amyloidogenic properties of a dn mutated 12 amino acid fragment of the c-terminal domain of the cholesteryl-ester transfer protein (cetp)amyloidogenic属性的dn突变12 c端域的氨基酸片段cholesteryl-ester转运蛋白(cetp).pdfVIP

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amyloidogenic properties of a dn mutated 12 amino acid fragment of the c-terminal domain of the cholesteryl-ester transfer protein (cetp)amyloidogenic属性的dn突变12 c端域的氨基酸片段cholesteryl-ester转运蛋白(cetp).pdf

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amyloidogenic properties of a dn mutated 12 amino acid fragment of the c-terminal domain of the cholesteryl-ester transfer protein (cetp)amyloidogenic属性的dn突变12 c端域的氨基酸片段cholesteryl-ester转运蛋白(cetp)

Int. J. Mol. Sci. 2011, 12, 2019-2035; doi:10.3390/ijms OPEN ACCESS International Journal of Molecular Sciences ISSN 1422-0067 /journal/ijms Article Amyloidogenic Properties of a D/N Mutated 12 Amino Acid Fragment of the C-Terminal Domain of the Cholesteryl-Ester Transfer Protein (CETP) Victor García-González and Jaime Mas-Oliva * Institute of Cell Physiology, National Autonomus University of Mexico (UNAM), AP 70-243, 04510 Mexico, D.F., Mexico; E-Mail: vgarcia@emailifc.unam.mx * Author to whom correspondence should be addressed; E-Mail: jmas@ifc.unam.mx; Tel.: +52-55-5622-5584; Fax: +52-55-5622-5611. Received: 10 January 2011; in revised form: 2 March 2011 / Accepted: 14 March 2011 / Published: 21 March 2011 Abstract: The cholesteryl-ester transfer protein (CETP) facilitates the transfer of cholesterol esters and triglycerides between lipoproteins in plasma where the critical site for its function is situated in the C-terminal domain. Our group has previously shown that this domain presents conformational changes in a non-lipid environment when the mutation D470N is introduced. Using a series of peptides derived from this C-terminal domain, the present study shows that these changes favor the induction of a secondary β-structure as characterized by spectroscopic analysis and fluorescence techniques. From this type of secondary structure, the formation of peptide aggregates and fibrillar structures with