Toward β-peptide tertiary structure: Self-association of an amphiphilic 14-helix in aqueous solution

Tami L. Raguse, Jonathan R. Lai, Paul R. LePlae, Samuel H. Gellman

Research output: Contribution to journalArticle

111 Citations (Scopus)

Abstract

equation presented A major frontier in foldamer research is creation of unnatural oligomers that adopt discrete tertiary structures; at present, only biopolymers are known to fold into such compact conformations. We report an initial step toward helix-bundle tertiary structure in the β-peptide realm by showing that a 10-residue β-peptide designed to adopt an amphiphilic helical conformation forms small soluble aggregates in water. Sedimentation equilibrium data indicate that the aggregated state falls in the tetramer-hexamer size range.

Original languageEnglish (US)
Pages (from-to)3963-3966
Number of pages4
JournalOrganic Letters
Volume3
Issue number24
DOIs
StatePublished - Nov 29 2001
Externally publishedYes

Fingerprint

helices
peptides
Conformations
Association reactions
aqueous solutions
Peptides
Biopolymers
biopolymers
oligomers
Sedimentation
Oligomers
bundles
Water
Research
water

ASJC Scopus subject areas

  • Molecular Medicine

Cite this

Toward β-peptide tertiary structure : Self-association of an amphiphilic 14-helix in aqueous solution. / Raguse, Tami L.; Lai, Jonathan R.; LePlae, Paul R.; Gellman, Samuel H.

In: Organic Letters, Vol. 3, No. 24, 29.11.2001, p. 3963-3966.

Research output: Contribution to journalArticle

Raguse, Tami L. ; Lai, Jonathan R. ; LePlae, Paul R. ; Gellman, Samuel H. / Toward β-peptide tertiary structure : Self-association of an amphiphilic 14-helix in aqueous solution. In: Organic Letters. 2001 ; Vol. 3, No. 24. pp. 3963-3966.
@article{0d5812e3c034404f9fa61b99f3d91103,
title = "Toward β-peptide tertiary structure: Self-association of an amphiphilic 14-helix in aqueous solution",
abstract = "equation presented A major frontier in foldamer research is creation of unnatural oligomers that adopt discrete tertiary structures; at present, only biopolymers are known to fold into such compact conformations. We report an initial step toward helix-bundle tertiary structure in the β-peptide realm by showing that a 10-residue β-peptide designed to adopt an amphiphilic helical conformation forms small soluble aggregates in water. Sedimentation equilibrium data indicate that the aggregated state falls in the tetramer-hexamer size range.",
author = "Raguse, {Tami L.} and Lai, {Jonathan R.} and LePlae, {Paul R.} and Gellman, {Samuel H.}",
year = "2001",
month = "11",
day = "29",
doi = "10.1021/ol016868r",
language = "English (US)",
volume = "3",
pages = "3963--3966",
journal = "Organic Letters",
issn = "1523-7060",
publisher = "American Chemical Society",
number = "24",

}

TY - JOUR

T1 - Toward β-peptide tertiary structure

T2 - Self-association of an amphiphilic 14-helix in aqueous solution

AU - Raguse, Tami L.

AU - Lai, Jonathan R.

AU - LePlae, Paul R.

AU - Gellman, Samuel H.

PY - 2001/11/29

Y1 - 2001/11/29

N2 - equation presented A major frontier in foldamer research is creation of unnatural oligomers that adopt discrete tertiary structures; at present, only biopolymers are known to fold into such compact conformations. We report an initial step toward helix-bundle tertiary structure in the β-peptide realm by showing that a 10-residue β-peptide designed to adopt an amphiphilic helical conformation forms small soluble aggregates in water. Sedimentation equilibrium data indicate that the aggregated state falls in the tetramer-hexamer size range.

AB - equation presented A major frontier in foldamer research is creation of unnatural oligomers that adopt discrete tertiary structures; at present, only biopolymers are known to fold into such compact conformations. We report an initial step toward helix-bundle tertiary structure in the β-peptide realm by showing that a 10-residue β-peptide designed to adopt an amphiphilic helical conformation forms small soluble aggregates in water. Sedimentation equilibrium data indicate that the aggregated state falls in the tetramer-hexamer size range.

UR - http://www.scopus.com/inward/record.url?scp=0035969621&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035969621&partnerID=8YFLogxK

U2 - 10.1021/ol016868r

DO - 10.1021/ol016868r

M3 - Article

C2 - 11720580

AN - SCOPUS:0035969621

VL - 3

SP - 3963

EP - 3966

JO - Organic Letters

JF - Organic Letters

SN - 1523-7060

IS - 24

ER -