Surface Induced nanofiber growth by self-assembly of a silk-elastin-like protein polymer.
Many synthetic and natural peptides are known to self-assemble to form various nanostructures. During the self-assembling process, environmental conditions such as salt concentration, pH, temperature, and surface characteristics play a critical role by influencing intermolecular interactions, and hence the process of self-assembly. Here we studied the self-assembly of a genetically engineered protein polymer composed of silk-like and elastin-like repeats on a mica surface. Silk-elastin-like protein polymers (SELPs) consist of tandem repeats of Gly-Ala-Gly-Ala-Gly-Ser from Bombyx mori (silkworm) and Gly-Val-Gly-Val-Pro from mammalian elastin. At a very low polymer concentration of 1 mug/mL, SELPs self-assembled into nanofibrous structures on a mica surface. Examination using atomic force microscopy (AFM) and dynamic light scattering techniques showed that SELPs self-assembled into nanofibers in the presence of the mica surface but not in the bulk state. Ionic strength had a significant influence on nanofiber growth, indicating the importance of electrostatic interactions between the polymer and the mica surface. At low ionic strength, the kinetics of nanofiber growth showed that the mica surface effectively removed a lag phase by providing nucleating sites, facilitating nanofiber self-assembly of SELPs. Furthermore, self-assembly on additional substrates such as silicon and a hydrophobic pyrolytic carbon surface revealed that the charged hydrophilic surface provides the optimal surface to facilitate self-assembly of SELPs.
Department of Materials Science and Engineering, University of Maryland, College Park, Maryland 20742, USA.
Wonseok
W
Hwang
Bo-Hyun
BH
Kim
Ramesh
R
Dandu
Joseph
J
Cappello
Hamidreza
H
Ghandehari
Joonil
J
Seog
D001704:Biopolymers / Q000737:chemistry*; D004549:Elastin / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D057139:Nanofibers; D009994:Osmolar Concentration; D047011:Silk
D001704:Biopolymers; D047011:Silk; D004549:Elastin