Boris Akhremitchev 

Associate Professor of Chemistry

Diploma, Moscow Institue of Physics and Technology
Ph.D., University of Pittsburgh 

Phone: (321) 674-8587

Office: 338 Olin Physical Sciences Building (Chemistry Departemnt office)




Biophysical chemistry, physical chemistry, single-molecule investigation of intra- and inter-molecular forces

Dr. Akhremitchev’s research interests are in experimental biophysical chemistry and physical chemistry.  Research program aims at uncovering nanoscale details of intermolecular interactions and structural dynamics that control many important biological processes including protein aggregation, receptor-ligand binding and formation of supramolecular biological structures.  Experimental approaches utilize high spatial and force resolution of scanning probe techniques to investigate molecular structures at the nanoscale and at a single-molecule level.  The main research directions are:

  • Quantitative characterization of energy landscape that holds molecules together in the dimeric, oligomeric or aggregated states.  This research aims to develop deep physical insights into the mechanisms of interactions between flexible biomolecules that currently are difficult to measure or compute.
  • Investigations of effects of external force of molecules in the bound state.  External forces significantly affect propensities of molecules to bind and to dissociate.  It is becoming widely recognized that these effects are different from thermal effects.  This research direction contributes to the rapidly developing field of molecular mechanochemistry.
  • Development of new force-based approaches that provide quantitative information about macromolecules that is not available from other techniques.  Significant attention is given to the development of experimental and data analysis methodology permitting accurate quantification of kinetic and thermodynamic parameters of interactions between individual molecules at the nanoscale.

Research of Dr. Akhremitchev is supported by grants from the National Science Foundation and from the industry.


Selected Publications

Guo, S.; Li, N.; Lad, N.; Ray, C.; Akhremitchev, B. B. “Mechanical Distortion of Protein Receptor Decreases the Lifetime of a Receptor-Ligand Bond”  J. Am. Chem. Soc. 2010, 132, 9681–9687.

Averett, L. E.; Schoenfisch, M. H.; Akhremitchev, B. B.; Gorkun, O. V.  “Kinetics of the Multi-Step Rupture of Fibrin ‘A-a’ Polymerization Interactions Measured using AFM” Biophys. J.  2009, 97, 2820-2828.

Guo, S.; Lad, N.; Ray, C.; Akhremitchev, B. B.  “Association Kinetics from Single Molecule Force Spectroscopy Measurements.”  Biophys. J. 2009, 96, 3412-3422.

Ray, C; Gu, C.; Brown, J. R.; Kirkpatrick, A.; Akhremitchev, B. B.  “Anisotropy of Pairwise Interactions between Hexadecanes in Water Measured by AFM Force Spectroscopy”  J. Phys. Chem. –C 2008, 112, 18164-18172.

Guo, S.; Ray, C.; Kirkpatrick, A.; Lad, N.; Akhremitchev B. B.  “Effects of Multiple-Bond Ruptures on Kinetic Parameters Extracted from Force Spectroscopy Measurements: Revisiting Biotin-Streptavidin Interactions”  Biophys. J. 2008, 95, 3964-3976.

Ray, C.; Brown, J. R.; Kirkpatrick, A.; Akhremitchev, B. B. “Pairwise Interactions Between Linear Alkanes in Water Measured by AFM Force Spectroscopy” J. Am. Chem. Soc.  2008, 130, 10008-10018.

Gu, C.; Ray, C; Guo, S.; Akhremitchev, B. B. “Single-Molecule Force Spectroscopy Measurements of Interactions between C60 Fullerene Molecules” J. Phys. Chem. -C  2007, 111, 12898-12905.

Ray, C; Brown, J. R.; Akhremitchev, B. B. “Single-Molecule Force Spectroscopy Measurements of "Hydrophobic Bond" between Tethered Hexadecane Molecules” J. Phys. Chem. - B  2006, 110, 17578-17583.

Guo, S.; Akhremitchev, B. B. “Packing Density and Structural Heterogeneity of Insulin Amyloid Fibrils Measured by AFM Nanoindentation” Biomacromolecules 2006, 7, 1630-1636.

Ray, C.; Akhremitchev, B. B. “Conformational Heterogeneity of Surface-Grafted Amyloidogenic Fragments of alpha-Synuclein Dimers Detected by Atomic Force Microscopy” J. Am. Chem. Soc.  2005, 127, 14739-14744.