Different expression systems resulted in varied binding properties of anti-paclitaxel single-chain variable fragment antibody clone 1C2

Gorawit Yusakul, Seiichi Sakamoto, Poomraphie Nuntawong, Hiroyuki Tanaka, Satoshi Morimoto

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

The binding properties of recombinant antibody fragments, such as affinity and specificity, determine their usefulness for therapeutic and analytical applications. Anti-paclitaxel single-chain variable fragment clone 1C2 (anti-PT scFv1C2) was expressed using Escherichia coli cell and Bombyx mori larvae expression systems. The binding characteristics of the scFvs were evaluated using indirect competitive ELISA. The linear range of binding between anti-PT scFv1C2 and paclitaxel was significantly different between the anti-PT scFv1C2s derived from E. coli (1.056–5.700 μg/ml) and B. mori (7.813–1000 ng/ml), which indicated that different expression systems resulted in different sensitivities for paclitaxel determination. In addition, the binding specificity of anti-PT scFv1C2 varied between expression systems. This finding implied that the expression system significantly affects the binding properties of recombinant antibodies, especially antibodies against low-molecular-weight targets.

Original languageEnglish
Pages (from-to)310-316
Number of pages7
JournalJournal of Natural Medicines
Volume72
Issue number1
DOIs
Publication statusPublished - Jan 1 2018

Fingerprint

Single-Chain Antibodies
Paclitaxel
Bombyx
Clone Cells
Escherichia coli
Immunoglobulin Fragments
Antibodies
Larva
Molecular Weight
Enzyme-Linked Immunosorbent Assay
Molecular weight
Therapeutics

All Science Journal Classification (ASJC) codes

  • Pharmaceutical Science
  • Drug Discovery
  • Complementary and alternative medicine
  • Organic Chemistry

Cite this

Different expression systems resulted in varied binding properties of anti-paclitaxel single-chain variable fragment antibody clone 1C2. / Yusakul, Gorawit; Sakamoto, Seiichi; Nuntawong, Poomraphie; Tanaka, Hiroyuki; Morimoto, Satoshi.

In: Journal of Natural Medicines, Vol. 72, No. 1, 01.01.2018, p. 310-316.

Research output: Contribution to journalArticle

@article{42fe43922be54979be6d21b20b07573c,
title = "Different expression systems resulted in varied binding properties of anti-paclitaxel single-chain variable fragment antibody clone 1C2",
abstract = "The binding properties of recombinant antibody fragments, such as affinity and specificity, determine their usefulness for therapeutic and analytical applications. Anti-paclitaxel single-chain variable fragment clone 1C2 (anti-PT scFv1C2) was expressed using Escherichia coli cell and Bombyx mori larvae expression systems. The binding characteristics of the scFvs were evaluated using indirect competitive ELISA. The linear range of binding between anti-PT scFv1C2 and paclitaxel was significantly different between the anti-PT scFv1C2s derived from E. coli (1.056–5.700 μg/ml) and B. mori (7.813–1000 ng/ml), which indicated that different expression systems resulted in different sensitivities for paclitaxel determination. In addition, the binding specificity of anti-PT scFv1C2 varied between expression systems. This finding implied that the expression system significantly affects the binding properties of recombinant antibodies, especially antibodies against low-molecular-weight targets.",
author = "Gorawit Yusakul and Seiichi Sakamoto and Poomraphie Nuntawong and Hiroyuki Tanaka and Satoshi Morimoto",
year = "2018",
month = "1",
day = "1",
doi = "10.1007/s11418-017-1136-z",
language = "English",
volume = "72",
pages = "310--316",
journal = "Journal of Natural Medicines",
issn = "1340-3443",
publisher = "Springer Verlag",
number = "1",

}

TY - JOUR

T1 - Different expression systems resulted in varied binding properties of anti-paclitaxel single-chain variable fragment antibody clone 1C2

AU - Yusakul, Gorawit

AU - Sakamoto, Seiichi

AU - Nuntawong, Poomraphie

AU - Tanaka, Hiroyuki

AU - Morimoto, Satoshi

PY - 2018/1/1

Y1 - 2018/1/1

N2 - The binding properties of recombinant antibody fragments, such as affinity and specificity, determine their usefulness for therapeutic and analytical applications. Anti-paclitaxel single-chain variable fragment clone 1C2 (anti-PT scFv1C2) was expressed using Escherichia coli cell and Bombyx mori larvae expression systems. The binding characteristics of the scFvs were evaluated using indirect competitive ELISA. The linear range of binding between anti-PT scFv1C2 and paclitaxel was significantly different between the anti-PT scFv1C2s derived from E. coli (1.056–5.700 μg/ml) and B. mori (7.813–1000 ng/ml), which indicated that different expression systems resulted in different sensitivities for paclitaxel determination. In addition, the binding specificity of anti-PT scFv1C2 varied between expression systems. This finding implied that the expression system significantly affects the binding properties of recombinant antibodies, especially antibodies against low-molecular-weight targets.

AB - The binding properties of recombinant antibody fragments, such as affinity and specificity, determine their usefulness for therapeutic and analytical applications. Anti-paclitaxel single-chain variable fragment clone 1C2 (anti-PT scFv1C2) was expressed using Escherichia coli cell and Bombyx mori larvae expression systems. The binding characteristics of the scFvs were evaluated using indirect competitive ELISA. The linear range of binding between anti-PT scFv1C2 and paclitaxel was significantly different between the anti-PT scFv1C2s derived from E. coli (1.056–5.700 μg/ml) and B. mori (7.813–1000 ng/ml), which indicated that different expression systems resulted in different sensitivities for paclitaxel determination. In addition, the binding specificity of anti-PT scFv1C2 varied between expression systems. This finding implied that the expression system significantly affects the binding properties of recombinant antibodies, especially antibodies against low-molecular-weight targets.

UR - http://www.scopus.com/inward/record.url?scp=85031400722&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85031400722&partnerID=8YFLogxK

U2 - 10.1007/s11418-017-1136-z

DO - 10.1007/s11418-017-1136-z

M3 - Article

C2 - 29027080

AN - SCOPUS:85031400722

VL - 72

SP - 310

EP - 316

JO - Journal of Natural Medicines

JF - Journal of Natural Medicines

SN - 1340-3443

IS - 1

ER -