Name: Dr Abraham Olusegun Oluwole
I grew up and had my basic education in Ogbomoso, south-west Nigeria. Chemistry happened to be one of my favourite subjects in high school; I was always fascinated by those colour-change, heat-change transformations. I wanted to know why, how, and possibly do the same. I received B. Tech. Chemistry (first class) from Ladoke Akintola University of Technology, Ogbomoso and subsequently obtained an M.Sc. and Ph.D. in Physical Chemistry from the University of Ibadan, Ibadan.
My journey into studying biological systems began with my master’s project in the lab of Prof. Jonathan Babalola where I investigated the kinetics and thermodynamics of ligand binding to haemoglobin. Initially, I planned to study drug-protein interactions for my Ph.D. until I discovered the huge significance of membrane-anchored proteins as drug targets and the associated difficulty of handling them in vitro. Fortunately, I got a Ph.D. scholarship from the German Academic Exchange Services to investigate interactions of membrane proteins and lipids with amphiphilic polymers in the lab of Prof. Dr. Sandro Keller at the University of Kaiserslautern, Germany. We were the first to produce diisobutylene/maleic acid lipid particles (DIBMALPs), a kind of “native nanodiscs” that allows investigations of membrane proteins by a wider range of biophysical techniques, particularly far-UV CD spectroscopy. Later, I wondered whether our “native nanodiscs” are amenable to native mass spectrometry, an established technique for investigating membrane proteins released from detergent micelles in the gas phase. The pioneering works and expertise of Prof. Carol Robinson group in this field attracted me to join Oxford as a postdoctoral research associate in 2018.
My current project aims to employ the “native nanodiscs” approach to capture membrane-bound transporters and channels along with their endogenous ligands, and analyse these complexes by native mass spectrometry. Coupling native mass spectrometry with native nanodiscs technology will ease off the bottleneck of poor stability of membrane proteins and foster high-throughput identification of endogenous metabolites and development of new membrane protein-targeting therapeutics.
Membrane proteins are the major components of biological membranes and mediate several functions and dysfunctions of cells. However, they are difficult to study mainly because of their insolubility in biological buffers. Detergents are currently used to overcome the problem of insolubility, but potential denaturing effect of detergents remains a challenge. Amphiphilic polymers such as SMA and DIBMA are the emerging alternatives, being able to solubilise cell membranes into “native nanodiscs” whereby the targeted protein is embedded within its own native lipid bilayer. Native mass spectrometry is ideal for investigating such macromolecular complexes. We hope to learn how endogenous ligands or external agents such as drug molecules interact with membrane protein while the latter is maintained within its own native lipid environment. Being a Chemistry major, my current project affords me the opportunity to learn various applications of native mass spectrometry as well as basic techniques in molecular biology.
A little bit extra
I enjoy an arsenal of museums and historic sites in Oxford, and I am thrilled to work where several scientific breakthroughs were - and are - being made. I hope my future will revolve around scientific research, writing, engaging the public with scientific discourse, and education policies.