Exploring Drug and Antibody-Based Treatment Options for Creutzfeldt-Jakob Disease
Vasanth Senthilraja1, Eric Lou2, Abirath Nakka1, Preny Karamian1, Ishaq Aslam1, Joel Rabara3, Nimrit Gahoonia1, Noor Kaur1, Akshay Reddy1, The Ber1 and Himanshu Wagh3*
1California Northstate University College of Health Sciences, Rancho Cordova, USA
2University of California Los Angeles, Los Angeles, USA
3California Northstate University College of Medicine, Elk Grove, USA
Creutzfeldt-Jakob Disease (CJD) is a neurodegenerative disease characterized by mutant PrP prion proteins, which accumulates and impairs the function of wild-type PrPc proteins. The interaction of prion proteins with wild-type proteins converts the PrPc proteins to mutant PrP proteins. These mutant prion proteins lead to neural tissue degradation and other nervous system problems that can eventually lead to death. The use of antibodies to target and destroy prion proteins can be used to decrease PrP levels that can stop CJD progression. The binding affinities of different anti-PrP Fab antibodies are analyzed to determine which antibody best binds to PrP proteins and targets them for destruction. Through antibody-based targeting of prion proteins, potential treatment methods could be developed for CJD. In addition, the use of drugs, such as quinacrine and doxycycline, also show short-term effects in decreasing the progression of CJD. These drugs extend the average lifespan of tested subjects with CJD but also lead to the development of drug-resistant prion proteins that eventually cause the death of the subject affected by CJD.
Neurodegenerative, Antibody, Doxycycline, Prion