SCIENCE AT THE EDGE SEMINAR
http://www.pa.msu.edu/seminars/edge/

Friday, October 4, 2002
11:30 a.m., Room 1400 Biomedical and Physical Sciences Building
Refreshments served at 11:15 in Room 1400A BPS

Title:
    CREATING FUNCTIONAL BIOMOLECULAR ARCHITECTURES AT INTERFACES

Speaker:
    Matthew Tirrell
    Departments of Chemical Engineering and Materials
    University of California
    Santa Barbara, CA 93106

Abstract:
Short peptide sequences, derived from whole proteins, can be useful
synthetic agents for conferring a specific biological function to a material
surface.  Their ability to do this depends on delivering them to the surface
in a biologically recognizable form, that is in a spatial configuration that
is not too different from that adopted by the peptide in the whole protein.
Most functional proteins have secondary and tertiary levels of structure
that are essential to their activities; peptides have simpler but no less
important structures.  In our work, we have focussed on peptides derived
from extracellular matrix proteins.  We have found that attaching synthetic
lipid tails to peptides fragments gives them two very useful properties for
surface modification.  The hydrophobic tails give rise to a self-assembly
capacity enabling these molecules to organize into membrane, monolayer and
bilayer structures.  Less expected is that this level of self-assembly
induces a second level in the peptide headgroup. Peptides from alpha-helical
and triple-helical regions of protein are induced by the lipid tails to form
protein-like secondary structures and therefore to have more effective
biological activity.