RIENSTRA GROUP
 
UNIVERSITY OF ILLINOIS
 
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AGNIESZKA LEWANDOWSKA

Research Scientist

Office: A127A Chemical and Life Sciences Lab (CLSL)
Phone: (217) 244-1583

E-mail:alewando_at_illinois.edu


 

education

Postdoctoral Fellow, advised by Prof. Victor Muñoz, Centro National de Biotechnología (CNB-CSIC), Madrid, Spain (2015)
Postdoctoral Fellow, advised by Prof. Heinrich Roder, Fox Chase Cancer Center (FCCC), Philadelphia, PA (2010)
Ph.D. Chemistry, University of Gdansk, Gdansk, Poland (2009)
M.Sc. Chemistry, University of Gdansk, Gdansk, Poland (2004)
 

research interests

My research interests fall mainly within the areas of protein structure, folding and dynamics as well as antifungal drugs/membrane interactions.

During my PhD program, I studied the protein folding mechanism by NMR-based and temperature-dependent conformational studies of protein fragments by means of different spectroscopic methods, such as circular dichroism spectroscopy (CD), Fourier transform infrared (FT-IR) spectroscopy, differential scanning calorimetry (DSC), and nuclear magnetic resonance spectroscopy (NMR). As a result of these studies I presented mechanism of formation of the C-terminal beta-hairpin of the B3 domain of the immunoglobulin binding protein G from Streptococcus as well as proposed the most possible mechanisms of folding of the B3 domain that gave a better understanding of the forces driving the folding of proteins.

As a Postdoctoral Associate at Fox Chase Cancer Center (FCCC) in Philadelphia, I worked on conformational and dynamic properties of an intrinsically disordered region of a multidomain protein (NHERF1) by means of different spectroscopic methods, such as CD, Fluorescence and paramagnetic relaxation enhancement (PRE-NMR) experiments. These studies provided more detailed information on the conformational properties and dynamics of the intrinsically disordered regions of NHERF1, which is critical for understanding its function as a molecular switch in cancer-related cell signaling.

As part of my Postdoctoral work at the National Center of Biotechnology (CNB-CSIC) in Madrid, Spain, I have been involved in two projects: 1. Investigating the equilibrium unfolding behavior of the small all-beta protein WW (FBP11WW1 domain) at atomic resolution using nuclear magnetic resonance (NMR), and 2. Studying the conformational rheostat concept in protein functional regulation as complement to conventional conformational switches in one of the biological processes that involve complex protein conformational behavior; namely: upon binding to multiple structurally-diverse partners.

Currently, my research focuses on the mode of action of the clinically vital but also highly toxic antifungal drug Amphotericin B (AmB). AmB forms large extramembranous aggregates that extract sterols from lipid bilayers and thereby kill cells. My goal is to determine the structure of the complexes of the AmB sponge with ergosterol and cholesterol by employing solution NMR as well as other spectroscopic methods.

 

 

Selected honors and awards

  • Fellowship for young researchers from the Foundation for the Development of Gdansk University, 2010
  • Scholarship for academic performance from the Polish Ministry of Higher Education and Science, 2007
  • The best poster among those presented by young scientists during the 18th Polish Peptide Symposium in Wrocɫaw (A. Lewandowska, S. Rodziewicz-Motowidlo, S. Oldziej, W. Wiczk, A. Liwo, “Conformational studies of short peptides corresponding to secondary-structure elements of proteins”) acknowledged by participants of the symposium and the Symposium Scientific Committee, 2005
  • Distinction for the best Master Thesis from the Gdansk division of the Polish Chemical Society, 2004
  • The scholarship of Koscierzyna’s Mayor, 2004
  • Rector Prize for winning the University elimination for VIII Competition of Procter & Gamble Poland for the Best Graduate of Higher Education, 2004
  • Rector Prize for academic performance, 2003

 

 

Selected Publications

"A Maximum-Likelihood Approach to Force-Field Calibration", Zaborowski B., Jagiela D., Czaplewski C., Halabis A., Lewandowska A., Zmudzinska W., Oldziej S., Karczynska A., Omieczynski C., Wirecki T., Liwo A.J. Chem. Inf. Model, 2015, 55, 2050-2070 (Published online, Aug 11, 2015).

β-hairpin-forming peptides; models of early stages of protein folding", Lewandowska A., Oɫdziej S., Liwo A., Scheraga H.A. Biophys. Chem., 2010, 151, 1-9 (Published online, May 6, 2010).

"Mechanism of formation of the C-terminal β-hairpin of the B3 domain of the immunoglobulin binding protein G from Streptococcus. Part IV. Implication for the mechanism of folding of the parent protein.", Lewandowska A. , Oɫdziej S., Liwo A., Scheraga H.A.,Biopolymers, 2010, 93, 469-480 (Published online, May 2010).

"Mechanism of formation of the C-terminal β-hairpin of the B3 domain of the immunoglobulin binding protein G from Streptococcus. Part III. Dynamics of long-range hydrophobic interactions.", Lewandowska A. , Oɫdziej S., Liwo A., Scheraga H.A.,Proteins Struct. Funct. Bioinform, 2009, 78, (Published online, February 15, 2010).

"Mechanism of formation of the C-terminal β-hairpin of the B3 domain of the immunoglobulin binding protein G from Streptococcus. Part I. Importance of hydrophobic interactions in stabilization of β-hairpin structure.", Skwierawska A., Makowska J., Oɫdziej S., Liwo A., Scheraga H.A.,Proteins Struct. Funct. Bioinform, 2009, 75, 931-953, (Published online, June 2009).

"Conformational studies of the C-terminal 16-amino-acid-residue fragment of the B3 domain of the immunoglobulin binding protein G from Streptococcus.", Skwierawska A., Oɫdziej S., Liwo A., Scheraga H.A.,Biopolymers, 2009, 91, 37-51, (Published online, January 2009).

"Conformational studies of the alpha-helical 28-43 fragment of the B3 domain of the immunoglobulin binding protein G from Streptococcus.", Skwierawska A., Rodziewicz-Motowidɫo S.; Oɫdziej S., Liwo A., Scheraga H.A.,Biopolymers, 2008, 89, 1032-1044, (Published online, November 2008).