Abstract
The gas-phase helix propensities of alanine-based polypeptides are studied with different locations of a Lys residue and host-guest interactions with 18-Crown-6 (18C6). A series of model peptides Ac-Ala 9-n-LysH +-Ala n (n = 0, 1, 3, 5, 7, and 9) is examined alone and with 18C6 using traveling wave ion mobility mass spectrometry combined with molecular dynamics (MD) simulations. The gas-phase helices are observed from the peptides whose Lys residue is located close to the C-terminus so that the Lys exerts its capping effect on the C-terminal carbonyl groups. The peptides, which interact with 18C6 in the gas phase, show enhanced helical propensities. The enhanced helicity of the peptide in the complex is attributed by isolation of the Lys butylammonium group from the helix backbone and the interaction of methylene groups of 18C6, which possess localized positive partial charges, with C-terminal carbonyl groups serving as a cap to stabilize the helix.
| Original language | English |
|---|---|
| Pages (from-to) | 14215-14220 |
| Number of pages | 6 |
| Journal | Journal of Physical Chemistry A |
| Volume | 115 |
| Issue number | 49 |
| DOIs | |
| Publication status | Published - 2011 Dec 15 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Physical and Theoretical Chemistry
Cite this
Host-guest chemistry in the gas phase : Complex formation with 18-crown-6 enhances helicity of alanine-based peptides. / Ko, Jae Yoon; Heo, Sung Woo; Lee, Joon Ho; Oh, Han Bin; Kim, Hyungjun; Kim, Hugh I.
In: Journal of Physical Chemistry A, Vol. 115, No. 49, 15.12.2011, p. 14215-14220.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Host-guest chemistry in the gas phase
T2 - Complex formation with 18-crown-6 enhances helicity of alanine-based peptides
AU - Ko, Jae Yoon
AU - Heo, Sung Woo
AU - Lee, Joon Ho
AU - Oh, Han Bin
AU - Kim, Hyungjun
AU - Kim, Hugh I.
PY - 2011/12/15
Y1 - 2011/12/15
N2 - The gas-phase helix propensities of alanine-based polypeptides are studied with different locations of a Lys residue and host-guest interactions with 18-Crown-6 (18C6). A series of model peptides Ac-Ala 9-n-LysH +-Ala n (n = 0, 1, 3, 5, 7, and 9) is examined alone and with 18C6 using traveling wave ion mobility mass spectrometry combined with molecular dynamics (MD) simulations. The gas-phase helices are observed from the peptides whose Lys residue is located close to the C-terminus so that the Lys exerts its capping effect on the C-terminal carbonyl groups. The peptides, which interact with 18C6 in the gas phase, show enhanced helical propensities. The enhanced helicity of the peptide in the complex is attributed by isolation of the Lys butylammonium group from the helix backbone and the interaction of methylene groups of 18C6, which possess localized positive partial charges, with C-terminal carbonyl groups serving as a cap to stabilize the helix.
AB - The gas-phase helix propensities of alanine-based polypeptides are studied with different locations of a Lys residue and host-guest interactions with 18-Crown-6 (18C6). A series of model peptides Ac-Ala 9-n-LysH +-Ala n (n = 0, 1, 3, 5, 7, and 9) is examined alone and with 18C6 using traveling wave ion mobility mass spectrometry combined with molecular dynamics (MD) simulations. The gas-phase helices are observed from the peptides whose Lys residue is located close to the C-terminus so that the Lys exerts its capping effect on the C-terminal carbonyl groups. The peptides, which interact with 18C6 in the gas phase, show enhanced helical propensities. The enhanced helicity of the peptide in the complex is attributed by isolation of the Lys butylammonium group from the helix backbone and the interaction of methylene groups of 18C6, which possess localized positive partial charges, with C-terminal carbonyl groups serving as a cap to stabilize the helix.
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U2 - 10.1021/jp208045a
DO - 10.1021/jp208045a
M3 - Article
VL - 115
SP - 14215
EP - 14220
JO - Journal of Physical Chemistry A
JF - Journal of Physical Chemistry A
SN - 1089-5639
IS - 49
ER -