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SUMMARY:The Role of Hydrophobicity in the Stability and pH-Switchability of
  (RXDX)4 and Coumarin-(RXDX)4 ?-sheet Fibers
LOCATION:Chemistry A101
TZID:America/Denver
DTSTART:20191201T000000
UID:2026-04-16-20-00-00@natsci.colostate.edu
DTSTAMP:20260416T200000
Description:Research Seminar\nCoumarin–peptide derivatives are ideal for 
 the design of switchable self-assembling biomaterials with applications in
  nanoelectronics. We probe the role of hydrophobicity and aromaticity in t
 he stability and pH-switchability of (RXDX)4 fibers using molecular dynami
 c simulations. Furthermore\, we study the effect of mutating a single hydr
 ophobic residue in the (RXDX)4 to an unnatural coumarin amino acid. Using 
 a variety of peptide and coumarin order metrics\, we show the hydrophobici
 ty of the peptide sequence changes fiber stability and pH-switchability in
  both (RXDX)4 and coumarin-(RXDX)4 fibers. Increasing hydrophobicity leads
  to increased fiber stability at both neutral and acidic pH and a reductio
 n in pH switchability of (RXDX)4 fibers. These trends are consistent for (
 RXDX)4-coumarin fibers with subtle differences due to the addition of coum
 arin. Our work suggests that we can use hydrophobicity to tune the pH-swit
 chability of the optical properties of coumarin-(RXDX)4 fibers. 4:00 pm
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