Abstract
Although significant progress has been achieved with short peptide nanostructures, the construction of switchable membrane assemblies remains a great challenge. Here we report short α-peptide assemblies that undergo thermo-reversible switching between assembly and disassembly states, triggered by the conformational change of laterally grafted short peptides from a folded α-helix to a random coil conformation. The α-helical peptide based on two oligoether dendron side groups forms flat disks, while the peptide helix based on three dendron side groups forms hollow vesicles. The vesicular membrane can spontaneously capture a racemic mixture through the self-formation of vesicular containers upon heating and enantioselectively release the chiral guest molecule through preferential diffusion across the vesicular walls.
| Original language | English |
|---|---|
| Pages (from-to) | 5773-5776 |
| Number of pages | 4 |
| Journal | Journal of the American Chemical Society |
| Volume | 138 |
| Issue number | 18 |
| DOIs | |
| Publication status | Published - 2016 May 11 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Catalysis
- Chemistry(all)
- Biochemistry
- Colloid and Surface Chemistry
Cite this
Reversible, short α-peptide assembly for controlled capture and selective release of enantiomers. / Chen, Xi; He, Ying; Kim, Yongju; Lee, Myongsoo.
In: Journal of the American Chemical Society, Vol. 138, No. 18, 11.05.2016, p. 5773-5776.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Reversible, short α-peptide assembly for controlled capture and selective release of enantiomers
AU - Chen, Xi
AU - He, Ying
AU - Kim, Yongju
AU - Lee, Myongsoo
PY - 2016/5/11
Y1 - 2016/5/11
N2 - Although significant progress has been achieved with short peptide nanostructures, the construction of switchable membrane assemblies remains a great challenge. Here we report short α-peptide assemblies that undergo thermo-reversible switching between assembly and disassembly states, triggered by the conformational change of laterally grafted short peptides from a folded α-helix to a random coil conformation. The α-helical peptide based on two oligoether dendron side groups forms flat disks, while the peptide helix based on three dendron side groups forms hollow vesicles. The vesicular membrane can spontaneously capture a racemic mixture through the self-formation of vesicular containers upon heating and enantioselectively release the chiral guest molecule through preferential diffusion across the vesicular walls.
AB - Although significant progress has been achieved with short peptide nanostructures, the construction of switchable membrane assemblies remains a great challenge. Here we report short α-peptide assemblies that undergo thermo-reversible switching between assembly and disassembly states, triggered by the conformational change of laterally grafted short peptides from a folded α-helix to a random coil conformation. The α-helical peptide based on two oligoether dendron side groups forms flat disks, while the peptide helix based on three dendron side groups forms hollow vesicles. The vesicular membrane can spontaneously capture a racemic mixture through the self-formation of vesicular containers upon heating and enantioselectively release the chiral guest molecule through preferential diffusion across the vesicular walls.
UR - http://www.scopus.com/inward/record.url?scp=84971378825&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84971378825&partnerID=8YFLogxK
U2 - 10.1021/jacs.6b02401
DO - 10.1021/jacs.6b02401
M3 - Article
C2 - 27078796
AN - SCOPUS:84971378825
VL - 138
SP - 5773
EP - 5776
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 18
ER -