Jennifer S. Laurence Ph.D
Associate Professor
Departments: Pharmaceutical Chemistry
Office: 2030 Becker Dr., MRB 320F
Phone: (785) 864-3405
Fax: (785) 864-5736

Educational Background:

Postdoctoral research, Biological Sciences, Purdue University, 2004
Ph.D., Chemistry, Purdue University, 2000
B.A., History, Miami University, 1994


Research Interests:

Mechanisms of Protein Stabilization
One of our primary interests is to better understand the relationship between intrinsic protein stability and extrinsic stabilization of a protein by its environment.  Protein therapeutics compose a fast growing segment of the drug pipeline because of their excellent specificity, which eliminates most side effects.  Proper formulation is, however, needed to ensure stability, which is critical for preserving a protein’s function during storage and for preventing the formation of aggregates, which can induce undesirable immune reactions.  

We utilize a variety of analytical, biochemical, and biophysical techniques to investigate how a protein’s stability is controlled by solution conditions1,2.  In order to assess the mechanism of stabilization, general structural stability is examined and site-specific information that indicates the positions at which a protein is affected by its environment is acquired.  Such detailed molecular information is obtained using high-field, multidimensional solution NMR.  The NMR data reveal structural and dynamic changes that occur to proteins under various solution and environmental conditions.

Targeted Delivery and Controlled Release of Therapeutic Metals
This research began with the discovery of a novel tripeptide-metal complex by our lab (patents pending), which we named the metal abstraction peptide (MAP).  MAP is able to rob a metal ion from a chelator and form an extraordinarily stable complex that is resistant to heat, light, and denaturants.  Release of the metal specifically occurs, however, upon acidification.  MAP is capable of binding a variety of metal ions, including nickel (Ni) and platinum (Pt). Two interesting chemistries result from formation of the Ni-MAP complex: 1) it mimics the catalytic antioxidant activity of Ni superoxide dismutase3 and 2) it undergoes site-specific chiral inversion at residues within the tag4.  

Platinum is one of the most widely used and potent anti-cancer drugs, but its high toxicity to normal cells limits dosing.  It has been generally asserted that attaching a drug to a protein that targets cancer cells would reduce general toxicity and improve efficacy.  Antibody-drug conjugates (ADCs) using organic compounds have recently been shown to improve outcomes while dramatically reducing side effects of chemotherapy.  Our peptide tag provides the first viable way to accomplish targeted delivery of platinum and other metals.  The chemical properties of the MAP complex are unique and highly compatible with its use as a tag for accomplishing targeted delivery and controlled release of metals in therapeutic and diagnostic applications.  MAP tag has several key benefits, including the ability to site-specifically encode the tripeptide sequence into any protein during its production to generate a homogeneous, single product. Moreover, the product is easily characterized and placement/copy number optimized for stability and potency.

Protein Adhesion to Polymers

Composite dental restorations are particularly vulnerable to decay at the gingival margin, where the dental adhesive provides the primary barrier between the tooth and oral environment. Adhesion of salivary proteins and cariogenic bacteria to surfaces in the mouth creates an environment that supports biofilm formation. While this biofilm cannot be eliminated, degradation of the dental reconstruction could be reduced by engineering novel anti-cariogenic dentin adhesives. In partnership with Dr. Spencer's lab in the Bioengineering Research Center, we are investigating a strategy to develop adhesives that (i) limit attachment of proteins and microbes to the adhesive polymer and (ii) neutralize the acidic micro-environment to prevent demineralization of the adjacent tooth structure. Our goal is to show how alterations in the chemistry of methacrylate-based adhesives will lead to predictable changes in material properties and to optimize features for in situ adhesive/dentin bond formation. We are generating and analyzing promising, new methacrylate-based adhesives for their ability to minimize protein attachment and neutralize the acidic micro-environment. These studies will facilitate understanding how the chemical composition of the adhesive polymer affects protein binding and microbial recruitment as well as the effect of biofilm formation on the longevity of dental composite reconstructions.


To see publications from the Laurence lab please visit:



The University of Kansas prohibits discrimination on the basis of race, color, ethnicity, religion, sex, national origin, age, ancestry, disability, status as a veteran, sexual orientation, marital status, parental status, gender identity, gender expression and genetic information in the University’s programs and activities. The following person has been designated to handle inquiries regarding the non-discrimination policies: Director of the Office of Institutional Opportunity and Access,, 1246 W. Campus Road, Room 153A, Lawrence, KS, 66045, (785)864-6414, 711 TTY.