Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Study of hydrophobic interactions between acylated proteins and phospholipid bilayers using BIACORE
Autore:
Roy, MO; Pugniere, M; Jullien, M; Chopineau, J; Mani, JC;
Indirizzi:
Fac Pharm Montpellier, CNRS, UMR 9921, Inst Biotechnol & Pharmacol, F-34060 Montpellier 2, France Fac Pharm Montpellier Montpellier France 2 F-34060 Montpellier 2, France Ctr Biochim Struct, CNRS UMR 9955, UMI, INSERM U414, Montpellier, France Ctr Biochim Struct Montpellier France INSERM U414, Montpellier, France Univ Technol Compiegne, Technol Enzymat Lab, UPRESA CNRS 6022, F-60206 Compiegne, France Univ Technol Compiegne Compiegne France F-60206 -60206 Compiegne, France
Titolo Testata:
JOURNAL OF MOLECULAR RECOGNITION
fascicolo: 1, volume: 14, anno: 2001,
pagine: 72 - 78
SICI:
0952-3499(200101/02)14:1<72:SOHIBA>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
SURFACE-PLASMON RESONANCE; BINDING-KINETICS; MASS-TRANSPORT; MEMBRANE; PALMITOYLATION; BIOSENSORS; CRYSTALLIZATION; MONOLAYERS; VESICLES;
Keywords:
hydrophobic interactions; interaction kinetics; BIACORE; acylated RNase; phospholipid bilayer; hydrophobic sensor chip;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
22
Recensione:
Indirizzi per estratti:
Indirizzo: Mani, JC Fac Pharm Montpellier, CNRS, UMR 9921, Inst Biotechnol & Pharmacol, 15 AveCharles Flahault, F-34060 Montpellier 2, France Fac Pharm Montpellier 15 Ave Charles Flahault Montpellier France 2
Citazione:
M.O. Roy et al., "Study of hydrophobic interactions between acylated proteins and phospholipid bilayers using BIACORE", J MOL RECOG, 14(1), 2001, pp. 72-78

Abstract

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 (C) 2001 John Wiley & Sons, Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 15:53:51