Conformational resemblance between the structures of integrin-activating pentapetides derived from βig-h3 and RGD peptide analogues in a membrane environment

Sung Jean Park, Sangho Park, Hee Chul Ahn, In-San Kim, Bong Jin Lee

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

The peptides NKDIL and EPDIM, respectively derived from the 2nd and 4th domains of βig-h3, were fully active in mediating cell adhesion through interactions with α3β1 integrin [Biochem. Biophys. Res. Commun. 294 (2002) 940; J. Biol. Chem. 275 (2000) 30907]. Here, the conformational differences between NKDIL and EPDIM in water and in membrane environments were studied using CD spectroscopy, and their structures in sodium dodecylsulfate micelles were determined by NMR. The two peptides adopt β-turn structures like RGD peptides, and have more regular structures in micelles than in aqueous buffers. EPDIM shows a distorted type I β-turn for the PDIM segment in a membrane environment. The structure of NKDIL is similar with the standard type I′ β-turn, but shows large backbone flexibility even in a membrane environment. The conformational change of the 4th repeated domain of βig-h3 in micelle solutions suggests that the Asp-Ile motif of the 4th fas-1 domain (EPDIM) would be solvent-exposed and could interact with integrin α3β1 in a membrane environment. The present study provides a structural basis of βig-h3 function and information for the development of integrin-regulating drugs involving the wound healing protein.

Original languageEnglish
Pages (from-to)199-205
Number of pages7
JournalPeptides
Volume25
Issue number2
DOIs
Publication statusPublished - 2004 Feb 1
Externally publishedYes

Fingerprint

Integrins
Micelles
Membranes
Peptides
Cell adhesion
Cell Adhesion
Wound Healing
Spectrum Analysis
Buffers
Sodium
Nuclear magnetic resonance
Spectroscopy
arginyl-glycyl-aspartic acid
Water
Pharmaceutical Preparations
Proteins
Immunoglobulin Domains

Keywords

  • βig-h3
  • CD
  • EPDIM
  • Membrane-binding
  • NKDIL
  • NMR

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience

Cite this

Conformational resemblance between the structures of integrin-activating pentapetides derived from βig-h3 and RGD peptide analogues in a membrane environment. / Park, Sung Jean; Park, Sangho; Ahn, Hee Chul; Kim, In-San; Lee, Bong Jin.

In: Peptides, Vol. 25, No. 2, 01.02.2004, p. 199-205.

Research output: Contribution to journalArticle

@article{f80a7a13bc214228a06569bc358e4141,
title = "Conformational resemblance between the structures of integrin-activating pentapetides derived from βig-h3 and RGD peptide analogues in a membrane environment",
abstract = "The peptides NKDIL and EPDIM, respectively derived from the 2nd and 4th domains of βig-h3, were fully active in mediating cell adhesion through interactions with α3β1 integrin [Biochem. Biophys. Res. Commun. 294 (2002) 940; J. Biol. Chem. 275 (2000) 30907]. Here, the conformational differences between NKDIL and EPDIM in water and in membrane environments were studied using CD spectroscopy, and their structures in sodium dodecylsulfate micelles were determined by NMR. The two peptides adopt β-turn structures like RGD peptides, and have more regular structures in micelles than in aqueous buffers. EPDIM shows a distorted type I β-turn for the PDIM segment in a membrane environment. The structure of NKDIL is similar with the standard type I′ β-turn, but shows large backbone flexibility even in a membrane environment. The conformational change of the 4th repeated domain of βig-h3 in micelle solutions suggests that the Asp-Ile motif of the 4th fas-1 domain (EPDIM) would be solvent-exposed and could interact with integrin α3β1 in a membrane environment. The present study provides a structural basis of βig-h3 function and information for the development of integrin-regulating drugs involving the wound healing protein.",
keywords = "βig-h3, CD, EPDIM, Membrane-binding, NKDIL, NMR",
author = "Park, {Sung Jean} and Sangho Park and Ahn, {Hee Chul} and In-San Kim and Lee, {Bong Jin}",
year = "2004",
month = "2",
day = "1",
doi = "10.1016/j.peptides.2003.12.002",
language = "English",
volume = "25",
pages = "199--205",
journal = "Peptides",
issn = "0196-9781",
publisher = "Elsevier Inc.",
number = "2",

}

TY - JOUR

T1 - Conformational resemblance between the structures of integrin-activating pentapetides derived from βig-h3 and RGD peptide analogues in a membrane environment

AU - Park, Sung Jean

AU - Park, Sangho

AU - Ahn, Hee Chul

AU - Kim, In-San

AU - Lee, Bong Jin

PY - 2004/2/1

Y1 - 2004/2/1

N2 - The peptides NKDIL and EPDIM, respectively derived from the 2nd and 4th domains of βig-h3, were fully active in mediating cell adhesion through interactions with α3β1 integrin [Biochem. Biophys. Res. Commun. 294 (2002) 940; J. Biol. Chem. 275 (2000) 30907]. Here, the conformational differences between NKDIL and EPDIM in water and in membrane environments were studied using CD spectroscopy, and their structures in sodium dodecylsulfate micelles were determined by NMR. The two peptides adopt β-turn structures like RGD peptides, and have more regular structures in micelles than in aqueous buffers. EPDIM shows a distorted type I β-turn for the PDIM segment in a membrane environment. The structure of NKDIL is similar with the standard type I′ β-turn, but shows large backbone flexibility even in a membrane environment. The conformational change of the 4th repeated domain of βig-h3 in micelle solutions suggests that the Asp-Ile motif of the 4th fas-1 domain (EPDIM) would be solvent-exposed and could interact with integrin α3β1 in a membrane environment. The present study provides a structural basis of βig-h3 function and information for the development of integrin-regulating drugs involving the wound healing protein.

AB - The peptides NKDIL and EPDIM, respectively derived from the 2nd and 4th domains of βig-h3, were fully active in mediating cell adhesion through interactions with α3β1 integrin [Biochem. Biophys. Res. Commun. 294 (2002) 940; J. Biol. Chem. 275 (2000) 30907]. Here, the conformational differences between NKDIL and EPDIM in water and in membrane environments were studied using CD spectroscopy, and their structures in sodium dodecylsulfate micelles were determined by NMR. The two peptides adopt β-turn structures like RGD peptides, and have more regular structures in micelles than in aqueous buffers. EPDIM shows a distorted type I β-turn for the PDIM segment in a membrane environment. The structure of NKDIL is similar with the standard type I′ β-turn, but shows large backbone flexibility even in a membrane environment. The conformational change of the 4th repeated domain of βig-h3 in micelle solutions suggests that the Asp-Ile motif of the 4th fas-1 domain (EPDIM) would be solvent-exposed and could interact with integrin α3β1 in a membrane environment. The present study provides a structural basis of βig-h3 function and information for the development of integrin-regulating drugs involving the wound healing protein.

KW - βig-h3

KW - CD

KW - EPDIM

KW - Membrane-binding

KW - NKDIL

KW - NMR

UR - http://www.scopus.com/inward/record.url?scp=1942452237&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=1942452237&partnerID=8YFLogxK

U2 - 10.1016/j.peptides.2003.12.002

DO - 10.1016/j.peptides.2003.12.002

M3 - Article

VL - 25

SP - 199

EP - 205

JO - Peptides

JF - Peptides

SN - 0196-9781

IS - 2

ER -