Construction of di-scFv through a trivalent alkyne-azide 1,3-dipolar cycloaddition

Arutselvan Natarajan; Wenjun Du; Cheng Yi Xiong; Gerald L Denardo; Sally J. DeNardo; Jacquelyn Gervay-Hague

doi:10.1039/b611636a

Construction of di-scFv through a trivalent alkyne-azide 1,3-dipolar cycloaddition

Arutselvan Natarajan, Wenjun Du, Cheng Yi Xiong, Gerald L Denardo, Sally J. DeNardo, Jacquelyn Gervay-Hague

Research output: Contribution to journal › Article › peer-review

42 Scopus citations

Abstract

Heterofunctional azide and alkyne PEG-linkers have been synthesized and site specifically conjugated to scFv via a reactive thiol functionality; two scFv were coupled by copper catalyzed 1,3-dipolar cycloaddition to make divalent scFv (di-scFv) with an inter-scFv distance defined to provide divalent binding; antigen binding was maintained for the di-scFv construct and increased several times compared to that of the parent scFv; the cycloaddition reaction reported herein represents an important ligation strategy to covalently link macromolecular proteins and retain sensitive structural conformations.

Original language	English (US)
Pages (from-to)	695-697
Number of pages	3
Journal	Chemical Communications
Issue number	7
DOIs	https://doi.org/10.1039/b611636a
State	Published - 2007

ASJC Scopus subject areas

Chemistry(all)

Access to Document

10.1039/b611636a

Fingerprint Dive into the research topics of 'Construction of di-scFv through a trivalent alkyne-azide 1,3-dipolar cycloaddition'. Together they form a unique fingerprint.

Cite this

@article{0790c272caf04ad5960dbd4f84baf05b,

title = "Construction of di-scFv through a trivalent alkyne-azide 1,3-dipolar cycloaddition",

abstract = "Heterofunctional azide and alkyne PEG-linkers have been synthesized and site specifically conjugated to scFv via a reactive thiol functionality; two scFv were coupled by copper catalyzed 1,3-dipolar cycloaddition to make divalent scFv (di-scFv) with an inter-scFv distance defined to provide divalent binding; antigen binding was maintained for the di-scFv construct and increased several times compared to that of the parent scFv; the cycloaddition reaction reported herein represents an important ligation strategy to covalently link macromolecular proteins and retain sensitive structural conformations.",

author = "Arutselvan Natarajan and Wenjun Du and Xiong, {Cheng Yi} and Denardo, {Gerald L} and DeNardo, {Sally J.} and Jacquelyn Gervay-Hague",

year = "2007",

doi = "10.1039/b611636a",

language = "English (US)",

pages = "695--697",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "7",

}

TY - JOUR

T1 - Construction of di-scFv through a trivalent alkyne-azide 1,3-dipolar cycloaddition

AU - Natarajan, Arutselvan

AU - Du, Wenjun

AU - Xiong, Cheng Yi

AU - Denardo, Gerald L

AU - DeNardo, Sally J.

AU - Gervay-Hague, Jacquelyn

PY - 2007

Y1 - 2007

N2 - Heterofunctional azide and alkyne PEG-linkers have been synthesized and site specifically conjugated to scFv via a reactive thiol functionality; two scFv were coupled by copper catalyzed 1,3-dipolar cycloaddition to make divalent scFv (di-scFv) with an inter-scFv distance defined to provide divalent binding; antigen binding was maintained for the di-scFv construct and increased several times compared to that of the parent scFv; the cycloaddition reaction reported herein represents an important ligation strategy to covalently link macromolecular proteins and retain sensitive structural conformations.

AB - Heterofunctional azide and alkyne PEG-linkers have been synthesized and site specifically conjugated to scFv via a reactive thiol functionality; two scFv were coupled by copper catalyzed 1,3-dipolar cycloaddition to make divalent scFv (di-scFv) with an inter-scFv distance defined to provide divalent binding; antigen binding was maintained for the di-scFv construct and increased several times compared to that of the parent scFv; the cycloaddition reaction reported herein represents an important ligation strategy to covalently link macromolecular proteins and retain sensitive structural conformations.

UR - http://www.scopus.com/inward/record.url?scp=33846902068&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33846902068&partnerID=8YFLogxK

U2 - 10.1039/b611636a

DO - 10.1039/b611636a

M3 - Article

C2 - 17392953

AN - SCOPUS:33846902068

SP - 695

EP - 697

JO - Chemical Communications

JF - Chemical Communications

SN - 1359-7345

IS - 7

ER -