Solution structures of casein peptides: NMR, FTIR, CD, and molecular modeling studies of alpha(s1)-casein, 1-23: NMR, FTIR, CD, and molecular modeling studies of α_s1-casein, 1-23

To determine its potential for interacting with other components of the casein micelle, the N-terminal section of bovine α_s1-casein-B, residues 1-23, was investigated with nuclear magnetic resonance (NMR), Fourier transform infrared (FTIR) and circular dichroism (CD) spectroscopies, and molecular modeling. NMR data were not consistent with conventional α-helical or β-sheet structures, but changes in N-H proton chemical shifts suggested thermostable structures. Both CD and FTIR predicted a range of secondary structures for the peptide (30-40% turns, 25-30% extended) that were highly stable from 5°C to 25°C. Other conformational elements, such as loops and polyproline II helix, were indicated by FTIR only. Molecular dynamics simulation of the peptide predicted 32% turns and 27% extended, in agreement with FTIR and CD predictions and consistent with NMR data. This information is interpreted in accord with recent spectroscopic evidence regarding the nature of unordered conformations, leading to a possible role of α_s1-casein (1-23) in facilitating casein-casein interactions.