Annual Report 2011 - Center for Advanced Biotechnology and ...

properties by lowering susceptibility to proteolysis. Typically, such modifications are
introduced in lead compounds by trial-and-error or combinatorial approaches.
Our laboratory is developing components in protCAD to simulate the impact of nonnatural
amino acids on structure and stability. Using fundamental principles of protein
design, we will pursue the computational, structure-based development of peptides
with variable chirality, broadly extending our capacity to create safe and potent
therapeutics.
Biochemical Basis of Food Allergies
A crucial and unanswered question in the field of food allergy research is why certain
proteins elicit an IgE mediated immune response, while others are tolerated. One
compelling model is that non-allergens are more digestible, resulting in sufficient
protein degradation in the stomach and intestine to render the remaining fragments
immunologically inert. In this project, we develop a highly defined system for
exploring the relationship between digestibility and allergenicity using engineered
variants of protein allergens from peanut and shrimp.
Natural collagens in the connective
tissue or the basement membrane
assemble in a hierarchic fashion.
Our peptides proceed from
monomer to trimer to fiber, and
finally to a hydrogel. Hydrogels are
versatile materials with applications
in drug delivery, tissue scaffolds
and enzyme immobilization. Insight
gained from this study will improve
molecular design of biomimetic
materials. TOP PICTURE: Phase
diagram of peptides CPB and CPC
combinations showing the diversity
of self-assembling structures
formed. BOTTOM PICTURE:
Electron Microscopy images of
negatively stained CPB:CPC
samples at various mixing ratios.
Mihir Joshi
Research Assistant
Kenneth
McGuinness
Research Asstistant
Yolanda Hom
Technician
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