Proteins and Peptides

Date: March 23, 2023 2:00 pm (ET)


  • David Sabatino
    Carleton University
  • Raneem Akel
    Jumi Shin’s group

Dr. David Sabatino
Carleton University

Structure and Self-Assembly of Amphiphilic Cell-Targeting and Penetrating Peptides: Applications in RNA Delivery

Abstract: Peptides form an interesting class of simple, medium-sized tunable building blocks whose hydrophobic and hydrophilic (amphiphilic) nature, based on primary sequence composition, can have a profound impact on structure and self-assembly. Of specific interest, are the amphiphilic cell-targeting and penetrating peptides (CTPs and CPPs), armed with dual functionality for targeting selective receptor and cell types, while enabling membrane translocation and intracellular localization for biological activity. In our research, we are focused on the design and development of de novo CTPs and CPPs with structure and self-assembly profiles conducive of cell specific uptake for RNA delivery applications. Our RNA chemical biology approach is centered upon the short-interfering RNA (siRNA), that silence oncogenic mRNA expression leading to cancer cell death through the RNA interference (RNAi) pathway. Our target is based on the oncogenic Glucose Regulated Protein of 78 kilodalton (GRP78) that has been classified as a clinically relevant biological marker (bio-marker) in cancer detection and therapy. To potentiate siRNA therapeutic efficacy in cancer, we are applying synthetic CTPs and CPPs for siRNA assembly into nanoparticle formulations that enables delivery in selected cancer cell types for oncogene therapy activity. This presentation will serve to highlight the importance of structure and assembly of amphiphilic peptides for RNA delivery applicable to therapeutic oncology research.

Biography: Dr. David Sabatino was born and raised in Montreal, Quebec, Canada where he completed his B.Sc. (2002) and Ph.D. (2007) at McGill University in the area of nucleic acid biochemistry under the supervision of Professor Masad J. Damha.  As a research fellow, he completed his post-doctoral training with Professor William D. Lubell at the University of Montreal in 2010 developing new methods in the chemical synthesis of peptide mimics.

In September 2010, Dr. Sabatino joined the faculty at Seton Hall University where he served as Associate Professor and Director of Graduate Studies in the Department of Chemistry and Biochemistry. Dr. Sabatino was also appointed Adjunct Associate Professor in the Department of Medical Sciences at the Hackensack-Meridian School of Medicine where he participated in multiple research collaborations. Dr. Sabatino has instructed Nanotechnology, Biochemistry, Bio-Organic Chemistry, and General Chemistry courses to more than 500 students at the undergraduate and graduate levels. Moreover, Dr. Sabatino has mentored more than 50 students in his research lab, including 12 PhD and 5 MS students to completion. In January 2022, Dr. Sabatino joined the faculty at Carleton University where he is currently serving as Associate Professor in the Department of Chemistry and the Institute of Biochemistry.

Dr. Sabatino’s research spans the areas of nucleic acid and peptide chemical biology. More specifically, Dr. Sabatino’s research focuses on developing innovative bio-organic chemistry methods to produce synthetic biologicals for drug discovery applications. His research aims to explore the influence of structural modification on the anti-cancer activity of biological molecules for enhancing their therapeutic potential.

Dr. Sabatino is co-author of more than 40 peer-reviewed scientific publications, conference proceedings, patents and a book chapter. Dr. Sabatino has also co-authored more than 60 conference presentations at regional, national and international meetings. Dr. Sabatino has received funding from the NIH, NCI, CFI, Seton Hall and Carleton Universities for research related to the development of anti-cancer treatment strategies. His research accomplishments have also been recognized and awarded at the Dr. George Perez Research Colloquium in the Medical Sciences in 2016 and 2017 as well as being recently nominated Researcher of the Year in 2019 at Seton Hall University. Dr. Sabatino is also acting topics editor of Molecules and Frontiers in Chemistry-open access journals, is a current contributing member of the ACS, CSC/CCCE, APS and AAAS, and is co-organizing the upcoming nucleic acids symposium at the CSC 2023 meeting. He has also participated in the Chemical Biology steering committee at the New York and New Jersey Academy of Sciences. Dr Sabatino has been a proud sponsor of the ACS SEED program which engaged high school students from underprivileged communities to research in his lab. In an effort to broadly disseminate Science & Art instruction in underserved elementary schools, Dr Sabatino has also been involved in the Molecules of Life Project (


Raneem Akel
University of Toronto

Design of a Cross-species Orthogonal DNA-Binding Protein

Abstract: Synthetic biology, where an organism’s biological system is manipulated towards a particular purpose, has generated much excitement over the last decade. To obtain desired results, unwanted interactions with the host’s native functions must be avoided. Molecular elements from non-host organisms can be used to achieve orthogonality with the host’s own cellular elements. We combined bacterial and mammalian transcription-factor elements to design a DNA-binding protein orthogonal to any host system. Our structure is modeled after the homeodomain-leucine zipper (HD-Zip), a class of transcription factors unique to plants. By hybridizing mammalian and bacterial protein structures to create a frankenprotein modeled after the plant HD-Zip motif, we ensure that the combination of cross-species elements remains orthogonal to any synthetic biology system to regulate gene circuits more efficiently and effectively.

Biography: Raneem Akel completed her HBSc degree with high distinction at the University of Toronto in 2019. Double majoring in human biology and chemistry. To dive deeper into biological chemistry, she joined the Shin lab at the University of Toronto as a Ph.D. student to study the rational and irrational design of recombinant proteins.