Amino Acids

, Volume 44, Issue 3, pp 993–1000

Preference toward a polylysine enantiomer in inhibiting prions

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

DOI: 10.1007/s00726-012-1430-8

Cite this article as:
Jackson, K.S., Yeom, J., Han, Y. et al. Amino Acids (2013) 44: 993. doi:10.1007/s00726-012-1430-8

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

PolylysineEnantiomersPrionInhibitionPlasminogen

Supplementary material

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

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