supported membrane

Biological Physics

Supramolecular Structures Lab
Lösche Group

www.cmu.edu
 
     

Supramolecular Structures Lab

Ordered molecular assemblies form the structural basis of life. Their length scales range from nanometers, the thickness of a biomembrane, to micrometers, the length of polymers that form the cytoskeleton. They are chemically diverse – building blocks include proteins, nucleic acids, lipids and polysaccharides – and formidably complex.

As are the underlying interactions: Van-der-Waals, electrostatic, hydrogen bonding and hydrophobic forces all contribute to their specific organization. Since these interactions are characterized by thermal energies, the resulting structures are highly dynamic, capable of reorganizing in response to a changing environment.

We are particularly interested in biomembranes and membrane-related biological processes. For example, many toxins exert their damage on target cells by interfering with membrane functions. Misfolded peptides affect membranes of neuronal cells so that the communication between these cells is abolished; diseases such as Alzheimer's or Parkinson's are the consequence. As a further example, viral assembly, such as that of the Human Immunodeficiency Virus occurs at the plasma membrane of host cells and is a complex process involving specific interactions between proteins, viral nucleic acid and specific membrane components, which is poorly understood.


Traditional biological tools have been invaluable in identifying the molecular components of biomolecular assemblies and determining their qualitative functions. Yet, an integrated understanding of the underlying mechanisms and principles, as well as their dynamic function is largely incomplete.

Physics contributes to this understanding on many levels, from providing a theoretical framework for the quantitative description of Soft Condensed Matter to providing experimental characterization tools for probing the dynamics of function, assembly and disassembly. Progress in the understanding of supramolecular complexes will impact science and technology areas far beyond biology. Already to date it exerts a significant impact on materials engineering and biotechnology, and is likely to extend into areas yet unforeseen.

 

News

 

April 2009

Tristan Bereau wins Guy C. Berry Graduate Research Award. In 2009, the Berry Award, recognizing excellence in research performed by MCS graduate students, goes to Tristan for his development of coarse-grained peptide models. Tristan performs his research under the guidance of Markus Deserno.

April 2009

Prof. Alex Evilevitch of Lund University in Sweden accepted the offer to join the Biological Physics group at the Carnegie Mellon Physics Department.

Alex made a name in experimental research on viral genome packing, viral assembly and the molecular details of infection mechanisms of bacteriophages. Among various honors, he was awarded the 2008 Hagbergs Prize of the Swedish Royal Academy for his ground-breaking research in virus biophysics. He is currently a Lecturer and Associate Professor in Lund's Dept. of Biochemistry and will join CMU in June, 2009. More ...

January 2009

An NIH Program Grant (1 P01 AG032131) is awarded to the Lösche / Deserno / Valincius / Hall and Glabe collaboration. For the next 3 years, the collaboration is funded to study the imact of Amyloid-β on membranes.

December 2008

Study on the molecular origins of membrane damage by soluble oligomers of the Alzheimer's peptide amyloid β appears in the Biophysical Journal. This work is a collaboration with the Valincius lab in Vilnius (Lithuania) and with Jim Hall's lab at UC Irvine. Electrochemical Impedance Spectroscopy and Neutron Reflection on tethered bilayers suggest that the membrane damage inferred by Aβ is different from that inferred by the membrane pore, α-hemolysin.
Read more: Valincius et al., Biophys. J. 95 (2008), 4845.

News Archive ...

Contact

SMSL, c/o Donna Thomas
Physics Department
Wean Hall
5000 Forbes Ave
Pittsburgh PA 15213
USA

Tel. 412-268-8367
Fax 412-268-8252

We are a member of the joint UPSM-CMU MBSB graduate program.