Peptide Modification via N‑Terminal-Residue-Directed γ‑C(sp3)−H Arylation

Zhen Lin Hou; Feipeng Yuan; Bo Yao

doi:10.1021/acs.orglett.0c03279

Peptide Modification via N‑Terminal-Residue-Directed γ‑C(sp³)−H Arylation

Zhen Lin Hou
, Feipeng Yuan
, Bo Yao^*

^*此作品的通讯作者

Beijing Institute of Technology
CAS - Institute of Chemistry

科研成果: 期刊稿件 › 文章 › 同行评审

19 引用（Scopus）

摘要

Postassembly modification of peptides via C(sp³)−H functionalization provides an efficient way to prepare functionalized peptides for biological study and pharmaceutical development. In this work, we developed a new method for γ-C(sp³)−H functionalization of aliphatic side chains of N-terminus-unprotected peptides. With the N-terminal residues as directing groups, a wide range of di-, tri-, tetra-, and pentapeptides underwent C−H arylation of the residues (Val, Ile, Tle) at the +2 position from the N-terminus.

源语言	英语
页（从-至）	8692-8696
页数	5
期刊	Organic Letters
卷	22
期	21
DOI	https://doi.org/10.1021/acs.orglett.0c03279
出版状态	已出版 - 6 11月 2020
已对外发布	是

访问文件

10.1021/acs.orglett.0c03279

其它文件与链接

链接到 Scopus 的出版物

引用此

@article{884b0b9429a14af0aeaae7aa294d8074,

title = "Peptide Modification via N‑Terminal-Residue-Directed γ‑C(sp3)−H Arylation",

abstract = "Postassembly modification of peptides via C(sp3)−H functionalization provides an efficient way to prepare functionalized peptides for biological study and pharmaceutical development. In this work, we developed a new method for γ-C(sp3)−H functionalization of aliphatic side chains of N-terminus-unprotected peptides. With the N-terminal residues as directing groups, a wide range of di-, tri-, tetra-, and pentapeptides underwent C−H arylation of the residues (Val, Ile, Tle) at the +2 position from the N-terminus.",

author = "Hou, \{Zhen Lin\} and Feipeng Yuan and Bo Yao",

note = "Publisher Copyright: {\textcopyright} 2020 American Chemical Society.",

year = "2020",

month = nov,

day = "6",

doi = "10.1021/acs.orglett.0c03279",

language = "English",

volume = "22",

pages = "8692--8696",

journal = "Organic Letters",

issn = "1523-7060",

publisher = "American Chemical Society",

number = "21",

}

TY - JOUR

T1 - Peptide Modification via N‑Terminal-Residue-Directed γ‑C(sp3)−H Arylation

AU - Hou, Zhen Lin

AU - Yuan, Feipeng

AU - Yao, Bo

PY - 2020/11/6

Y1 - 2020/11/6

N2 - Postassembly modification of peptides via C(sp3)−H functionalization provides an efficient way to prepare functionalized peptides for biological study and pharmaceutical development. In this work, we developed a new method for γ-C(sp3)−H functionalization of aliphatic side chains of N-terminus-unprotected peptides. With the N-terminal residues as directing groups, a wide range of di-, tri-, tetra-, and pentapeptides underwent C−H arylation of the residues (Val, Ile, Tle) at the +2 position from the N-terminus.

AB - Postassembly modification of peptides via C(sp3)−H functionalization provides an efficient way to prepare functionalized peptides for biological study and pharmaceutical development. In this work, we developed a new method for γ-C(sp3)−H functionalization of aliphatic side chains of N-terminus-unprotected peptides. With the N-terminal residues as directing groups, a wide range of di-, tri-, tetra-, and pentapeptides underwent C−H arylation of the residues (Val, Ile, Tle) at the +2 position from the N-terminus.

UR - https://www.scopus.com/pages/publications/85095861545

U2 - 10.1021/acs.orglett.0c03279

DO - 10.1021/acs.orglett.0c03279

M3 - Article

C2 - 33075231

AN - SCOPUS:85095861545

SN - 1523-7060

VL - 22

SP - 8692

EP - 8696

JO - Organic Letters

JF - Organic Letters

IS - 21

ER -

Peptide Modification via N‑Terminal-Residue-Directed γ‑C(sp3)−H Arylation

摘要

访问文件

其它文件与链接

指纹

引用此

Peptide Modification via N‑Terminal-Residue-Directed γ‑C(sp³)−H Arylation