Bilayer fibril formation by genetically engineered polypeptides: preparation and characterization.
A de novo, genetically engineered 687 residue polypeptide expressed in E. coli has been found to form highly rectilinear, beta-sheet containing fibrillar structures. Tapping-mode atomic force microscopy, deep-UV Raman spectroscopy, and transmission electron microscopy definitively established the tendency of the fibrils to predominantly display an apparently planar bilayer or ribbon assemblage. The ordered self-assembly of designed, extremely repetitive, high molecular weight peptides is a harbinger of the utility of similar materials in nanoscience and engineering applications.
Topilina
Natalya I
NI
Department of Chemistry and College of Nanoscale Science and Engineering, The University at Albany, State University of New York, Albany, New York 12222, USA.
Higashiya
Seiichiro
S
Rana
Narender
N
Ermolenkov
Vladimir V
VV
Kossow
Christopher
C
Carlsen
Autumn
A
Ngo
Silvana C
SC
Wells
Christopher C
CC
Eisenbraun
Eric T
ET
Dunn
Kathleen A
KA
Lednev
Igor K
IK
Geer
Robert E
RE
Kaloyeros
Alain E
AE
Welch
John T
JT
D001483:Base Sequence; D004247:DNA / Q000737:chemistry / Q000235:genetics; D008051:Lipid Bilayers / Q000138:chemical synthesis* / Q000737:chemistry* / Q000302:isolation & purification; D018625:Microscopy, Atomic Force; D046529:Microscopy, Electron, Transmission; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010316:Particle Size; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D015202:Protein Engineering; D017433:Protein Structure, Secondary; D012680:Sensitivity and Specificity; D013059:Spectrum Analysis, Raman
D008051:Lipid Bilayers; D010455:Peptides; D004247:DNA