Title:
Self-assembly of Interfacially Confined Sheet Forming Peptides
Self-assembly of Interfacially Confined Sheet Forming Peptides
Author(s)
Tu, Raymond
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Abstract
Periodically sequenced peptides can be confined to interfaces and assembled into patterns that
present chemical functionalities with exceptional spatial precision. The role of dynamics during
the assembly of these peptides appears to be very important for inorganic nucleation and growth.
Our work applies periodically sequenced sheet-forming peptides at interfaces to explore the
dynamics of assembly. The peptide molecules are rationally designed to have amphiphilic
properties and a propensity for sheet-like secondary structure. These designed peptides are
deposited at the air-water interface to explore the dynamics of self-assembly and investigate their
2D order. To characterize the phase behavior, we apply Langmuir Blodgett techniques and
Brewster angle microscopy. Thermodynamic analysis of structure formation with increasing
pressure allows us to understand the nature of self-assembly with iterative changes in the peptide
sequence. Additionally, we look at the dynamics of the self-assembled state, where the organic
phase switches between short- and long-range order as a function of surface pressure. This model
system allows us to explore our underlying hypothesis that the time scale of the confined peptide
phase-transitions defines the length-scale of the crystalline phase. This is in contrast to a system
that starts with a well-ordered preformed template that defines the mineral phase. We have
shown that our model peptides can effectively be used to control the polycrystallinity in gold by
controlling the surface pressure and diffusive time scales at the interface.
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Date Issued
2010-04-21
Extent
57:42 minutes
Resource Type
Moving Image
Resource Subtype
Lecture