title: Evaluation of interaction between histidine binding Cu2+ ion and histidine by atomic force microscopy.
abstract: This paper presents a direct interaction force measurement between histidine molecules using AFM force-distance curve measurement. AFM force-distance curves between the histidine-modified cantilever and substrate in the different conditions with or without intercalating Cu2+ ion were measured and interpreted via Gaussian curve fitting analyses. The adhesion force between histidine molecules was shown to be 110 pN under the presence of Cu2+. The result was compareable to the measured adhesion force about 0 pN, which was measured by the removal of Cu2+ ion with the addition of EDTA. The result indicated the direct histidine-histidie interaction was difficult without the role of the bridigible ionic component. From the results, the possibility of direct measurement on chemical affinities between biomolecules was suggested by using AFM force-distance curve analyses. Especially, the current approach showed the possible affinity measurement techniques that elucidate the role of bridge ions.
authors.affiliation: Department of Chemical Engineering, Dong-A University, Hadan, Saha, Busan 604-714, Korea.
authors.forename: Jong Min
authors.initials: JM
authors.lastname: Kim
authors.forename: Haeng-Ja
authors.initials: HJ
authors.lastname: Lee
authors.forename: Woo-Sik
authors.initials: WS
authors.lastname: Kim
authors.forename: Masato
authors.initials: M
authors.lastname: Sano
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Muramatsu
authors.forename: Sang-Mok
authors.initials: SM
authors.lastname: Chang
mesh_terms: D000268:Adhesiveness; D001665:Binding Sites; D003300:Copper / Q000737:chemistry*; D006639:Histidine / Q000737:chemistry*; D007477:Ions; D018625:Microscopy, Atomic Force / Q000379:methods*; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D013314:Stress, Mechanical
chemical_list: D007477:Ions; D006639:Histidine; D003300:Copper