Chiroptical transcription of helical information through supramolecular harmonization with dynamic helices.
With biologically important "peptide bundling" as the motif, new chromophoric cyclic host 1 was designed, which consists of two zinc porphyrin units that are connected by dynamic peptide helices of nonameric aminoisobutyric acid (Aib) units. Upon inclusion of pyridine-anchored helical peptides between the zinc porphyrin units, 1 displayed an intense exciton-coupled circular dichroism (CD) band at 410-450 nm, whose sign reflected the helical sense of the guest peptides. Studies with conformationally defined dehydrophenylalanine-containing analogues indicated that the dynamic helical chains in the host are stereochemically harmonized with right- or left-handed helices of the guest peptides in a confined nano space, leading to either clockwise- or anticlockwise-twisted geometry (chiroptical output) of the connecting zinc porphyrin chromophores.
Guo
Yan-Ming
YM
Aida Nanospace Project, Exploratory Research for Advanced Technology, Japan Science and Technology Agency (JST), 2-41 Aomi, Koto-ku, Tokyo 135-0064, Japan.
Oike
Hideaki
H
Aida
Takuzo
T
D000621:Aminoisobutyric Acids / Q000138:chemical synthesis / Q000737:chemistry*; D040761:Biomimetic Materials / Q000138:chemical synthesis / Q000737:chemistry*; D002942:Circular Dichroism; D008665:Metalloporphyrins / Q000138:chemical synthesis / Q000737:chemistry*; D008958:Models, Molecular; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013237:Stereoisomerism; D013329:Structure-Activity Relationship
D000621:Aminoisobutyric Acids; D008665:Metalloporphyrins; D009842:Oligopeptides; C017802:zinc hematoporphyrin