Bioconjugation with Thiols by Benzylic Substitution

Kenji Watanabe, Takashi Ohshima

研究成果: ジャーナルへの寄稿記事

1 引用 (Scopus)

抄録

A benzylic substitution of 3-indolyl(hydroxyl)acetate derivatives with thiols proceeded specifically in the presence of amino, carboxy, and phosphate groups in weakly acidic aqueous solutions under nearly physiological condition, while no reaction occurred at pH over 7. Kinetic studies revealed that the reaction followed second-order kinetics (first-order in the reactant and first-order in thiol) in contrast with the SN1 mechanism of common benzylic substitution of alcohols. The utility of the present method for functionalization of biomacromolecules was demonstrated using several model proteins, such as lysozyme, insulin, trypsin, and serum albumin. The catalytic bioactivity of lysozyme in lysis of Micrococcus lysodeikticus cells was completely retained after the modification.

元の言語英語
ページ(範囲)3959-3964
ページ数6
ジャーナルChemistry - A European Journal
24
発行部数16
DOI
出版物ステータス出版済み - 3 15 2018

Fingerprint

Muramidase
Sulfhydryl Compounds
Substitution reactions
Enzymes
Kinetics
Insulin
Bioactivity
Serum Albumin
Hydroxyl Radical
Trypsin
Phosphates
Acetates
Alcohols
Derivatives
Proteins
carboxy phosphate

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Organic Chemistry

これを引用

Bioconjugation with Thiols by Benzylic Substitution. / Watanabe, Kenji; Ohshima, Takashi.

:: Chemistry - A European Journal, 巻 24, 番号 16, 15.03.2018, p. 3959-3964.

研究成果: ジャーナルへの寄稿記事

Watanabe, Kenji ; Ohshima, Takashi. / Bioconjugation with Thiols by Benzylic Substitution. :: Chemistry - A European Journal. 2018 ; 巻 24, 番号 16. pp. 3959-3964.
@article{9067439f5470487d83b6cea6cb7ad8aa,
title = "Bioconjugation with Thiols by Benzylic Substitution",
abstract = "A benzylic substitution of 3-indolyl(hydroxyl)acetate derivatives with thiols proceeded specifically in the presence of amino, carboxy, and phosphate groups in weakly acidic aqueous solutions under nearly physiological condition, while no reaction occurred at pH over 7. Kinetic studies revealed that the reaction followed second-order kinetics (first-order in the reactant and first-order in thiol) in contrast with the SN1 mechanism of common benzylic substitution of alcohols. The utility of the present method for functionalization of biomacromolecules was demonstrated using several model proteins, such as lysozyme, insulin, trypsin, and serum albumin. The catalytic bioactivity of lysozyme in lysis of Micrococcus lysodeikticus cells was completely retained after the modification.",
author = "Kenji Watanabe and Takashi Ohshima",
year = "2018",
month = "3",
day = "15",
doi = "10.1002/chem.201706149",
language = "English",
volume = "24",
pages = "3959--3964",
journal = "Chemistry - A European Journal",
issn = "0947-6539",
publisher = "Wiley-VCH Verlag",
number = "16",

}

TY - JOUR

T1 - Bioconjugation with Thiols by Benzylic Substitution

AU - Watanabe, Kenji

AU - Ohshima, Takashi

PY - 2018/3/15

Y1 - 2018/3/15

N2 - A benzylic substitution of 3-indolyl(hydroxyl)acetate derivatives with thiols proceeded specifically in the presence of amino, carboxy, and phosphate groups in weakly acidic aqueous solutions under nearly physiological condition, while no reaction occurred at pH over 7. Kinetic studies revealed that the reaction followed second-order kinetics (first-order in the reactant and first-order in thiol) in contrast with the SN1 mechanism of common benzylic substitution of alcohols. The utility of the present method for functionalization of biomacromolecules was demonstrated using several model proteins, such as lysozyme, insulin, trypsin, and serum albumin. The catalytic bioactivity of lysozyme in lysis of Micrococcus lysodeikticus cells was completely retained after the modification.

AB - A benzylic substitution of 3-indolyl(hydroxyl)acetate derivatives with thiols proceeded specifically in the presence of amino, carboxy, and phosphate groups in weakly acidic aqueous solutions under nearly physiological condition, while no reaction occurred at pH over 7. Kinetic studies revealed that the reaction followed second-order kinetics (first-order in the reactant and first-order in thiol) in contrast with the SN1 mechanism of common benzylic substitution of alcohols. The utility of the present method for functionalization of biomacromolecules was demonstrated using several model proteins, such as lysozyme, insulin, trypsin, and serum albumin. The catalytic bioactivity of lysozyme in lysis of Micrococcus lysodeikticus cells was completely retained after the modification.

UR - http://www.scopus.com/inward/record.url?scp=85042086068&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85042086068&partnerID=8YFLogxK

U2 - 10.1002/chem.201706149

DO - 10.1002/chem.201706149

M3 - Article

AN - SCOPUS:85042086068

VL - 24

SP - 3959

EP - 3964

JO - Chemistry - A European Journal

JF - Chemistry - A European Journal

SN - 0947-6539

IS - 16

ER -