Role of sphingomyelin in membrane-domain formation and the influence on protein interaction: focussing on the nanometer scale.

SABINA M. MATÉ; VANESA S. HERLAX; ROMINA F. VAZQUEZ; LAURA BAKÁS

Membrane organization and lipid rafts in the cell and artificial membranes

NOVA SCIENCE PUBLISHERS, INC.

Año: 2016; p. 89 - 112

The advent of novel experimental techniques based on physical principles opens a window to the nanometer world facilitating a renewed and detailed study of membranes. These specific techniques enable an understanding of how biologic-membrane functioning is related to membrane physical properties on various scales of time and dimension.A preferential interaction between sphingomyelin (SM) and cholesterol (Cho) in both cell and model membranes has been proposed as a key influence on the formation of Cho- and SM-rich membrane domains. This chapter provides insights into the lateral structure and molecular organization of lipid membranes on the nanometer scale. We focus on how the specific molecular structure of SM affects the lateral behavior and physical properties of both model and natural membranes.In addition, the lateral structure controls the mechanical properties of the membrane and thereby protein-membrane interactions. Many proteins, targeted to membrane microdomains by favorable associations with ordered lipids, are linked to the saturated acyl chains that partition well into these domains. This chapter shows, on the nanometer scale, the interaction with membranes of -hemolysin (HlyA), an acylated protein.