One-dimensional self-assembly of a rational designed β-structure peptide

摘要: Fabricating various nanostructures based on the self-assembly of diverse biological molecules is now great interest to field bionanotechnology. In this study, we report a de novo designed peptide (T1) with preferential β-hairpin forming property that can spontaneously assemble into nanofibrils in ultrapure water. The assembled by T1 could grow up tens microns length left-handed helical twist and an average height 4.9 ± 0.9 nm. Moreover, protofilaments nucleus structures both similar 1.4 0.2 nm were observed during fibrilization as well via sonication mature nanofibrils. A typical conformational transition from random coil β-structure was association fibrilization. Molecular modeling assemblies displayed organize parallel fashion which β-strands align antiparallel each adjoining β-strand runs at about 2.9° respect one located before it along fibrillar axis. It also revealed maximum thickness assembly intermediate, tape structure, four tapes further fibril diameter 4.1 Taken together results obtained AFM, CD, molecular modeling, probably undergoes hierarchy approach, aromatic stacking electrostatic interactions between are most likely two major factors directing one-dimensional self-assembly. Based these studies, propose be used model investigate β-sheet process potential bioorganic template develop functional materials. © 2007 Wiley Periodicals, Inc. Biopolymers 86: 23–31, 2007. This article originally published online accepted preprint. “Published Online” date corresponds preprint version. You request copy emailing editorial office biopolymers@wiley.com