Amino Acids

, Volume 44, Issue 3, pp 993–1000 | Cite as

Preference toward a polylysine enantiomer in inhibiting prions

  • Karen S. Jackson
  • Jihyun Yeom
  • Youngmi Han
  • Younsoo Bae
  • Chongsuk Ryou
Original Article

Abstract

Differential anti-prion activity of polylysine enantiomers was studied. Based on our recent discovery that poly-l-lysine (PLK) is a potent anti-prion agent, we investigated suppression of prions in cultured cells using poly-d-lysine (PDK). The results showed that PDK was more efficacious than PLK to inhibit prions. Protein misfolding cyclic amplification assay demonstrated improved efficacy of PDK in inhibiting plasminogen-mediated prion propagation, corresponding to the enantio-preference of PDK observed in cultured cells. Furthermore, our study demonstrated that polylysines formed a complex with plasminogen. These results propose to hypothesize a plausible mechanism that elicits prion inhibition by polylysine enantiomers.

Keywords

Polylysine Enantiomers Prion Inhibition Plasminogen 

Notes

Acknowledgments

The authors thank P. Thomason for editorial and H. Lee for technical assistance.

Conflict of interest

The authors declare that we have no conflict of interest.

Supplementary material

726_2012_1430_MOESM1_ESM.doc (50 kb)
Supplementary material 1 (DOC 49 kb)

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Copyright information

© Springer-Verlag Wien 2012

Authors and Affiliations

  • Karen S. Jackson
    • 1
  • Jihyun Yeom
    • 2
  • Youngmi Han
    • 2
  • Younsoo Bae
    • 3
  • Chongsuk Ryou
    • 2
    • 4
    • 5
  1. 1.Division of Laboratory Animal ResourcesUniversity of KentuckyLexingtonUSA
  2. 2.Sanders-Brown Center on Aging, College of MedicineUniversity of KentuckyLexingtonUSA
  3. 3.Department of Pharmaceutical Sciences, College of PharmacyUniversity of KentuckyLexingtonUSA
  4. 4.Department of Microbiology, Immunology and Molecular Genetics, College of MedicineUniversity of KentuckyLexingtonUSA
  5. 5.Department of Pharmacology, College of PharmacyHanyang UniversityAnsanRepublic of Korea

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