tailieunhanh - Báo cáo khoa học: Protein oligomerization induced by oleic acid at the solid–liquid interface – equine lysozyme cytotoxic complexes

Protein oligomeric complexes have emerged as a major target of current research because of their key role in aggregation processes in living systems andin vitro. Hydrophobic and charged surfaces may favour the self-assembly process by recruiting proteins and modifying their interactions. We found that equine lysozyme assembles into multimeric complexes with oleic acid (ELOA) at the solid–liquid interface within an ion-exchange chromatography column preconditioned with oleic acid. | Protein oligomerization induced by oleic acid at the solid-liquid interface - equine lysozyme cytotoxic complexes Kristina Wilhelm1 Adas Darinskas2 Wim Noppe3 Elke Duchardt1 K. Hun Mok5 Vladana Vukojevic6 Jurgen Schleucher1 and Ludmilla A. Morozova-Roche1 1 Department of MedicalBiochemistry and Biophysics Umea University Sweden 2 Institute of Immunology Vilnius University Lithuania 3 Interdisciplinary Research Center Campus Kortrijk Leuven University Belgium 4 Institute of Molecular Biosciences Johann Wolfgang Goethe University Frankfurt Germany 5 Trinity College Schoolof Biochemistry and Immunology University of Dublin Ireland 6 Department of ClinicalNeuroscience Karolinska Institute Stockholm Sweden Keywords amyloid HAMLET lysozyme oleic acid oligomers Correspondence L. A. Morozova-Roche Department of MedicalBiochemistry and Biophysics Umea University 901 87 Umea Sweden Fax 46 90 786 9795 Tel 46 90 786 5283 E-mail Received 30 March 2009 revised 6 May 2009 accepted 21 May 2009 doi Protein oligomeric complexes have emerged as a major target of current research because of their key role in aggregation processes in living systems and in vitro. Hydrophobic and charged surfaces may favour the self-assembly process by recruiting proteins and modifying their interactions. We found that equine lysozyme assembles into multimeric complexes with oleic acid ELOA at the solid-liquid interface within an ion-exchange chromatography column preconditioned with oleic acid. The properties of ELOA were characterized using NMR spectroscopic methods and atomic force microscopy and showed similarity with both amyloid oligomers and the complexes with oleic acid and its structural homologous protein a-lactalbumin known as humana-lactalbumin made lethal for tumour cells HAMLET . As determined by NMR diffusion measurements ELOA may consist of 4-30 lysozyme molecules. Each lysozyme molecule is able to bind 11-48 oleic .