Origins of the high 14-helix propensity of cyclohexyl-rigidified residues in β-peptides

Myung Ryul Lee; Tami L. Raguse; Marina Schinnerl; William C. Pomerantz; Xiaodong Wang; Peter Wipf; Samuel H. Gellman

doi:10.1021/ol070511r

Origins of the high 14-helix propensity of cyclohexyl-rigidified residues in β-peptides

Myung Ryul Lee, Tami L. Raguse, Marina Schinnerl, William C. Pomerantz, Xiaodong Wang, Peter Wipf, Samuel H. Gellman

Chemistry (Twin Cities)

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

45 Scopus citations

Abstract

β-Peptides containing residues derived from trans-2- aminocyclohexanecarboxylic acid (ACHC) display high population of 14-helical secondary structure in aqueous solution. We show that hydrophobic interactions between cyclohexyl rings are not responsible for this conformationpromoting effect, and that polar groups may be attached to the cyclohexyl ring without diminishing the effect.

Original language	English (US)
Pages (from-to)	1801-1804
Number of pages	4
Journal	Organic Letters
Volume	9
Issue number	9
DOIs	https://doi.org/10.1021/ol070511r
State	Published - Apr 26 2007

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abstract = "β-Peptides containing residues derived from trans-2- aminocyclohexanecarboxylic acid (ACHC) display high population of 14-helical secondary structure in aqueous solution. We show that hydrophobic interactions between cyclohexyl rings are not responsible for this conformationpromoting effect, and that polar groups may be attached to the cyclohexyl ring without diminishing the effect.",

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AU - Lee, Myung Ryul

AU - Raguse, Tami L.

AU - Schinnerl, Marina

AU - Pomerantz, William C.

AU - Wang, Xiaodong

AU - Wipf, Peter

AU - Gellman, Samuel H.

PY - 2007/4/26

Y1 - 2007/4/26

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AB - β-Peptides containing residues derived from trans-2- aminocyclohexanecarboxylic acid (ACHC) display high population of 14-helical secondary structure in aqueous solution. We show that hydrophobic interactions between cyclohexyl rings are not responsible for this conformationpromoting effect, and that polar groups may be attached to the cyclohexyl ring without diminishing the effect.

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Origins of the high 14-helix propensity of cyclohexyl-rigidified residues in β-peptides

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