CROSSLINKED DOMAINS OF APOA-I BUT NOT OF ΔK107 ARE INVOLVED IN rHDL´S SHAPE

DÍAZ LUDOVICO IVO; GONZALEZ MARINA CECILIA; GARDA, H. A.

La Plata

Congreso; XLVII Reunión Anual de la Sociedad Argentina de Biofísica; 2018

INIBIOLP-UNLP

Human apolipoprotein A-I (apoA-I) is the major proteincomponent of high-density lipoproteins (HDL) that plays a pivotal role in reversecholesterol transport. A natural mutant of apoA-I having a deletion of the singleresidue Lys107 (K) induces severe atherosclerosis. The structural and functionaleffects due to mutation are studied to elucidate the pro-atherogenicity of this variant. In this study, we investigate the structural effects of K107 deletion in a comparative approach with wild type (W) protein. Attending to structural alterations caused by deletion we have crosslinked with BS3 the lysine residues of both proteins in the native monomeric state (KBS3 and WBS3).