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Secondary structure of the particle associating domain of apolipoprotein B-100 in low-density lipoprotein by attenuated total reflection infrared spectroscopy.

par Goormaghtigh, Erik ;Cabiaux, Véronique ;De Meutter, J;Rosseneu, Maryvonne;Ruysschaert, Jean Marie
Référence Biochemistry, 32, 23, page (6104-6110)
Publication Publié, 1993-06

Article révisé par les pairs

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Résumé :

The secondary structure of the human low-density lipoprotein (LDL) apo B-100 fragment embedded in the lipid domain of the particle has been investigated by Fourier transform attenuated total reflection infrared spectroscopy (FTIR-ATR). The solvent-exposed region of the protein was hydrolyzed by using different proteases (alpha-chymotrypsin, trypsin, proteinase K) for incubation times varying between 24 min and 48 h. Analysis of the FTIR-ATR spectra after repurification of the digested LDL particle indicates the same trend for all the hydrolysis conditions tested: the peptides remaining associated with the particle are rich in beta-sheet structure. Dichroism spectra reveal that at least part of the beta-sheets is associated with the phospholipid component of the particle.