| Title | PrP106-126 peptide disrupts lipid membranes: Influence of C-terminal amidation |
| Authors | Zheng, Wenfu Wang, Lijun Hong, Yuankai Sha, Yinlin |
| Affiliation | Peking Univ, Single Mol & Nanobiol Lab, Dept Biophys, Sch Basic Med Sci, Beijing 100191, Peoples R China. Peking Univ, Ctr Prot Sci, Beijing 100191, Peoples R China. Peking Univ, Biomed X Ctr, Beijing 100191, Peoples R China. Peking Univ, Single Mol & Nanobiol Lab, Dept Biophys, Sch Basic Med Sci, Xueyuan Rd 38, Beijing 100191, Peoples R China. |
| Keywords | PrP106-126 C-terminal amidation Supported lipid bilayers Large unilamellar vesicles Flat high-rise domains Atomic force microscopy Surface plasmon resonance PRION PROTEIN-FRAGMENT SURFACE-PLASMON RESONANCE ATOMIC-FORCE MICROSCOPY NEUROTOXICITY RESIDUES-106-126 CONVERSION LIPOSOMES OXIDATION BILAYERS BINDING |
| Issue Date | 2009 |
| Publisher | 生物化学与生物物理学研究通讯 |
| Citation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS.2009,379,(2),298-303. |
| Abstract | PrP106-126 is located within the important domain concerning membrane related conformational conversion of human Prion protein (from cellular isoform PrPC to scrapie isoform PrPSc). Recent advances reveal that the pathological and physicochemical properties of PrP106-126 peptide are very sensitive to its N-terminal amidation, however, the detailed mechanism remains unclear. In this work, we studied the interactions of the PrP106-126 isoforms (PrP106-126(CONH2) and PrP106-426(COOH)) with the neutral lipid bilayers by atomic force microscopy, surface plasmon resonance and fluorescence spectroscopy. The membrane structures were disturbed by the two isoforms in a similarly stepwise process. The distinct morphological changes of the membrane were characterized by formation of semi-penetrated defects and sigmoidal growth of flat high-rise domains on the supported lipid bilayers. However, PrP106-126(COOH) displayed a higher peptide-lipid binding affinity than PrP106-126(CONH2) (similar to 2.9 times) and facilitated the peptide-lipid interactions by shortening the lag time. These results indicate that the C-terminal amidation may influence the pathological actions of PrP106-126 by lowering the interaction potentials with lipid membranes. (c) 2008 Elsevier Inc. All rights reserved. |
| URI | http://hdl.handle.net/20.500.11897/197325 |
| ISSN | 0006-291X |
| DOI | 10.1016/j.bbrc.2008.12.049 |
| Indexed | SCI(E) PubMed |
| Appears in Collections: | 基础医学院 |
