Self-assembly of Interfacially Confined Sheet Forming Peptides

Tu, Raymond

Title:

Self-assembly of Interfacially Confined Sheet Forming Peptides

dc.contributor.author	Tu, Raymond
dc.contributor.corporatename	Georgia Institute of Technology. School of Chemical and Biomolecular Engineering
dc.contributor.corporatename	City University of New York. City College
dc.date.accessioned	2010-05-18T21:21:11Z
dc.date.available	2010-05-18T21:21:11Z
dc.date.issued	2010-04-21
dc.description	Presented on April 21, 2010 from 4-5 pm in room G011 of the Molecular Science and Engineering Building on the Georgia Tech Campus.	en_US
dc.description	Runtime: 57:42 minutes
dc.description.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.	en_US
dc.format.extent	57:42 minutes
dc.identifier.uri	http://hdl.handle.net/1853/33061
dc.language.iso	en_US	en_US
dc.publisher	Georgia Institute of Technology	en_US
dc.relation.ispartofseries	School of Chemical and Biomolecular Engineering Seminar Series	en_US
dc.relation.ispartofseries	School of Chemical and Biomolecular Engineering Seminar Series
dc.subject	Materials processing	en_US
dc.subject	Nanotechnology	en_US
dc.subject	Peptide	en_US
dc.subject	Self-assembly	en_US
dc.title	Self-assembly of Interfacially Confined Sheet Forming Peptides	en_US
dc.type	Moving Image
dc.type.genre	Lecture
dspace.entity.type	Publication
local.contributor.corporatename	School of Chemical and Biomolecular Engineering
local.contributor.corporatename	College of Engineering
local.relation.ispartofseries	School of Chemical and Biomolecular Engineering Seminar Series
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relation.isOrgUnitOfPublication	7c022d60-21d5-497c-b552-95e489a06569
relation.isSeriesOfPublication	388050f3-0f40-4192-9168-e4b7de4367b4