title: Evaluation of interaction forces between profilin and designed peptide probes by atomic force microscopy.
abstract: We evaluated the binding affinity of peptide probes for profilin (protein) using force curve measurement techniques and atomic force microscopy (AFM). The peptide probes designed and synthesized for this investigation were H-A3GP5GP5GP5G-OH (1), H-A3GP5G-OH (2), H-A3G7-OH (3), and H-A3G-OH (4). Each peptide probe was immobilized on a cantilever tip, and the interaction force to profilin, immobilized on a mica substrate, was examined by force curve measurements. The retraction forces obtained showed a sequence-dependent affinity of the peptide probe for profilin. The retraction force for peptide probe 1 was the largest of the four probes examined, and it confirmed that peptide probe 1 has high affinity for profilin. The single molecular retraction force between peptide probe 1 and profilin was estimated to be 96 pN, as determined by Gaussian fitting to the histogram of the retraction forces.
authors.affiliation: School of Bionics, Tokyo University of Technology, Katakura, Hachioji, Tokyo, Japan.
authors.forename: Tomoko
authors.initials: T
authors.lastname: Okada
authors.forename: Masato
authors.initials: M
authors.lastname: Sano
authors.forename: Yuji
authors.initials: Y
authors.lastname: Yamamoto
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Muramatsu
mesh_terms: D018625:Microscopy, Atomic Force; D015335:Molecular Probes / Q000737:chemistry* / Q000648:ultrastructure*; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry*; D051304:Profilins / Q000737:chemistry* / Q000648:ultrastructure*; D013057:Spectrum Analysis
chemical_list: D015335:Molecular Probes; D010455:Peptides; D051304:Profilins