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SUMMARY:Characterizing The Self-Assembly Of Hydrophobic Dipeptides
LOCATION:Chemistry A101
TZID:America/Denver
DTSTART:20191101T000000
UID:2026-04-28-23-15-50@natsci.colostate.edu
DTSTAMP:20260428T231550
Description:Research Seminar\nThe self-assembly of diphenylalanine (FF) int
 o macroscopic nanostructures has prompted a wide variety of potential appl
 ications to be proposed including use as a nanowire scaffold\, as a means 
 for drug delivery\, and as an antibacterial agent. These applications\, am
 ong others\, are predicated on the rational modification of FF to self-ass
 emble into an optimized structure for a given application. While previous 
 molecular simulations have been utilized to understand the underlying driv
 ing forces of FF self-assembly\, inconsistencies in models chosen as well 
 as a lack of quantitative analysis has resulted in conflicting conclusions
 . This presentation examines results from all-atom molecular dynamics simu
 lations at various points in the FF self-assembly process from dimerizatio
 n to nanotube growth. Using a free energy decomposition analysis in conjun
 ction with order quantification analyses\, we suggest initial aggregation 
 of FF is driven by backbone electrostatics\, where as solvent-mediated for
 ces drive FF nanotube growth. Since valine-phenylalanine (VF) and phenylal
 anine-valine (FV) have significantly reduced aggregation\, results highlig
 hting sequence dependence will then be presented. Using molecular dynamic 
 simulations of VF and FV monomers\, differences in monomer conformation co
 mbined with water dynamics are shown to have comparable rates to unassigne
 d experimental rates. These results are further supported by agreement in 
 calculated IR spectra using quantum mechanical techniques to experimental 
 IR spectra. 4:00 pm
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