Biological Interfaces

Development of Systematic Methodology to Deduce Interfacial Structures of Peptides/Proteins

The behavior of proteins and peptides at interfaces plays important roles in many applications and research fields such as biomaterials, marine antifouling coatings, biosensors using surface immobilized enzymes, membrane proteins, antibody drugs, antimicrobial peptides etc.

We are developing systematic methodology to deduce interfacial conformation and orientation of peptides and proteins.

This methodology is a combined approach with SFG measurements, Hamiltonian spectra calculation, spectral matching between experimental and calculated spectra, molecular dynamics simulations, and isotope labeling.

This method is widely applicable to study peptides and proteins at interfaces such as membrane proteins, surface immobilized enzymes and peptides, membrane associated antimicrobial peptides, antibody drugs on surfaces, physically adsorbed proteins, and adhesive proteins/peptides adhered to surfaces, etc.

Surface Immobilized Peptides

Surface immobilized peptides are widely used for biosening, bacteria capture, antimicrobial coating etc.

Using SFG supplemented by other analytical tools such as ATR-FTIR and CD spectroscopy, we are studying conformation and orientation of surface immobilized peptides.

Surface immobilized antimicrobial peptides and peptide linkers to bind antibodies for medical diagnosis are under the current investigation.

Interfacial Enzymes

Interfacial enzymes are widely used for biosensing, biochips, biocatalysis, and polymer biodegradation.

We are applying SFG to study orientation and conformation of a variety of interfacial enzymes.

The interfacial enzyme structures are correlated to enzymatic activity to understand the structure-function relationships of interfacial enzymes.