Biophysical Society Newsletter | September 2017

4

2017

BIOPHYSICAL SOCIETY NEWSLETTER

SEPTEMBER

advisor, and there was lack of mentorship,” she says. “In both cases, I had to take a risk by moving on. Both times, it was an extremely scary deci- sion to make but God worked it for my good in the end. I finally ended up in the Fanucci group, and it was all worth it. I had the perfect mentor and work that aligned with my interests. I grew exponentially thanks to that match.” Biophysics was a great fit for her, too. “Biophys- ics makes sense,” she says. “It provides you with tangible explanations of how biological systems are able to function. It assembles the puzzle with such a versatile range of tools, and to me exempli- fies just how important it is to combine different fields in tackling important questions.” Following completion of her PhD studies in 2014, Braide-Moncoeur began at Gordon Col- lege, a primarily undergraduate institution in northeastern Massachusetts, as assistant professor of chemistry. Her lab works on furthering the mechanistic understanding

to reduce surface tension and closely associates with lipids in the bulk phase of liquid below alveoli surface film (hypophase). As SP-B is highly hydrophobic and structurally complex, challenges in synthesis and expression of a functionally active recombinant have led to increased efforts to use synthetic alternatives in developing novel thera- peutics for RDS treatment, and to elucidate the mechanism of function.” Braide-Moncoeur continues, “Despite several advances in elucidating structural properties of the synthetic surfactant peptides, molecular level in- formation is still pertinent to understanding how it moderates surface tension reduction and inter- facial film fluidity in the alveoli, and to elucidate the mechanism by which lipid trafficking occurs.” The goal of the project is to further understanding of fundamental membrane-protein interactions and of specific LS component functions, using fluorescence spectroscopy to study localized envi- ronmental changes in fluidity and lipid dynamics. At an institution focused on teaching, it can be a challenge for Braide-Moncoeur to stay current and active in scientific research, but seeing her students develop an enthusiasm for research is hugely grati- fying. “[The most rewarding aspect of my work] is seeing the passion that develops in research stu- dents as their work begins to make sense to them,” she says. “They become so motivated and actually look forward to sharing their progress in various settings — local research symposia, conferences, etc.” “I am grateful to be able to have a position in academia because it combines my interests in teaching and research but I would also like to play a more active role in mentorship of students within the STEM field beyond my current place of employment. I believe there is a need for it,” she shares. “As for my contribution to biophysics, I am hopeful that I can continue adding clarifying pieces to the puzzle of understanding. Our world is complex and fascinating: it is worth studying.”

Braide-Moncoeur with her husband Ronald and son Nathan.

“ [Biophysics] exemplifies just how important it is to combine different fields in tackling important questions ” — Braide-Moncoeur

of pulmonary surfactant at the membrane-fluid in- terface. “Premature infants with underdeveloped lungs typically develop respiratory distress syndrome (RDS) because their lungs lack the surfactant lining crucial for

oxygen absorption or have genetically failed to produce critical components of lung surfactant (LS) needed for proper function. LS is a complex mixture of lipids and proteins known to provide a protective barrier against inhaled pathogens, lower alveolar surface tension, and promote oxygen exchange. The functional significance of LS is clear; however, a detailed mechanistic understand- ing of how lipids are trafficked to and from the air-fluid interface for oxygen absorption remains unknown,” she explains. “Though the bulk of LS is made up of lipids (~90%), it is non-functional without the presence of surfactant proteins (SP-A, B, C, and D), especially SP-B, which is known