Folding of beta-structured fibrous proteins and self-assembling peptides.
Natural fibrous proteins include families found in natural materials such as wool and silk; in tissue components such as collagen and elastin; or in virus and bacteriophage adhesins. They have long fascinated scientists and engineers because of their mechanical and elastic properties, and considerable efforts have been made in order to produce artificial materials inspired from these natural proteins. The understanding of their structure, folding, and assembly properties is necessary in order to achieve these objectives. However, because of their complexity, structural information is quite often extremely difficult to obtain for these proteins. In this chapter, we focus on a particular family of fibrous proteins: trimeric, beta-stranded viral adhesins. We describe folding strategies that led to the identification of stable domains that could be crystallized, and the novel structural motifs that are emerging. We also discuss self-assembling peptides derived from these motifs. Finally, we review the possibilities of designing novel macroscopic materials as well as nanoscale fibrous objects with controlled dimensions and properties based on these novel structural motifs.
Mitraki
Anna
A
Institut de Biologie Structurale, Grenoble, France.
van Raaij
Mark J
MJ
D000256:Adenoviridae / Q000737:chemistry / Q000378:metabolism; D017122:Bacteriophage T4 / Q000737:chemistry / Q000378:metabolism; D036103:Nanotechnology; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism
D010455:Peptides; D014764:Viral Proteins