(194o) Exploring the Potential Applications of Molecular Simulations to the Food Industry

Molecular dynamics simulations (MD) is the tool of choice for many researchers in their effort to investigate in atomistic (or near-atomistic) detail the structure, dynamic, or thermodynamic properties of biological and chemical systems. Employing MD in the food industry can produce a deep understanding of the structure-function relationship of the molecules of interest. Most of the application of MD to food-related problems revolves around the behavior of simple carbohydrates molecules in water and their interaction with proteins or other components. In this paper, we will discuss the impact that MD simulations could have in food research and, particularly, in Cargill. We will focus on two examples that show great potential for application to that area.

First, we studied the hydration properties of Scleroglucan (Sclg), which is a polysaccharide of D-glucose that is produced by fermentation of fungi. It consists of β-1,3 beta-glucans with β-1,6 branching. Sclg is quite an interesting molecule, as it has been shown to form a rod-like, triple helical structure, stabilized by both backbone hydrogen bonds at the center of the helix and side chain water bridges. Moreover, it has been suggested that multiple triple helices approach each other, creating sub-nanometer water channels between them that allow the permeation of small molecules only. We performed MD simulations to investigate the behavior of the helices and of the water surrounding them. We try to answer the questions regarding the stability of the triple helices and the impact they have on their environment.

Next, we discuss our work on elucidating the interaction between steviol glycosides with the bitter taste receptor that they bind to. There is an increasing demand for natural, zero-calorie sweeteners. Stevia is such a sweetener, extracted from leaves of the plant species Stevia rebaudiana, and it can be used as a sugar substitute. Stevia is a mixture of different components, with the most active being RebA, which is up to 150 times sweeter than sugar. Experimental studies have revealed that RebA binds to a specific bitter taste receptor that belongs to the GPCR group, which is a well-studied group of transmembrane proteins. We have employed structure-prediction methods and MD simulations to study the interactions that take place between the receptor and RebA. Our goal is to create a reliable model that can be used to explore the structure-activity relationship of RebA, and to potentially be able to predict the taste profiles of RebA analogues.