Imperial College London

Professor Molly Stevens

Faculty of EngineeringDepartment of Materials

Professor of Biomedical Materials and Regenerative Medicine



+44 (0)20 7594 6804m.stevens




208Royal School of MinesSouth Kensington Campus






BibTex format

author = {Stevens, MM and Allen, S and Chan, WC and Davies, MC and Roberts, CJ and Tendler, SJ and Williams, PM},
doi = {10.1039/a907741c},
journal = {Analyst},
pages = {245--250},
title = {Probing protein-peptide-protein molecular architecture by atomic force microscopy and surface plasmon resonance.},
url = {},
volume = {125},
year = {2000}

RIS format (EndNote, RefMan)

AB - We demonstrate the creation of a protein multilayer which utilises the high affinity interaction between streptavidin and biotin and incorporates a peptidic spacer. Surface plasmon resonance measurements enabled us to monitor the construction of the multilayer in real time. Atomic force microscopy was utilised to determine surface functionality at each stage of the multilayer construction, allowing us to investigate the associated mechanical properties. In this context we observed an increase in biomolecular stretching on the formation of the multilayer. We demonstrate, utilising circular dichroism, that variations in the solvent can affect the secondary structure of the peptide linker and hence its mechanical properties. Trifluoroethanol titrations on the assembled system indicate that the multilayer properties are also stimuli responsive with regard to solvent conditions. These results indicate that the multilayer stretch before cleavage is increased in the presence of trifluoroethanol. This was not expected from the study of the individual linker alone, indicating the need to study the system as a whole as opposed to the isolated components.
AU - Stevens,MM
AU - Allen,S
AU - Chan,WC
AU - Davies,MC
AU - Roberts,CJ
AU - Tendler,SJ
AU - Williams,PM
DO - 10.1039/a907741c
EP - 250
PY - 2000///
SN - 0003-2654
SP - 245
TI - Probing protein-peptide-protein molecular architecture by atomic force microscopy and surface plasmon resonance.
T2 - Analyst
UR -
UR -
VL - 125
ER -