摘要
Vpu from HIV-1 is an 81 amino acid type I integral membrane protein which consists of a cytoplasmic and a transmembrane (TM) domain. The TM domain is known to alter membrane permeability for ions and substrates when inserted into artificial membranes. Peptides corresponding to the TM domain of Vpu (Vpu 1-32) and mutant peptides (Vpu1-32-W23L, Vpu 1-32-R31V, Vpu1-32-S24L) have been synthesized and reconstituted into artificial lipid bilayers. All peptides show channel activity with a main conductance level of around 20 pS. Vpu1-32-W23L has a considerable flickering pattern in the recordings and longer open times than Vpu1-32. Whilst recordings for Vpu1-32-R31V are almost indistinguishable from those of the WT peptide, recordings for Vpu 1-32-S24L do not exhibit any noticeable channel activity. Recordings of WT peptide and Vpu1-32-W23L indicate Michaelis-Menten behavior when the salt concentration is increased. Both peptide channels follow the Eisenman series I, indicative for a weak ion channel with almost pore like characteristics.
原文 | English |
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頁(從 - 到) | 1488-1497 |
頁數 | 10 |
期刊 | Proteins: Structure, Function and Genetics |
卷 | 70 |
發行號 | 4 |
DOIs | |
出版狀態 | Published - 3月 2008 |