First crystallographic signature of an acyclic peptide nanorod: molecular mechanism of nanorod formation by a self-assembled tetrapeptide.
A terminally protected acyclic tetrapeptide Boc-Aib-Val-Aib-beta-Ala-OMe 1 (Aib: alpha-aminoisobutyric acid, beta-Ala: beta-Alanine) self-assembles into a continuous hydrogen-bonded supramolecular helix with an average diameter of 10 A (1 nm) starting from a double bend molecular conformation in crystals and further self-assembly of this supramolecular architecture leads to the formation of polydisperse nanorods of diameters 10-40 nm.
Haldar
Debasish
D
Department of Biological Chemistry, Indian Association for the Cultivation of Science, Jadavpur, Kolkata-700 032, India.
Banerjee
Arijit
A
Drew
Michael G B
MG
Das
Apurba Kumar
AK
Banerjee
Arindam
A
D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D008854:Microscopy, Electron; D008958:Models, Molecular; D036103:Nanotechnology; D009842:Oligopeptides / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D013329:Structure-Activity Relationship
D009842:Oligopeptides