Researchers at the University of Pittsburgh have developed 2nd generation griffithsin mutants with enhanced stability and solubility. Griffithsin is a potent antiviral protein effective against HIV and other viruses. The modified griffithsin polypeptides exhibit reduced methionine oxidation, increased shelf-life, and improved solubility, making them more suitable for pharmaceutical development and extending their usable storage times. These advancements could significantly impact the development of antiviral therapies and improve the efficacy of griffithsin-based treatments.
Description
Griffithsin is a small protein known for its potent antiviral activity, particularly against HIV. The 2nd generation griffithsin mutants have been engineered to include specific mutations that enhance their stability and solubility. These modifications include changes to the amino acid sequence that prevent methionine oxidation and alter the isoelectric point of the protein, improving its solubility in various pH ranges. The mutants can be used to create fusion proteins, conjugates, and other constructs for targeted antiviral therapies.
Applications
• Antiviral therapies
• HIV inhibition
• Pharmaceutical formulations
• Research tool for studying protein-protein interactions
Advantages
• Enhanced stability and solubility of griffithsin polypeptides
• Increased shelf-life due to reduced oxidation
• Improved bioavailability in different body compartments
• Potential for use in a wide range of antiviral applications
• Ability to form fusion proteins and conjugates for targeted therapies
Invention Readiness
The 2nd generation griffithsin mutants have undergone extensive in vitro studies, demonstrating their enhanced stability and solubility compared to the wild-type protein. These studies have shown that the modified polypeptides exhibit reduced methionine oxidation and increased shelf-life.
IP Status
https://patents.google.com/patent/US20220315629A1
