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.
| Original language | English |
|---|---|
| Pages (from-to) | 3959-3964 |
| Number of pages | 6 |
| Journal | Chemistry - A European Journal |
| Volume | 24 |
| Issue number | 16 |
| DOIs | |
| Publication status | Published - Mar 15 2018 |
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All Science Journal Classification (ASJC) codes
- Catalysis
- Organic Chemistry
Cite this
Bioconjugation with Thiols by Benzylic Substitution. / Watanabe, Kenji; Ohshima, Takashi.
In: Chemistry - A European Journal, Vol. 24, No. 16, 15.03.2018, p. 3959-3964.Research output: Contribution to journal › Article
}
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.
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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 -