Biological and physicochemical evaluation of the conformational stability of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)

Yu Seok Youn; Min Jae Shin; Su Young Chae; Cheng Hao Jin; Tae Hyung Kim; Kang Choon Lee

doi:10.1007/s10529-006-9300-7

Biological and physicochemical evaluation of the conformational stability of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)

Yu Seok Youn, Min Jae Shin, Su Young Chae, Cheng Hao Jin, Tae Hyung Kim, Kang Choon Lee

Department of Pharmacy

Sungkyunkwan University

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

23 Scopus citations

Abstract

Tumor necrosis factor (TNF)-related, apoptosis-inducing ligand (Apo2L/TRAIL) has a unique homotrimeric structure, and its conformational stability is essential for its apoptotic activity. The conformational stability of a modified version of TRAIL(114-281) with two additional domains of histidine tag and isoleucine zipper [His-ILZ-TRAIL(114-281)] was evaluated in various pH environments according to three different biological or physicochemical considerations: cytotoxicity, antibody-binding affinity, and tertiary structure. The biological properties of His-ILZ-TRAIL(114-281) were the most stably maintained at pH 6.0. The physicochemical analyses (circular dichroism and fluorescence spectroscopy) demonstrate that its bioactivity loss by pH challenge was originated from its structural collapse as a homotrimer.

Original language	English
Pages (from-to)	713-721
Number of pages	9
Journal	Biotechnology Letters
Volume	29
Issue number	5
DOIs	https://doi.org/10.1007/s10529-006-9300-7
State	Published - May 2007

Keywords

Apoptosis
Conformational
Homotrimer
Stability
TRAIL

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This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1007/s10529-006-9300-7

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title = "Biological and physicochemical evaluation of the conformational stability of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)",

abstract = "Tumor necrosis factor (TNF)-related, apoptosis-inducing ligand (Apo2L/TRAIL) has a unique homotrimeric structure, and its conformational stability is essential for its apoptotic activity. The conformational stability of a modified version of TRAIL(114-281) with two additional domains of histidine tag and isoleucine zipper [His-ILZ-TRAIL(114-281)] was evaluated in various pH environments according to three different biological or physicochemical considerations: cytotoxicity, antibody-binding affinity, and tertiary structure. The biological properties of His-ILZ-TRAIL(114-281) were the most stably maintained at pH 6.0. The physicochemical analyses (circular dichroism and fluorescence spectroscopy) demonstrate that its bioactivity loss by pH challenge was originated from its structural collapse as a homotrimer.",

keywords = "Apoptosis, Conformational, Homotrimer, Stability, TRAIL",

author = "Youn, \{Yu Seok\} and Shin, \{Min Jae\} and Chae, \{Su Young\} and Jin, \{Cheng Hao\} and Kim, \{Tae Hyung\} and Lee, \{Kang Choon\}",

year = "2007",

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doi = "10.1007/s10529-006-9300-7",

language = "English",

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journal = "Biotechnology Letters",

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T1 - Biological and physicochemical evaluation of the conformational stability of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)

AU - Youn, Yu Seok

AU - Shin, Min Jae

AU - Chae, Su Young

AU - Jin, Cheng Hao

AU - Kim, Tae Hyung

AU - Lee, Kang Choon

PY - 2007/5

Y1 - 2007/5

N2 - Tumor necrosis factor (TNF)-related, apoptosis-inducing ligand (Apo2L/TRAIL) has a unique homotrimeric structure, and its conformational stability is essential for its apoptotic activity. The conformational stability of a modified version of TRAIL(114-281) with two additional domains of histidine tag and isoleucine zipper [His-ILZ-TRAIL(114-281)] was evaluated in various pH environments according to three different biological or physicochemical considerations: cytotoxicity, antibody-binding affinity, and tertiary structure. The biological properties of His-ILZ-TRAIL(114-281) were the most stably maintained at pH 6.0. The physicochemical analyses (circular dichroism and fluorescence spectroscopy) demonstrate that its bioactivity loss by pH challenge was originated from its structural collapse as a homotrimer.

AB - Tumor necrosis factor (TNF)-related, apoptosis-inducing ligand (Apo2L/TRAIL) has a unique homotrimeric structure, and its conformational stability is essential for its apoptotic activity. The conformational stability of a modified version of TRAIL(114-281) with two additional domains of histidine tag and isoleucine zipper [His-ILZ-TRAIL(114-281)] was evaluated in various pH environments according to three different biological or physicochemical considerations: cytotoxicity, antibody-binding affinity, and tertiary structure. The biological properties of His-ILZ-TRAIL(114-281) were the most stably maintained at pH 6.0. The physicochemical analyses (circular dichroism and fluorescence spectroscopy) demonstrate that its bioactivity loss by pH challenge was originated from its structural collapse as a homotrimer.

KW - Apoptosis

KW - Conformational

KW - Homotrimer

KW - Stability

KW - TRAIL

UR - https://www.scopus.com/pages/publications/34147103447

U2 - 10.1007/s10529-006-9300-7

DO - 10.1007/s10529-006-9300-7

M3 - Article

C2 - 17318333

AN - SCOPUS:34147103447

SN - 0141-5492

VL - 29

SP - 713

EP - 721

JO - Biotechnology Letters

JF - Biotechnology Letters

IS - 5

ER -

Biological and physicochemical evaluation of the conformational stability of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)

Abstract

Keywords

UN SDGs

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