TY - JOUR
T1 - Relationship between the mobility of phosphocholine headgroup and the protein-liposome interaction
T2 - A dielectric spectroscopic study
AU - Shimanouchi, Toshinori
AU - Yoshimoto, Noriko
AU - Hiroiwa, Azusa
AU - Nishiyama, Keiichi
AU - Hayashi, Keita
AU - Umakoshi, Hiroshi
N1 - Funding Information:
The fundamental concept of this study was supported by the Research Group of “Membrane Stress Biotechnology” and the Sigma Multidisciplinary Research Laboratory Group (Grad. Sc. of Engineering Science, Osaka University) “Membranomics”. It was partly funded by a Cabinet Office, Government of Japan through its “ Funding Program for Next Generation World-Leading Researchers ” ( No. GR066 ), Grants-in-Aid for Scientific Research ( Nos. 23656525 and 24686086 ) from the Ministry of Education, Science, Sports, and Culture of Japan (MEXT) . It was also funded by the Okawa foundation (12-07) .
PY - 2014/4/1
Y1 - 2014/4/1
N2 - Proteins could affect the headgroup mobility of phospholipid within liposome membranes through the protein-liposome interaction. The variation of headgroup mobility of phospholipid was then investigated by using the dielectric dispersion analysis. The eight proteins (Mw=4.2-28.7kDa) were used to investigate the protein-liposome interaction. It has been revealed that the strength of the protein-liposome interaction at 25°C was linearly correlated with the stability of intramolecular hydrogen bondings of proteins, better than with their hydrophobicity and the surface charge density. Overall, liposomes composed of binary lipid system, appeared to strongly interact with proteins, in contrast to liposomes composed of single, ternary, and quaternary lipid systems. This is probably because liposomes composed of binary lipid system favored to form the microscopic environment where proteins could interact. The present result suggested the heterogeneous phase state of lipid membranes was one of dominant factors for the interaction between proteins and lipid membranes.
AB - Proteins could affect the headgroup mobility of phospholipid within liposome membranes through the protein-liposome interaction. The variation of headgroup mobility of phospholipid was then investigated by using the dielectric dispersion analysis. The eight proteins (Mw=4.2-28.7kDa) were used to investigate the protein-liposome interaction. It has been revealed that the strength of the protein-liposome interaction at 25°C was linearly correlated with the stability of intramolecular hydrogen bondings of proteins, better than with their hydrophobicity and the surface charge density. Overall, liposomes composed of binary lipid system, appeared to strongly interact with proteins, in contrast to liposomes composed of single, ternary, and quaternary lipid systems. This is probably because liposomes composed of binary lipid system favored to form the microscopic environment where proteins could interact. The present result suggested the heterogeneous phase state of lipid membranes was one of dominant factors for the interaction between proteins and lipid membranes.
KW - Hydrogen bond
KW - Lipid composition
KW - Liposome
KW - Protein
UR - http://www.scopus.com/inward/record.url?scp=84893872356&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84893872356&partnerID=8YFLogxK
U2 - 10.1016/j.colsurfb.2013.07.028
DO - 10.1016/j.colsurfb.2013.07.028
M3 - Article
C2 - 24524935
AN - SCOPUS:84893872356
SN - 0927-7765
VL - 116
SP - 343
EP - 350
JO - Colloids and Surfaces B: Biointerfaces
JF - Colloids and Surfaces B: Biointerfaces
ER -