title: Preference toward a polylysine enantiomer in inhibiting prions.
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.
authors.affiliation: Division of Laboratory Animal Resources, University of Kentucky, Lexington, KY, USA.
authors.forename: Karen S
authors.initials: KS
authors.lastname: Jackson
authors.forename: Jihyun
authors.initials: J
authors.lastname: Yeom
authors.forename: Youngmi
authors.initials: Y
authors.lastname: Han
authors.forename: Younsoo
authors.initials: Y
authors.lastname: Bae
authors.forename: Chongsuk
authors.initials: C
authors.lastname: Ryou
mesh_terms: D002460:Cell Line; D015536:Down-Regulation; D006801:Humans; D007700:Kinetics; D010958:Plasminogen / Q000378:metabolism; D011107:Polylysine / Q000737:chemistry / Q000378:metabolism*; D011328:Prions / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D017510:Protein Folding; D013237:Stereoisomerism
chemical_list: D011328:Prions; D011107:Polylysine; D010958:Plasminogen