CBI Alumni


Alumni Research Description

Rebecca Adamek

Rebecca Adamek 
Cohen Lab

CBI Trainee: 2015-17

New Delhi Metallo-ß-lactamase (NDM-1) is a metallo-ß-lactamase that confers bacterial resistance to ß-lactam antibiotics through the hydrolysis of the ß-lactam bond that is vital to the activity of this class of therapeutics. The goal of my research is to develop potent inhibitors of NDM-1 that restore ß-lactam activity against resistant bacteria. In order to meet this goal, metal binding pharmacophore (MBP) fragment libraries have been screened against NDM-1. This screen revealed 8-hydroxyquinoline analogs, 5-chloro-8-hydroxyquinoline and 2-carboxyl-8-hydroxyquinoline, as well as substituted 1,2-HOPTOs, as novel scaffolds for the development of NDM-1 inhibitors. Based on these results from the MBP fragment screening, my research is focused on derivatizing the 8-hydroxyquinoline and 1,2-HOPTO scaffolds in a fragment growth strategy, in order to discover potent and effective NDM-1 inhibitors.

 

 

Thomas Bartholow

Thomas Bartholow 
Burkart Lab

CBI Trainee: 2015-17

The Fatty acid biosynthetic (FAS) pathway functions through an iterative mechanism, using sequential conserved chemistries to efficiently and specifically build the fatty acids required for life. The acyl carrier protein (ACP) shuttles fatty acid chains as they are modified, facilitating each reaction and protecting the acyl chain. My research is focused on understanding the structure and dynamics of this pathway and ACPs interaction with its wide range of partner enzymes. Using NMR and crystallography I aim to characterize the interactions between ACP and partner enzymes which confer specific and efficient biosynthesis.

 


Naneki Collins

Naneki Collins  
Gianneschi Lab

CBI Trainee: 2015-17

My research is focused on using ring-opening metathesis polymerization (ROMP) to create self-assembled polymeric nanoparticles for the delivery of peptide targeted, platinum cancer therapeutics. I am also interested in developing degradable polymeric materials for drug delivery and other applications.

 

 


Ashley Kroll

Ashley Kroll 
Zhang Lab

CBI Trainee: 2015-16

My current research project aims to develop the cancer cell membrane-coated nanoparticle (CCNP) platform as an anticancer vaccine. Cancer immunotherapy works to modulate the immune system to overcome immune evasion mechanisms and elicit a specific antitumor immune response through methods such as vaccination and checkpoint blockades. One way that cancer cells are able to evade the immune system is due to their low immunogenicity. Vaccination strategies increase tumor immunogenicity by priming the immune system to specifically identify tumor cells as foreign and launch a destructive immune response. My current research project aims to address two main hurdles to cancer vaccine development—antigen selection and adjuvant co-delivery—using nanoparticle properties.

 

 


Rohit Subramanian

Rohit Subramanian
Tezcan Lab -

CBI Trainee: 2015-16


The self-assembly of proteins into higher order materials is a promising route for the development of new nanotechnologies. Crystalline protein lattices have the unique advantage of merging solution-state protein functionality with the dense packing of particles in a defined manner. Our research uses enzymes to selectively modulate semi-synthetic, crystalline protein and peptide arrays. Manipulating protein arrays via enzymatically driven reactions closely mirrors the processes of living cells and enables us to better understand natural design principles for functional supermolecular protein architectures. We use a minimized peptide sequence, labeled ybbR, to serve as a functional peptide tag on the surface of protein biomaterials. Arrays displaying the peptide can be readily modified using phosphopantetheinyl transferases and coenzyme A (CoA) analogues to covalently attach a functional biomolecule onto the ybbR peptide. The freedom to chemically modify CoA provides the means to enzymatically transfer a variety of biomolecules and functional organics to protein materials. The addition of this enzyme-directed functionality affords complex modularity to the protein assembly platform and allows us to study the selective labeling of protein superstructures.

CBI Trainees