title: Formation of Nanostructures by Peptides.
abstract: BACKGROUND
  Amyloid fibrils, which are implicated in several diseases, are highly ordered structures formed by aggregation of proteins. Intriguingly, several short peptides, some of which are unrelated to the disease-causing proteins, also aggregate to form amyloid fibrils in vitro. The aggregation behavior of these short peptides can be modulated so that they form nanostructures that are not in any way related to amyloid fibrils. These observations have led to extensive research aimed at getting insights into how peptides aggregate to form amyloids as well as non-amyloidogenic structures.
  
  
  METHODS
  This review examines the aggregation behavior of peptides that form highly polymorphic structures including fibrils, nanotubes, nanospheres and hydrogels. The review also describes how short peptides composed of only two and three hydrophobic and aromatic amino acids can selfassemble to form nanotubes and nanospheres.
  
  
  RESULTS
  Peptides with widely varying amino acid composition and lengths aggregate to form indistinguishable fibrils and nanostructures. The potential application of these aggregated structures in the design of novel biomaterials is reviewed and highlighted.
  
  
  CONCLUSIONS
  It is evident that highly polymorphic aggregated structures of peptides can be obtained by varying conditions such as solvent of dissolution, temperatures, pH and even surfaces of deposition.
authors.affiliation: CSIR- Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500007, India.
authors.forename: Sanjai Kumar
authors.initials: SK
authors.lastname: Pachahara
authors.affiliation: CSIR- Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007, India.
authors.forename: Chivukula
authors.initials: C
authors.lastname: Subbalakshmi
authors.affiliation: CSIR- Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007, India.
authors.forename: Ramakrishnan
authors.initials: R
authors.lastname: Nagaraj
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D000682:Amyloid / Q000737:chemistry; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D049329:Nanostructures / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D066329:Protein Aggregates; D011487:Protein Conformation
chemical_list: D000596:Amino Acids; D000682:Amyloid; D010455:Peptides; D066329:Protein Aggregates
keywords: Aggregation; amyloid fibrils; nanostructures; nanotube; peptides; self-assembly