A systematic study of the solid state and solution phase conformational preferences of beta-peptides derived from transpentacin

Elin Abraham; Callum W. Bailey; Timothy D. W. Claridge; Stephen G. Davies; Kenneth B. Ling; Barbara Odell; Thomas L. Rees; Paul M. Roberts; Angela J. Russell; Andrew D. Smith; Lorna J. Smith; Helen R. Storr; Miles J. Sweet; Amber L. Thompson; James E. Thomson; George E. Tranter; David J. Watkin; Andrew David Smith

doi:10.1016/j.tetasy.2010.06.001

A systematic study of the solid state and solution phase conformational preferences of beta-peptides derived from transpentacin

Elin Abraham, Callum W. Bailey, Timothy D. W. Claridge, Stephen G. Davies, Kenneth B. Ling, Barbara Odell, Thomas L. Rees, Paul M. Roberts, Angela J. Russell, Andrew D. Smith, Lorna J. Smith, Helen R. Storr, Miles J. Sweet, Amber L. Thompson, James E. Thomson, George E. Tranter, David J. Watkin, Andrew David Smith

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31 Citations (Scopus)

Abstract

The solid state and solution phase conformational preferences of a homologous series of beta-peptides derived from (S,S)-2-aminocyclopentanecarboxylic acid (transpentacin) have been investigated using a variety of spectroscopic and crystallographic techniques. These studies indicate that the hexamer and pentamer persist as a 12-helix in both the solid state and solution phase. Although the conformational traits of a 12-helix are exhibited by oligomers with as few as three residues in the solid state, in solution the trimer exists as an equilibrium of many alternative conformers whilst the tetramer has been shown to predominantly exist in either a 12-helix or a turn-type conformation. (C) 2010 Elsevier Ltd. All rights reserved.

Original language	English
Pages (from-to)	1797-1815
Number of pages	19
Journal	Tetrahedron: Asymmetry
Volume	21
Issue number	13-14
DOIs	https://doi.org/10.1016/j.tetasy.2010.06.001
Publication status	Published - 14 Jul 2010

Keywords

2-AMINOCYCLOPENTANECARBOXYLIC ACID-DERIVATIVES
HELICAL SECONDARY STRUCTURE
DE-NOVO DESIGN
ASYMMETRIC-SYNTHESIS
AQUEOUS-SOLUTION
FOLDAMERS
RESIDUES
(-)-(1R,2S)-CISPENTACIN
HEXAPEPTIDE
RESOLUTION

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10.1016/j.tetasy.2010.06.001

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Abraham, E., Bailey, C. W., Claridge, T. D. W., Davies, S. G., Ling, K. B., Odell, B., Rees, T. L., Roberts, P. M., Russell, A. J., Smith, A. D., Smith, L. J., Storr, H. R., Sweet, M. J., Thompson, A. L., Thomson, J. E., Tranter, G. E., Watkin, D. J., & Smith, A. D. (2010). A systematic study of the solid state and solution phase conformational preferences of beta-peptides derived from transpentacin. Tetrahedron: Asymmetry, 21(13-14), 1797-1815. https://doi.org/10.1016/j.tetasy.2010.06.001

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abstract = "The solid state and solution phase conformational preferences of a homologous series of beta-peptides derived from (S,S)-2-aminocyclopentanecarboxylic acid (transpentacin) have been investigated using a variety of spectroscopic and crystallographic techniques. These studies indicate that the hexamer and pentamer persist as a 12-helix in both the solid state and solution phase. Although the conformational traits of a 12-helix are exhibited by oligomers with as few as three residues in the solid state, in solution the trimer exists as an equilibrium of many alternative conformers whilst the tetramer has been shown to predominantly exist in either a 12-helix or a turn-type conformation. (C) 2010 Elsevier Ltd. All rights reserved.",

keywords = "2-AMINOCYCLOPENTANECARBOXYLIC ACID-DERIVATIVES, HELICAL SECONDARY STRUCTURE, DE-NOVO DESIGN, ASYMMETRIC-SYNTHESIS, AQUEOUS-SOLUTION, FOLDAMERS, RESIDUES, (-)-(1R,2S)-CISPENTACIN, HEXAPEPTIDE, RESOLUTION",

author = "Elin Abraham and Bailey, {Callum W.} and Claridge, {Timothy D. W.} and Davies, {Stephen G.} and Ling, {Kenneth B.} and Barbara Odell and Rees, {Thomas L.} and Roberts, {Paul M.} and Russell, {Angela J.} and Smith, {Andrew D.} and Smith, {Lorna J.} and Storr, {Helen R.} and Sweet, {Miles J.} and Thompson, {Amber L.} and Thomson, {James E.} and Tranter, {George E.} and Watkin, {David J.} and Smith, {Andrew David}",

year = "2010",

month = jul,

day = "14",

doi = "10.1016/j.tetasy.2010.06.001",

language = "English",

volume = "21",

pages = "1797--1815",

journal = "Tetrahedron: Asymmetry",

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Abraham, E, Bailey, CW, Claridge, TDW, Davies, SG, Ling, KB, Odell, B, Rees, TL, Roberts, PM, Russell, AJ, Smith, AD, Smith, LJ, Storr, HR, Sweet, MJ, Thompson, AL, Thomson, JE, Tranter, GE, Watkin, DJ & Smith, AD 2010, 'A systematic study of the solid state and solution phase conformational preferences of beta-peptides derived from transpentacin', Tetrahedron: Asymmetry, vol. 21, no. 13-14, pp. 1797-1815. https://doi.org/10.1016/j.tetasy.2010.06.001

TY - JOUR

T1 - A systematic study of the solid state and solution phase conformational preferences of beta-peptides derived from transpentacin

AU - Abraham, Elin

AU - Bailey, Callum W.

AU - Claridge, Timothy D. W.

AU - Davies, Stephen G.

AU - Ling, Kenneth B.

AU - Odell, Barbara

AU - Rees, Thomas L.

AU - Roberts, Paul M.

AU - Russell, Angela J.

AU - Smith, Andrew D.

AU - Smith, Lorna J.

AU - Storr, Helen R.

AU - Sweet, Miles J.

AU - Thompson, Amber L.

AU - Thomson, James E.

AU - Tranter, George E.

AU - Watkin, David J.

AU - Smith, Andrew David

PY - 2010/7/14

Y1 - 2010/7/14

N2 - The solid state and solution phase conformational preferences of a homologous series of beta-peptides derived from (S,S)-2-aminocyclopentanecarboxylic acid (transpentacin) have been investigated using a variety of spectroscopic and crystallographic techniques. These studies indicate that the hexamer and pentamer persist as a 12-helix in both the solid state and solution phase. Although the conformational traits of a 12-helix are exhibited by oligomers with as few as three residues in the solid state, in solution the trimer exists as an equilibrium of many alternative conformers whilst the tetramer has been shown to predominantly exist in either a 12-helix or a turn-type conformation. (C) 2010 Elsevier Ltd. All rights reserved.

AB - The solid state and solution phase conformational preferences of a homologous series of beta-peptides derived from (S,S)-2-aminocyclopentanecarboxylic acid (transpentacin) have been investigated using a variety of spectroscopic and crystallographic techniques. These studies indicate that the hexamer and pentamer persist as a 12-helix in both the solid state and solution phase. Although the conformational traits of a 12-helix are exhibited by oligomers with as few as three residues in the solid state, in solution the trimer exists as an equilibrium of many alternative conformers whilst the tetramer has been shown to predominantly exist in either a 12-helix or a turn-type conformation. (C) 2010 Elsevier Ltd. All rights reserved.

KW - 2-AMINOCYCLOPENTANECARBOXYLIC ACID-DERIVATIVES

KW - HELICAL SECONDARY STRUCTURE

KW - DE-NOVO DESIGN

KW - ASYMMETRIC-SYNTHESIS

KW - AQUEOUS-SOLUTION

KW - FOLDAMERS

KW - RESIDUES

KW - (-)-(1R,2S)-CISPENTACIN

KW - HEXAPEPTIDE

KW - RESOLUTION

U2 - 10.1016/j.tetasy.2010.06.001

DO - 10.1016/j.tetasy.2010.06.001

M3 - Article

SN - 0957-4166

VL - 21

SP - 1797

EP - 1815

JO - Tetrahedron: Asymmetry

JF - Tetrahedron: Asymmetry

IS - 13-14

ER -

A systematic study of the solid state and solution phase conformational preferences of beta-peptides derived from transpentacin

Abstract

Keywords

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