Nucleation effects in peptide foldamers

Anupam Patgiri, Stephen T. Joy, Paramjit Arora

Research output: Contribution to journalArticle

Abstract

Oligomers composed of β 3-amino acid residues and a mixture of α- and β 3-residues have emerged as proteolytically stable structural mimics of α-helices. An attractive feature of these oligomers is that they adopt defined conformations in short sequences. In this manuscript, we evaluate the impact of β 3-residues as compared to their α-amino acid analogs in prenucleated helices. Our hydrogen-deuterium exchange results suggest that heterogeneous sequences composed of "αααβ" repeats are conformationally more rigid than the corresponding homogeneous α-peptide helices, with the macrocycle templating the helical conformation having a significant influence.

Original languageEnglish (US)
Pages (from-to)11495-11502
Number of pages8
JournalJournal of the American Chemical Society
Volume134
Issue number28
DOIs
StatePublished - Jul 18 2012

Fingerprint

Oligomers
Peptides
Conformations
Amino acids
Nucleation
Amino Acids
Deuterium
Hydrogen

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

Nucleation effects in peptide foldamers. / Patgiri, Anupam; Joy, Stephen T.; Arora, Paramjit.

In: Journal of the American Chemical Society, Vol. 134, No. 28, 18.07.2012, p. 11495-11502.

Research output: Contribution to journalArticle

Patgiri, Anupam ; Joy, Stephen T. ; Arora, Paramjit. / Nucleation effects in peptide foldamers. In: Journal of the American Chemical Society. 2012 ; Vol. 134, No. 28. pp. 11495-11502.
@article{41d0f66b9a9f4867b5af8774388536e8,
title = "Nucleation effects in peptide foldamers",
abstract = "Oligomers composed of β 3-amino acid residues and a mixture of α- and β 3-residues have emerged as proteolytically stable structural mimics of α-helices. An attractive feature of these oligomers is that they adopt defined conformations in short sequences. In this manuscript, we evaluate the impact of β 3-residues as compared to their α-amino acid analogs in prenucleated helices. Our hydrogen-deuterium exchange results suggest that heterogeneous sequences composed of {"}αααβ{"} repeats are conformationally more rigid than the corresponding homogeneous α-peptide helices, with the macrocycle templating the helical conformation having a significant influence.",
author = "Anupam Patgiri and Joy, {Stephen T.} and Paramjit Arora",
year = "2012",
month = "7",
day = "18",
doi = "10.1021/ja301953j",
language = "English (US)",
volume = "134",
pages = "11495--11502",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "28",

}

TY - JOUR

T1 - Nucleation effects in peptide foldamers

AU - Patgiri, Anupam

AU - Joy, Stephen T.

AU - Arora, Paramjit

PY - 2012/7/18

Y1 - 2012/7/18

N2 - Oligomers composed of β 3-amino acid residues and a mixture of α- and β 3-residues have emerged as proteolytically stable structural mimics of α-helices. An attractive feature of these oligomers is that they adopt defined conformations in short sequences. In this manuscript, we evaluate the impact of β 3-residues as compared to their α-amino acid analogs in prenucleated helices. Our hydrogen-deuterium exchange results suggest that heterogeneous sequences composed of "αααβ" repeats are conformationally more rigid than the corresponding homogeneous α-peptide helices, with the macrocycle templating the helical conformation having a significant influence.

AB - Oligomers composed of β 3-amino acid residues and a mixture of α- and β 3-residues have emerged as proteolytically stable structural mimics of α-helices. An attractive feature of these oligomers is that they adopt defined conformations in short sequences. In this manuscript, we evaluate the impact of β 3-residues as compared to their α-amino acid analogs in prenucleated helices. Our hydrogen-deuterium exchange results suggest that heterogeneous sequences composed of "αααβ" repeats are conformationally more rigid than the corresponding homogeneous α-peptide helices, with the macrocycle templating the helical conformation having a significant influence.

UR - http://www.scopus.com/inward/record.url?scp=84863967321&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84863967321&partnerID=8YFLogxK

U2 - 10.1021/ja301953j

DO - 10.1021/ja301953j

M3 - Article

VL - 134

SP - 11495

EP - 11502

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

SN - 0002-7863

IS - 28

ER -