Peptides containing γ,δ,-dihydroxy-L-leucine

Benson J Edagwa, Carol M. Taylor

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

(Chemical Equation Presented) (±)-Dehydroleucine was prepared and resolved by porcine kidney acylase. Under the conditions of the Sharpless asymmetric dihydroxylation (SAD), employing AD-mix-α, Nα- carbobenzyloxy-(2S)-4,5-dehydroleucine methyl ester (16) gave rise to a 6.5:1.0 mixture of γ-lactones 17, favoring the 4R configuration. Such carbamate-protected α-amino-γ-hydroxylactones are not recommended as intermediates for peptide synthesis, since model studies showed that lactone 13 was unreactive toward amines. Moreover, the lactone ring could not be opened hydrolytically without epimerization at Cα. Nα-Carbobenzyloxy-(2S)- 4,5-dehydroleucine (22) was condensed with valine ethyl ester (19) to give dipeptide 23. Treatment of 23 with AD-mix-β, under the SAD conditions, converted the dehydroleucine residue to γ,δ-dihydroxyleucine with 4S configuration, as occurs in alloviroidin (3), a natural product isolated from Amanita suballiacea.

Original languageEnglish (US)
Pages (from-to)4132-4136
Number of pages5
JournalJournal of Organic Chemistry
Volume74
Issue number11
DOIs
StatePublished - Jun 5 2009

Fingerprint

Leucine
Lactones
Peptides
amidase
Esters
Carbamates
Dipeptides
Valine
Biological Products
Amines
dehydroleucine

ASJC Scopus subject areas

  • Organic Chemistry

Cite this

Peptides containing γ,δ,-dihydroxy-L-leucine. / Edagwa, Benson J; Taylor, Carol M.

In: Journal of Organic Chemistry, Vol. 74, No. 11, 05.06.2009, p. 4132-4136.

Research output: Contribution to journalArticle

Edagwa, Benson J ; Taylor, Carol M. / Peptides containing γ,δ,-dihydroxy-L-leucine. In: Journal of Organic Chemistry. 2009 ; Vol. 74, No. 11. pp. 4132-4136.
@article{9497738d0f3f4454bb1a46fbd4bcb1ed,
title = "Peptides containing γ,δ,-dihydroxy-L-leucine",
abstract = "(Chemical Equation Presented) (±)-Dehydroleucine was prepared and resolved by porcine kidney acylase. Under the conditions of the Sharpless asymmetric dihydroxylation (SAD), employing AD-mix-α, Nα- carbobenzyloxy-(2S)-4,5-dehydroleucine methyl ester (16) gave rise to a 6.5:1.0 mixture of γ-lactones 17, favoring the 4R configuration. Such carbamate-protected α-amino-γ-hydroxylactones are not recommended as intermediates for peptide synthesis, since model studies showed that lactone 13 was unreactive toward amines. Moreover, the lactone ring could not be opened hydrolytically without epimerization at Cα. Nα-Carbobenzyloxy-(2S)- 4,5-dehydroleucine (22) was condensed with valine ethyl ester (19) to give dipeptide 23. Treatment of 23 with AD-mix-β, under the SAD conditions, converted the dehydroleucine residue to γ,δ-dihydroxyleucine with 4S configuration, as occurs in alloviroidin (3), a natural product isolated from Amanita suballiacea.",
author = "Edagwa, {Benson J} and Taylor, {Carol M.}",
year = "2009",
month = "6",
day = "5",
doi = "10.1021/jo900459f",
language = "English (US)",
volume = "74",
pages = "4132--4136",
journal = "Journal of Organic Chemistry",
issn = "0022-3263",
publisher = "American Chemical Society",
number = "11",

}

TY - JOUR

T1 - Peptides containing γ,δ,-dihydroxy-L-leucine

AU - Edagwa, Benson J

AU - Taylor, Carol M.

PY - 2009/6/5

Y1 - 2009/6/5

N2 - (Chemical Equation Presented) (±)-Dehydroleucine was prepared and resolved by porcine kidney acylase. Under the conditions of the Sharpless asymmetric dihydroxylation (SAD), employing AD-mix-α, Nα- carbobenzyloxy-(2S)-4,5-dehydroleucine methyl ester (16) gave rise to a 6.5:1.0 mixture of γ-lactones 17, favoring the 4R configuration. Such carbamate-protected α-amino-γ-hydroxylactones are not recommended as intermediates for peptide synthesis, since model studies showed that lactone 13 was unreactive toward amines. Moreover, the lactone ring could not be opened hydrolytically without epimerization at Cα. Nα-Carbobenzyloxy-(2S)- 4,5-dehydroleucine (22) was condensed with valine ethyl ester (19) to give dipeptide 23. Treatment of 23 with AD-mix-β, under the SAD conditions, converted the dehydroleucine residue to γ,δ-dihydroxyleucine with 4S configuration, as occurs in alloviroidin (3), a natural product isolated from Amanita suballiacea.

AB - (Chemical Equation Presented) (±)-Dehydroleucine was prepared and resolved by porcine kidney acylase. Under the conditions of the Sharpless asymmetric dihydroxylation (SAD), employing AD-mix-α, Nα- carbobenzyloxy-(2S)-4,5-dehydroleucine methyl ester (16) gave rise to a 6.5:1.0 mixture of γ-lactones 17, favoring the 4R configuration. Such carbamate-protected α-amino-γ-hydroxylactones are not recommended as intermediates for peptide synthesis, since model studies showed that lactone 13 was unreactive toward amines. Moreover, the lactone ring could not be opened hydrolytically without epimerization at Cα. Nα-Carbobenzyloxy-(2S)- 4,5-dehydroleucine (22) was condensed with valine ethyl ester (19) to give dipeptide 23. Treatment of 23 with AD-mix-β, under the SAD conditions, converted the dehydroleucine residue to γ,δ-dihydroxyleucine with 4S configuration, as occurs in alloviroidin (3), a natural product isolated from Amanita suballiacea.

UR - http://www.scopus.com/inward/record.url?scp=66249111130&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=66249111130&partnerID=8YFLogxK

U2 - 10.1021/jo900459f

DO - 10.1021/jo900459f

M3 - Article

VL - 74

SP - 4132

EP - 4136

JO - Journal of Organic Chemistry

JF - Journal of Organic Chemistry

SN - 0022-3263

IS - 11

ER -