Toward the development of peptide nanofilaments and nanoropes as smart materials.
Protein design studies using coiled coils have illustrated the potential of engineering simple peptides to self-associate into polymers and networks. Although basic aspects of self-assembly in protein systems have been demonstrated, it remains a major challenge to create materials whose large-scale structures are well determined from design of local protein-protein interactions. Here, we show the design and characterization of a helical peptide, which uses phased hydrophobic interactions to drive assembly into nanofilaments and fibrils ("nanoropes"). Using the hydrophobic effect to drive self-assembly circumvents problems of uncontrolled self-assembly seen in previous approaches that used electrostatics as a mode for self-assembly. The nanostructures designed here are characterized by biophysical methods including analytical ultracentrifugation, dynamic light scattering, and circular dichroism to measure their solution properties, and atomic force microscopy to study their behavior on surfaces. Additionally, the assembly of such structures can be predictably regulated by using various environmental factors, such as pH, salt, other molecular crowding reagents, and specifically designed "capping" peptides. This ability to regulate self-assembly is a critical feature in creating smart peptide biomaterials.
Wagner
Daniel E
DE
Department of Biology, Haverford College, 370 Lancaster Avenue, Haverford, PA 19041, USA.
Phillips
Charles L
CL
Ali
Wasif M
WM
Nybakken
Grant E
GE
Crawford
Emily D
ED
Schwab
Alexander D
AD
Smith
Walter F
WF
Fairman
Robert
R
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D018625:Microscopy, Atomic Force; D008958:Models, Molecular; D008969:Molecular Sequence Data; D049329:Nanostructures / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D011108:Polymers / Q000737:chemistry; D017434:Protein Structure, Tertiary; D012542:Scattering, Radiation; D016415:Sequence Alignment; D055672:Static Electricity; D013694:Temperament
D010455:Peptides; D011108:Polymers