Interaction force of chitin-binding domains onto chitin surface.
Interaction force of chitin-binding domains (ChBD1 and ChBD2) from a thermostable chitinase onto chitin surface was directly measured by atomic force microscopy (AFM) in a buffer solution. In the force curve measurement, multiple pull-off events were observed for the AFM tips functionalized with either ChBD1 or ChBD2, whereas the AFM tips terminated with nitrilotriacetic acid groups without ChBD showed no interaction peak, suggesting that the detected forces are derived from the binding functions of ChBDs onto the chitin surface. The force curve analyses indicate that the binding force of ChBD2 is stronger than that of ChBD1. This result suggests that ChBD1 and ChBD2 play different roles in adsorption onto chitin surface.
Kikkawa
Yoshihiro
Y
Nanoarchitectonics Research Center, National Institute of Advanced Industrial Science and Technology, Tsukuba Central 4, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8562, Japan. y.kikkawa@aist.go.jp
Tokuhisa
Hideo
H
Shingai
Hajime
H
Hiraishi
Tomohiro
T
Houjou
Hirohiko
H
Kanesato
Masatoshi
M
Imanaka
Tadayuki
T
Tanaka
Takeshi
T
D000327:Adsorption; D002021:Buffers; D020134:Catalytic Domain; D002686:Chitin / Q000737:chemistry* / Q000378:metabolism; D002688:Chitinases / Q000737:chemistry; D006358:Hot Temperature; D018625:Microscopy, Atomic Force; D010455:Peptides / Q000737:chemistry; D010957:Plasmids / Q000378:metabolism; D011134:Polysaccharides / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry; D019712:Thermococcus / Q000201:enzymology
D002021:Buffers; D010455:Peptides; D011134:Polysaccharides; D011994:Recombinant Proteins; D002686:Chitin; D002688:Chitinases