Unknown

Dataset Information

0

"Helix-in-Helix" Superstructure Formation through Encapsulation of Fullerene-Bound Helical Peptides within a Helical Poly(methyl methacrylate) Cavity.


ABSTRACT: A one-handed 310 -helical hexapeptide is efficiently encapsulated within the helical cavity of st-PMMA when a fullerene (C60 ) derivative is introduced at the C-terminal end of the peptide. The encapsulation is accompanied by induction of a preferred-handed helical conformation in the st-PMMA backbone with the same-handedness as that of the hexapeptide to form a crystalline st-PMMA/peptide-C60 inclusion complex with a unique optically active helix-in-helix structure. Although the st-PMMA is unable to encapsulate the 310 -helical peptide without the terminal C60 unit, the helical hollow space of the st-PMMA is almost filled by the C60 -bound peptides. This result suggests that the C60 moiety can serve as a versatile molecular carrier of specific molecules and polymers in the helical cavity of the st-PMMA for the formation of an inclusion complex, thus producing unique supramolecular soft materials that cannot be prepared by other methods.

SUBMITTER: Ousaka N 

PROVIDER: S-EPMC5248627 | biostudies-other | 2017 Jan

REPOSITORIES: biostudies-other

altmetric image

Publications

"Helix-in-Helix" Superstructure Formation through Encapsulation of Fullerene-Bound Helical Peptides within a Helical Poly(methyl methacrylate) Cavity.

Ousaka Naoki N   Mamiya Fumihiko F   Iwata Yoshiaki Y   Nishimura Katsuyuki K   Yashima Eiji E  

Angewandte Chemie (International ed. in English) 20161221 3


A one-handed 3<sub>10</sub> -helical hexapeptide is efficiently encapsulated within the helical cavity of st-PMMA when a fullerene (C<sub>60</sub> ) derivative is introduced at the C-terminal end of the peptide. The encapsulation is accompanied by induction of a preferred-handed helical conformation in the st-PMMA backbone with the same-handedness as that of the hexapeptide to form a crystalline st-PMMA/peptide-C<sub>60</sub> inclusion complex with a unique optically active helix-in-helix struct  ...[more]

Similar Datasets

| S-EPMC9439638 | biostudies-literature
| S-EPMC1297517 | biostudies-literature
| S-EPMC1219581 | biostudies-other
| S-EPMC3074572 | biostudies-literature
| S-EPMC4195379 | biostudies-literature
| S-EPMC6905655 | biostudies-literature
| S-EPMC9183039 | biostudies-literature
| S-EPMC5510731 | biostudies-other
| S-EPMC6550408 | biostudies-literature
| S-EPMC6432498 | biostudies-literature