Morphological diversity and polymorphism of self-assembling collagen peptides controlled by length of hydrophobic domains.
Synthetic collagen mimetic peptides are used to probe the role of hydrophobic forces in mediating protein self-assembly. Higher order association is an integral property of natural collagens, which assemble into fibers and meshes that comprise the extracellular matrix of connective tissues. The unique triple-helix fold fully exposes two-thirds of positions in the protein to solvent, providing ample opportunities for engineering interaction sites. Inclusion of just a few hydrophobic groups in a minimal peptide promotes a rich variety of self-assembly behaviors, resulting in hundred-nanometer to micron size nanodiscs and nanofibers. Morphology depends primarily on the length of hydrophobic domains. Peptide discs contain lipophilic domains capable of sequestering small hydrophobic dyes. Combining multiple peptide types result in composite structures of discs and fibers ranging from stars to plates-on-a-string. These systems provide valuable tools to shed insight into the fundamental principles underlying hydrophobicity-driven higher order protein association that will facilitate the design of self-assembling systems in biomaterials and nanomedical applications.
Center for Advanced Biotechnology and Medicine, Robert Wood Johnson Medical School, Rutgers University , Piscataway, New Jersey 08854, United States.
Kenneth
K
McGuinness
I John
IJ
Khan
Vikas
V
Nanda
D000595:Amino Acid Sequence; D003094:Collagen / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D008969:Molecular Sequence Data; D057139:Nanofibers / Q000737:chemistry; D057786:Peptidomimetics / Q000737:chemistry*; D017434:Protein Structure, Tertiary
D057786:Peptidomimetics; D003094:Collagen
collagen mimetic peptides (CMPs); hydrophobicity; polymorphism; self-assembly