In the field of nanotechnology and applied engineering, an area that has received a great deal of attention is that of nanoassembly. The objective of this study was to demonstrate nanoassembly of type-I collagen on specified surfaces in response to an electric field. Two, otherwise identical, collagen solutions were prepared and adjusted to pHs of 5.5 and 8. The isoelectric fosusing point of collagen occurs at pH=6.7 which implies that the suspended collagen fibers in the aforementioned solutions possessed a net positive or negative charge, respectively. In each collagen solution, one volt was applied through a set of submerged electrodes for one minute. Atomic force microscopy was used to detect if and where assembly had occurred on the electrodes. The positively charged fibrils (pH=5.5) assembled on the negative electrode, but not on the positive electrode. The negatively charged fibrils (pH=8) assembled only on the positive electrode, but not on the negative electrode. In both cases, assembly occurred on the electrode of opposite charge of the suspended collagen fibrils, which was anticipated. The assembly of the positively charged fibrils (pH=5.5) on the cathode produced larger fibers than the fibers that were produced by the negatively charged fibrils (pH=8) on the anode. This indicated the more favorable environment for nanoassembly was the positively charged fibril solution (pH=5.5).

1.
Emerich
D. F.
and
Thanos
C. G.
,
Nanotechnology and medicine
.
Expert Opmion on Biological Therapy.
July
2003
, V
3
(
4
), pp.
655
663
.
2.
Barrias
C. C.
,
Martins
C. L.
,
Miranda
C. S.
,
Barbosa
M. A.
,
Adsorption of a therapeutic enzyme to self-assembled monolayers: effect of surface chemistry and solution pH on the amount and activity of adsorbed enzyme
.
Biomaterials
,
2005
,
26
, pp.
2695
2704
.
3.
Dupont-Gillain
Ch. C.
,
Pamula
E.
,
Denis
F. A.
,
De Cupere
V. M.
,
Dufrene
Y. F
,
Rouxhet
P. G
,
Controlling the supramolecular organization of adsorbed collagen layers
.
Journal of Materials Science: Materials in Medicine
,
2004
,
15
, pp.
347
353
.
4.
Chapman
J. A.
,
The Regulation of Size and Form in the Assembly of Collagen Fibrils in Vivo
.
Biopolymers
,
1989
, V
28
, pp.
1367
1382
.
5.
Zhang
G
,
Young
B. B.
,
Ezura
Y.
,
Favata
M.
,
Soslowsky
L. J.
,
Chakravarti
S.
,
Birk
D. E.
,
Development of tendon structure and function: Regulation of collagen fibrillogenesis
.
Journal of Musculoskeletal and Neuronal Interaction. March
2005
,
5
(
1
), pp.
5
21
.
6.
Nelson D.L and Cox, M.M. Lehninger Principles of Biochemistry, Third Edition, Worth Publishers. 2004.
7.
Kukkola, L., Collagen Prolyl 4-Hydroxylase, Academic Dissertation. Collagen Research Unit, Biocenter Oulu and Department of Medical Biochemistry and Molecular Biology, University of Oulu, 2003.
8.
Rasmol 1BKV structure from Protein Data Base,
Kramer
R. Z.
,
Bella
J.
,
Mayviller
P.
,
Brodsky
B.
,
Berman
H. M.
Sequence dependent conformational variations of collagen triple-helicle structure
.
Nature: Structural Biology
,
1999
,
6
, pp.
454
454
.
9.
On-line database: www.Expasy.org
This content is only available via PDF.
You do not currently have access to this content.