Events

CBE/ENGR 225 Seminar Presents: Anne Skaja Robinson, Ph.D., Professor and Department Chair in the Department of Chemical and Bimolecular Engineering, The Catherine and Henry Boh Professor in Engineering, Tulane University

Tuesday, January 9, 2018, Elings Hall #1601

         Tuesday, January 9, 2018

Elings Hall #1601

2pm-3pm

*Light refreshments will be provided*

   Anne Skaja Robinson, Ph.D.
Professor and Department Chair
Department of Chemical and Biomolecular Engineering
The Catherine and Henry Boh Professor in Engineering
Tulane University

Host: Kevin Plaxco

 

Molecular and Cellular Engineering: Transforming Pharmaceuticals

and Understanding Disease Mechanisms

 

ABSTRACT: Proteins are vital biomolecules that do most of the critical functions in the body,

including structural roles, enzymatic activity, and regulation of metabolism, and

interactions between proteins and other biomolecules, including proteins, DNA, or lipids

are critical to development and homeostasis. In this talk, I will highlight two areas our

laboratory has been interested in – the adenosine receptor family and antibodies and

antibody fragments.

     The adenosine subfamily (A 1 R, A 2a R, A 2b R and A 3 R) of G-protein coupled receptors binds

the natural ligand adenosine, an important energy metabolite, has important biological

roles during cellular and organismal stress. In addition, adenosine receptors are also

therapeutic targets for Alzheimer’s disease, Parkinson’s disease, heart disease, among

others. The adenosine family has some promiscuity for binding adenosine analogs, yet

play opposite roles in many cases in activating downstream cellular pathways. To better

understand the relationship between sequence homology in this family and ligand binding

and activation, we created chimeric and truncated adenosine receptors. Using yeast as a

screening platform, we identified a unique role for the C-terminus in downstream

signaling that have implications in drug discovery.

      Monoclonal antibodies (mAbs) account for a large fraction of the biologics portfolio, and

in 2015 alone, global sales of the five best-selling mAbs (HUMIRA®, REMICADE®,

Rituxan®, Avastin®, and Herceptin®) for indications ranging from breast cancer, colon

cancer, Crohn’s disease to rheumatoid arthritis exceeded US $45 billion. The

glycosylated antibody has different sugar moieties (glycan isoforms) attached to a single

glycosylation site and the resulting heterogeneous glycan distribution influences the

stability, half-line, and pharmacokinetic properties of the mAb, and hence, the final drug

product quality. Thus, there is considerable interest in understanding glycosylation,

designing assays to characterize the glycan distribution, and developing strategies to

control the glycosylation profile. I will describe some of our laboratory efforts to

investigate these issues and approaches to solving them from bioreactor (macroscopic) to

 protein level.