, brain, and other vital organs.
Potential use in clinical settings requiring modulation of inflammatory responses linked to protein aggregation and cellular senescence.
IP STATUS
Intellectual Property and Development Status
Patent pending, PCT application filed
This early stage innovation developed in the Drexel University College of Medicine is available for translational research, testing and licensing opportunities.
PUBLICATIONS
References
Pubinfo should be the citation for your publication. Publink is the full url linking to the publication online or a pdf.
Scientific Publication – “Peptide treatment of human plasma disrupts metabolic and age-related pathologies via heat shock protein 70”
Scientific Publication – “Anti-inflammatory peptide regulates the supply of heat shock protein 70 monomers: implications for aging and age-related disease”
Scientific Publication – “Heptamer Peptide Disassembles Native Amyloid in Human Plasma Through Heat Shock Protein 70”
Commercialization Opportunities This early stage innovation developed in the Drexel University College of Medicine is available for translational research, testing and licensing opportunities.
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Contact Information
For intellectual property and licensing inquiries, please contact Dr. Robin Stears, Director of IP & Agreements, at rls457@drexel.edu or applied_innovation@drexel.edu.