Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 119, Issue 29, Pages 9038-9048Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jp508473w
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Funding
- National Science Foundation (NSF) [CHE-1306386]
- NASA Earth and Space Science Graduate Fellowship
- CIRES Graduate Fellowship
- CU Chemistry Department
- NIH/CU Molecular Biophysics Training Program
- NSF CAICE Grant [45345218]
- Czech Science Foundation [13-06181S]
- RVO [61388963]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1306386] Funding Source: National Science Foundation
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The interaction of L-phenylalanine with a 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) monolayer at the air-water interface was explored using a combination of experimental techniques and molecular dynamics (MD) simulations. By means of Langmuir trough methods and Brewster angle microscopy, L-phenylalanine was shown to significantly alter the interfacial tension and the surface domain morphology of the DPPC film. In addition, confocal microscopy was used to explore the aggregation state of L-phenylalanine in the bulk aqueous phase. Finally, MD simulations were performed to gain molecular-level information on the interactions of L-phenylalanine and DPPC at the interface. Taken together, these results show that L-phenylalanine intercalates into a DPPC film at the air-water interface, thereby affecting the surface tension, phase morphology, and ordering of the DPPC film. The results are discussed in the context of biological systems and the mechanism of diseases such as phenylketonuria.
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