Predicting ATP-Binding Cassette Transporters Using Rough Set and Random Forest Model

Predicting ATP-Binding Cassette Transporters Using Rough Set and Random Forest Model

Rudra Kalyan Nayak, Ramamani Tripathy
DOI: 10.4018/978-1-6684-6523-3.ch008
OnDemand:
(Individual Chapters)
Available
$37.50
No Current Special Offers
TOTAL SAVINGS: $37.50

Abstract

In reality, all homosapiens species benefit greatly from the function of ATP-binding cassette (ABC) transporter proteins. Many studies have focused specifically on the drug transporter prediction because to the recent advancements in biology. Machine learning and soft computing with data mining methodologies have been used to identify valid motif sequences from biological datasets in general. In this work, the authors analysed the research on the ABC transporter with the prediction of cellular cholesterol. This research is focused on this new area, as ABC transporters are frequently employed as pharmacological targets. In this instance, the authors have focused on the ABC transporter's legitimate signature motif involving plasma membrane cholesterol. The authors used an unique hybrid model that is rough set with random forest for the prediction of motif structure that has clinical significance for predicting relevant motif sequences.
Chapter Preview
Top

Introduction

Plasma Membrane

The membrane (Chauhan, 2003) that divides the interior of the cell from the external environment is found in all cells and is referred to as the plasma membrane or cell membrane. A cell wall is affixed to the plasma membrane on the exterior of bacterial and plant cells. A semi-permeable lipid bilayer makes up the plasma membrane. The movement of materials into and out of the cell is controlled by the plasma membrane (Oram, 2002).

Figure 1.

Structural components of Plasma membrane

978-1-6684-6523-3.ch008.f01

Every living thing, including prokaryotic and eukaryotic organisms (Paila et al., 2010), has a plasma membrane that encloses its internal contents and acts as a semi-porous barrier to the outer world. The membrane serves as a barrier, keeping the components of the cell together and preventing the entry of outside chemicals. However, the plasma membrane is permeable to particular molecules, enabling the entry of nutrients and other vital components as well as the exit of waste products from the cell. Small molecules can move freely over the membrane, including oxygen, carbon dioxide, and water, but the movement of bigger molecules, such amino acids and carbohydrates, is strictly controlled.

Prokaryotic and Eukaryotic

The plasma membrane is an inner layer of protection in prokaryotes and plants because a stiff cell wall serves as the outer limit for their cells. Although the pores in the cell wall allow materials to enter and exit the cell, they are not particularly picky about what gets through. The final barrier between the inside of the cell and the outside world is the plasma membrane, which borders the cell wall.

It is generally accepted that eukaryotic animal cells are related to prokaryotes that shed their cell walls. These early organisms would have been able to grow in size and complexity because there would just be the pliable plasma membrane left to confine them. Eukaryotic cells contain membranes that enclose their internal organelles and are typically ten times bigger than prokaryotic cells. These membranes control material flow similarly to the external plasma membrane, enabling the cell to divide its chemical processes into distinct interior compartments.

Transporter

By facilitating the translocation of solutes such as ions, nutrients, neurotransmitters, and a variety of medications across biological membranes, membrane transport proteins perform a crucial job in every live cell. They play a critical part in the success or failure of cancer treatment, and their (mal)function is directly linked to a variety of illnesses, such as autism, epilepsy, migraine, depression, drug misuse, and cystic fibrosis. For target-oriented drug discovery and delivery, they are therefore of primary medical/pharmacological interest. On a regular basis, their activity is investigated in appropriate expression hosts and, if practical, after reconstitution into proteoliposomes. However, to do direct biophysical and structural analyses, including crystallisation, these integral membrane proteins must first be dissolved and purified, as shown in Figures 1 and 2. The absence of a vectorial environment prevents the measurement of transport activity between their extraction from the membrane and restoration. Because of this, studies to determine their role in detergent have been restricted to indirect binding methods, such as protecting substrates from cysteine modification or detecting tryptophan fluorescence changes caused by the substrate. These methods necessitate the fortuitous or engineered localization of cysteines or tryptophans as well as time-consuming development and implementation.

Complete Chapter List

Search this Book:
Reset