Environment- and sequence-dependence of helical type in membrane-spanning peptides composed of β3-amino acids

Ivan V. Korendovych; Scott J. Shandler; Geronda L. Montalvo; William F. Degrado

doi:10.1021/ol201218y

Environment- and sequence-dependence of helical type in membrane-spanning peptides composed of β³-amino acids

Ivan V. Korendovych, Scott J. Shandler, Geronda L. Montalvo, William F. Degrado

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

Abstract

Transmembrane (TM) β-peptides comprised of acyclic β³-amino acids demonstrate equilibrium between 12- and 14-helical structures in an environment- and sequence-dependent manner. Circular dichroism (CD) spectra of TM β³-peptides may be described as linear combinations of the 12- and 14-helical CD spectra. The apparent malleability of β³-substituted acyclic β-peptides has practical implications for foldamer design, as it suggests that both the 14-helix and 12-helix might be reasonable platforms for molecular recognition.

Original language	English (US)
Pages (from-to)	3474-3477
Number of pages	4
Journal	Organic Letters
Volume	13
Issue number	13
DOIs	https://doi.org/10.1021/ol201218y
State	Published - Jul 1 2011
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Physical and Theoretical Chemistry
Organic Chemistry

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10.1021/ol201218y

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abstract = "Transmembrane (TM) β-peptides comprised of acyclic β3-amino acids demonstrate equilibrium between 12- and 14-helical structures in an environment- and sequence-dependent manner. Circular dichroism (CD) spectra of TM β3-peptides may be described as linear combinations of the 12- and 14-helical CD spectra. The apparent malleability of β3-substituted acyclic β-peptides has practical implications for foldamer design, as it suggests that both the 14-helix and 12-helix might be reasonable platforms for molecular recognition.",

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AU - Korendovych, Ivan V.

AU - Shandler, Scott J.

AU - Montalvo, Geronda L.

AU - Degrado, William F.

PY - 2011/7/1

Y1 - 2011/7/1

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AB - Transmembrane (TM) β-peptides comprised of acyclic β3-amino acids demonstrate equilibrium between 12- and 14-helical structures in an environment- and sequence-dependent manner. Circular dichroism (CD) spectra of TM β3-peptides may be described as linear combinations of the 12- and 14-helical CD spectra. The apparent malleability of β3-substituted acyclic β-peptides has practical implications for foldamer design, as it suggests that both the 14-helix and 12-helix might be reasonable platforms for molecular recognition.

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Environment- and sequence-dependence of helical type in membrane-spanning peptides composed of β³-amino acids

Abstract

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