Single-Molecule Recognition and Manipulation Studied
by Scanning Probe Microscopy
Dr. Byung Kim, PhD
Department of Physics
Boise State University
Professor Kim conducts single-molecule biomolecular research using scanning
probe microscopy (SPM) techniques.
The first part of the talk will focus on chiral recognition, a fundamental
aspect of chemical biology that is of central importance in pharmaceutics.
Enantiomeric drugs are used to increase the chances of success in targeting
enzymes, hormones, and receptors on cell surfaces, along with other compounds
that are made up of chiral amino acids, carbohydrates, and lipids. Single-molecule
STM images allow us to understand the fundamental mechanism of the chiral
recognition of PVBA on Ag(111), but not on Pd(111)1.
The second part of the talk will discuss the binding mechanism between 5’-methylthioadenosine/S-adenosylhomocysteine
nucleo-sidase (MTAN) and homocystinyl immucillin A (HIA), the latter being
a known inhibitor of MTAN. The importance of MTAN lies in its uniqueness
as a player in the methionine salvage pathway of certain bacteria and its
absence of in the pathway of mammals. Such a feature makes it a potential
The third part of the talk involves controlling the adsorption and desorption
of proteins reversibly using a thermally switchable bioactive surface for
future drug delivery 2. At room temperature, a polymer PNIPAM(poly
n-isopropyl acrylamide) tethered to a solid surface creates a layer of ordered
water around each polymer chain, inhibiting protein adsorption. Above
the transition temperature, however, the water ordering is thermally disrupted,
allowing protein adsorption.
1. B.I. Kim, “Chiral Recognition of PVBA on Ag(111) and Pd(111)”, Langmuir
2. D. L. Huber, R. P. Maginell, M. A. Samara, B.-I. Kim, and B. C. Bunker,
“Programmed Adsorption and Release of Proteins in a Microfluidic Device”,
Science 301, 352(2003).