Welcome to Milan Mrksich's Group and the
Laboratory for BioInterface Science and Engineering
My group’s interests overlap
chemistry, biology and engineering, with an emphasis on the design and
synthesis of materials that are biologically active and in applications
of the materials to relevant problems in the biological and medical
sciences. Much of our work uses self-assembled monolayers of
alkanethiolates on gold to prepare model surfaces that are structurally
defined, yet that can have complex compositions and present the
ligands in spatially-organized patterns. We pioneered the design of
‘dynamic substrates’ that present ligands whose activities can be
switched on and off in response to electrical or optical signals,
particularly for studies that address the responses of adherent cells
to changes in the extracellular matrix. These mimics of the
extracellular matrix have led the way to the discovery of novel ligands
that mediate cell adhesion. We have also developed robust surface
chemistries for preparing biochip arrays and that are compatible with
new analytical methods for analyzing the arrays. For example, we have
developed the SAMDI method, which uses mass spectrometry to analyze
the arrays, and we have extended this method to the first label-free
approach for high throughput screening, to the functional annotation of
recently sequenced genes and towards an understanding of the networks
that regulate protein acetylation. Finally, a recent program is
creating defined systems for exploring biochemical reactions to
understand the role that localization of enzymes and substrates play in
controlling reaction networks.
Dr. Mrksich was inducted as a Fellow in the American Institute for Medical and Biological Engineering
Rafe and Shagufata's papers were submitted:
"Using Peptide Arrays to Understand the Role of Adaptor Domain Interactions in Enzyme Specificity" and
"Geometric Control of Cytoskeletal Elements: Impact on
Vimentin Intermediate Filaments"
Steady-State of an Enzymatic Reaction is Dependent on the Density of Reactant. S. Li, X. Liao, and M. Mrksich. Langmuir2013, 29, 294-298.
Modular Assembly of Protein Building Blocks to Create
Precisely-Defined MegaMolecules. J.A. Modica, S. Skarpathiotis and M.
Mrksich. ChemBioChem2012, 13, 2331-2334. [PDF]
The Mechano-Stability of Isolated Focal Adhesions is Strongly Dependent on pH. K.G. Beaumont and M. Mrksich. Chem. & Biol. 2012, 19, 711-720. [PDF]
Prognostics by Direct Detection of p53-Antibodies on Gold Surfaces by
Impedance Measurements. E. Prats-Alfonso, X. Sisquella, N. Zine, G.
Gabriel, A. Guimerà, F. Javier del Campo, Rosa Villa, A. H. Eisenberg,
M. Mrksich, A. Errachid, J. Aguiló and F Albericio. Small2012, 8, 1962-1969. [PDF]
Reaction Discovery Enabled by SAMDI Mass Spectrometry. T.J. Montavon,
J. Li, J.R. Cabrera-Pardo, M. Mrksich and S.A. Kozmin. Nature Chemistry2012, 4, 45-51. [PDF]
of Glycosyltransferases Using Carbohydrate Arrays and Mass
Spectrometry. L. Ban, N. Pettit, L. Li, A.D. Stuparu, L. Cai, W. Chen,
W. Guan, P.W. Wang and M. Mrksich. Nat. Chem. Biol. 2012, 8, 769-773. [PDF]
Directing Stem Cell Fate by Controlling the Affinity and Density of
Ligand-Receptor Interactions at the Biomaterials Interface. K.A.
Kilian and M. Mrksich. Ang. Chem. Int. Ed.2012, 51, 4891-4895. [PDF]
For general inquiries contact MrksichGroup at gmail.com