Citation: Shuai Wei, Charles L. Brooks Ⅲ. Stability and orientation of cecropin P1 on maleimide self-assembled monolayer (SAM) surfaces and suggested functional mutations[J]. Chinese Chemical Letters, ;2015, 26(4): 485-490. doi: 10.1016/j.cclet.2015.03.020 shu

Stability and orientation of cecropin P1 on maleimide self-assembled monolayer (SAM) surfaces and suggested functional mutations

Shuai Wei ^a ,
Charles L. Brooks Ⅲ ^a,b

1.
a Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA;
2.
b Department of Biophysics, University of Michigan, Ann Arbor, MI 48109, USA

Received Date: 28 January 2015
Available Online: 10 March 2015

One of the main challenges of biosensor design is to understand the protein or peptide stability on the chip in high resolution structural detail. Since conventional experimental methods are limited by the resolution for their applications on surface tethered peptides/proteins, a recently developed coarse grained simulation method is employed to explore the peptide/surface interaction in residue-level resolution. This work shows how the coarse grained model successfully describes peptide-surface interactions by evaluating thermal stability of the peptide cecropin P1 in bulk solution and on surfaces by physical adsorption and chemical tethering. The simulation also reproduces observations of peptide orientations on the self-assembled monolayer surface from earlier experimental work. Additionally, using knowledge obtained from the simulations, specific mutations are suggested and the desired structure and pose on the surface is obtained. In summary, this work sheds a light on the reasonable biosensor design that is guided by simulations.
- Coarse grained simulation,
- KB Go-like model,
- Peptide-surface interaction,
- Thermal stability,
- Orientation,
- Mutation
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