SECONDARY STRUCTURE OF THE PARTICLE ASSOCIATING DOMAIN OF APOLIPOPROTEIN-B-100 IN LOW-DENSITY-LIPOPROTEIN BY ATTENUATED TOTAL-REFLECTION INFRARED-SPECTROSCOPY
E. Goormaghtigh et al., SECONDARY STRUCTURE OF THE PARTICLE ASSOCIATING DOMAIN OF APOLIPOPROTEIN-B-100 IN LOW-DENSITY-LIPOPROTEIN BY ATTENUATED TOTAL-REFLECTION INFRARED-SPECTROSCOPY, Biochemistry, 32(23), 1993, pp. 6104-6110
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 wa
s 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 condition
s 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 th
e particle.