Conformational recovery and preservation of protein nature from heat-induced denaturation by water-soluble phospholipid polymer conjugation

Ji-Hun Seo, Ryosuke Matsuno, Yan Lee, Madoka Takai, Kazuhiko Ishihara

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

The effect of water-soluble phospholipid polymer conjugated to a protein on conformational change during heat-quenched stress was investigated in this study. Well-defined pyridine disulfide end-functional poly(2-methacryloyloxyethyl phosphorylcholine) (PMPC) was synthesized by well controlled atom transfer radical polymerization method. Synthesized PMPC was the site specifically conjugated to a protein, and the effect on conformational change during heat-quenched stress was estimated by circular dichroism and fluorescence study. As a result, a single phospholipid polymer chain conjugated to a protein give a great effect on conformational preservation in both secondary and tertiary structures even after the heat-quenced process. Moreover, even the conformational recovery which gave the completely reversible conformational preservation was observed in circular dichroism study. The resulting protein activity was also confirmed, and no significant decline was induced by heat-quenched stress.

Original languageEnglish
Pages (from-to)4859-4867
Number of pages9
JournalBiomaterials
Volume30
Issue number28
DOIs
Publication statusPublished - 2009 Oct 1
Externally publishedYes

Fingerprint

Denaturation
Phospholipids
Polymers
Hot Temperature
Proteins
Recovery
Water
Dichroism
Circular Dichroism
Atom transfer radical polymerization
Conjugated polymers
Polymerization
Disulfides
Pyridine
Fluorescence
poly(2-methacryloyloxyethyl-phosphorylcholine)

Keywords

  • Bioconjugation
  • Conformation change
  • Enzyme
  • Phospholipid polymer
  • Protein

ASJC Scopus subject areas

  • Biomaterials
  • Bioengineering
  • Ceramics and Composites
  • Mechanics of Materials
  • Biophysics

Cite this

Conformational recovery and preservation of protein nature from heat-induced denaturation by water-soluble phospholipid polymer conjugation. / Seo, Ji-Hun; Matsuno, Ryosuke; Lee, Yan; Takai, Madoka; Ishihara, Kazuhiko.

In: Biomaterials, Vol. 30, No. 28, 01.10.2009, p. 4859-4867.

Research output: Contribution to journalArticle

Seo, Ji-Hun ; Matsuno, Ryosuke ; Lee, Yan ; Takai, Madoka ; Ishihara, Kazuhiko. / Conformational recovery and preservation of protein nature from heat-induced denaturation by water-soluble phospholipid polymer conjugation. In: Biomaterials. 2009 ; Vol. 30, No. 28. pp. 4859-4867.
@article{736025dbfe104f2b918115d4800da6d6,
title = "Conformational recovery and preservation of protein nature from heat-induced denaturation by water-soluble phospholipid polymer conjugation",
abstract = "The effect of water-soluble phospholipid polymer conjugated to a protein on conformational change during heat-quenched stress was investigated in this study. Well-defined pyridine disulfide end-functional poly(2-methacryloyloxyethyl phosphorylcholine) (PMPC) was synthesized by well controlled atom transfer radical polymerization method. Synthesized PMPC was the site specifically conjugated to a protein, and the effect on conformational change during heat-quenched stress was estimated by circular dichroism and fluorescence study. As a result, a single phospholipid polymer chain conjugated to a protein give a great effect on conformational preservation in both secondary and tertiary structures even after the heat-quenced process. Moreover, even the conformational recovery which gave the completely reversible conformational preservation was observed in circular dichroism study. The resulting protein activity was also confirmed, and no significant decline was induced by heat-quenched stress.",
keywords = "Bioconjugation, Conformation change, Enzyme, Phospholipid polymer, Protein",
author = "Ji-Hun Seo and Ryosuke Matsuno and Yan Lee and Madoka Takai and Kazuhiko Ishihara",
year = "2009",
month = "10",
day = "1",
doi = "10.1016/j.biomaterials.2009.05.080",
language = "English",
volume = "30",
pages = "4859--4867",
journal = "Biomaterials",
issn = "0142-9612",
publisher = "Elsevier BV",
number = "28",

}

TY - JOUR

T1 - Conformational recovery and preservation of protein nature from heat-induced denaturation by water-soluble phospholipid polymer conjugation

AU - Seo, Ji-Hun

AU - Matsuno, Ryosuke

AU - Lee, Yan

AU - Takai, Madoka

AU - Ishihara, Kazuhiko

PY - 2009/10/1

Y1 - 2009/10/1

N2 - The effect of water-soluble phospholipid polymer conjugated to a protein on conformational change during heat-quenched stress was investigated in this study. Well-defined pyridine disulfide end-functional poly(2-methacryloyloxyethyl phosphorylcholine) (PMPC) was synthesized by well controlled atom transfer radical polymerization method. Synthesized PMPC was the site specifically conjugated to a protein, and the effect on conformational change during heat-quenched stress was estimated by circular dichroism and fluorescence study. As a result, a single phospholipid polymer chain conjugated to a protein give a great effect on conformational preservation in both secondary and tertiary structures even after the heat-quenced process. Moreover, even the conformational recovery which gave the completely reversible conformational preservation was observed in circular dichroism study. The resulting protein activity was also confirmed, and no significant decline was induced by heat-quenched stress.

AB - The effect of water-soluble phospholipid polymer conjugated to a protein on conformational change during heat-quenched stress was investigated in this study. Well-defined pyridine disulfide end-functional poly(2-methacryloyloxyethyl phosphorylcholine) (PMPC) was synthesized by well controlled atom transfer radical polymerization method. Synthesized PMPC was the site specifically conjugated to a protein, and the effect on conformational change during heat-quenched stress was estimated by circular dichroism and fluorescence study. As a result, a single phospholipid polymer chain conjugated to a protein give a great effect on conformational preservation in both secondary and tertiary structures even after the heat-quenced process. Moreover, even the conformational recovery which gave the completely reversible conformational preservation was observed in circular dichroism study. The resulting protein activity was also confirmed, and no significant decline was induced by heat-quenched stress.

KW - Bioconjugation

KW - Conformation change

KW - Enzyme

KW - Phospholipid polymer

KW - Protein

UR - http://www.scopus.com/inward/record.url?scp=67849090379&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=67849090379&partnerID=8YFLogxK

U2 - 10.1016/j.biomaterials.2009.05.080

DO - 10.1016/j.biomaterials.2009.05.080

M3 - Article

C2 - 19545892

AN - SCOPUS:67849090379

VL - 30

SP - 4859

EP - 4867

JO - Biomaterials

JF - Biomaterials

SN - 0142-9612

IS - 28

ER -