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Study of hydrophobic interactions between acylated proteins and phospholipid bilayers using BIACORE
Author(s) -
Roy MarieOdile,
Pugniere Martine,
Jullien Magali,
Chopineau Joël,
Mani JeanClaude
Publication year - 2001
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/1099-1352(200101/02)14:1<72::aid-jmr519>3.0.co;2-2
Subject(s) - phospholipid , chemistry , bovine pancreatic ribonuclease , ribonuclease , rnase p , hydrophobic effect , biochemistry , monolayer , membrane , surface plasmon resonance , biophysics , nanoparticle , rna , biology , chemical engineering , gene , engineering
Intracellular proteins of eukaryotic cells are frequently covalently modified by the addition of long chain fatty acids. These modifications are thought to allow otherwise soluble proteins to associate with membranes by lipid–lipid based hydrophobic interactions. The purpose of this work was to quantify the effect of acyl chain length on hydrophobic interactions between acylated proteins and phospholipid monolayers. The binding of an artificially acylated model protein to electrically neutral phospholipids was studied by surface plasmon resonance, using BIACORE. Kinetic rates for the binding of bovine pancreatic ribonuclease A (RNase A), monoacylated on its N‐terminal lysine with fatty acids of 10, 12, 14, 16 or 18 carbon atoms, to phospholipids on hydrophobic sensor chips, were measured. Unlike unmodified ribonuclease, acylated RNase A bound to the phospholipids, and the association level increased with the acyl chain length to reach a maximum for C16. Reproducible kinetics were obtained which did not fit a 1:1 Langmuir model but rather a two‐step binding profile. Copyright © 2001 John Wiley & Sons, Ltd. Abbreviations used: DPMC L ‐d‐dimyristoyl‐phosphatidylcholineRNase A ribonuclease A.