Time-resolved fluorescence spectroscopy and molecular dynamics simulations point out the effects of pressure on the stability and dynamics of the porcine odorant-binding protein

Maria Staiano, Michele Saviano, Petr Herman, Zygmunt Grycznyski, Carlo Fini, Antonio Varriale, Antonietta Parracino, Ane Bisgaard Kold, Mosè Rossi, Sabato D'Auria

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

The effects of hydrostatic pressure on the structure and stability of porcine odorant-binding protein (pOBP) in the presence and absence of the odorant molecule 2-isobutyl-3-methoxypyrazine (IBMP) were studied by steady-state and time-resolved fluorescence spectroscopy as well as by molecular dynamics simulation. The authors found that the application of moderate values of hydrostatic pressure to pOBP solutions perturbed the microenvironment of Trp16 and disrupted its highly quenched complex with Met.39 In addition, compared with the protein in the absence of IBMP, the MD simulations experiments carried out at different pressures highlighted the role of this ligand in stabilizing the Trp16/Met39 interaction even at 2000 bar. The obtained results will assist for the tailoring of this protein as specific sensing element in a new class of fluorescence-based biosensors for the detection of explosives.

Original languageEnglish
Pages (from-to)284-291
Number of pages8
JournalBiopolymers
Volume89
Issue number4
DOIs
StatePublished - 1 Apr 2008

Fingerprint

Hydrostatic Pressure
Fluorescence Spectrometry
Fluorescence spectroscopy
Hydrostatic pressure
Molecular Dynamics Simulation
Molecular dynamics
Swine
Proteins
Pressure
Computer simulation
Biosensing Techniques
Biosensors
Fluorescence
Ligands
Molecules
Experiments
odorant-binding protein
Carrier Proteins
Odorants
2-isobutyl-3-methoxypyrazine

Keywords

  • Biosensors
  • Frequency-domain
  • Molecular dynamics
  • Proteins
  • Stability
  • Time-resolved fluorescence

Cite this

Staiano, Maria ; Saviano, Michele ; Herman, Petr ; Grycznyski, Zygmunt ; Fini, Carlo ; Varriale, Antonio ; Parracino, Antonietta ; Kold, Ane Bisgaard ; Rossi, Mosè ; D'Auria, Sabato. / Time-resolved fluorescence spectroscopy and molecular dynamics simulations point out the effects of pressure on the stability and dynamics of the porcine odorant-binding protein. In: Biopolymers. 2008 ; Vol. 89, No. 4. pp. 284-291.
@article{ec8f8d4b10264142b19cd6520d170174,
title = "Time-resolved fluorescence spectroscopy and molecular dynamics simulations point out the effects of pressure on the stability and dynamics of the porcine odorant-binding protein",
abstract = "The effects of hydrostatic pressure on the structure and stability of porcine odorant-binding protein (pOBP) in the presence and absence of the odorant molecule 2-isobutyl-3-methoxypyrazine (IBMP) were studied by steady-state and time-resolved fluorescence spectroscopy as well as by molecular dynamics simulation. The authors found that the application of moderate values of hydrostatic pressure to pOBP solutions perturbed the microenvironment of Trp16 and disrupted its highly quenched complex with Met.39 In addition, compared with the protein in the absence of IBMP, the MD simulations experiments carried out at different pressures highlighted the role of this ligand in stabilizing the Trp16/Met39 interaction even at 2000 bar. The obtained results will assist for the tailoring of this protein as specific sensing element in a new class of fluorescence-based biosensors for the detection of explosives.",
keywords = "Biosensors, Frequency-domain, Molecular dynamics, Proteins, Stability, Time-resolved fluorescence",
author = "Maria Staiano and Michele Saviano and Petr Herman and Zygmunt Grycznyski and Carlo Fini and Antonio Varriale and Antonietta Parracino and Kold, {Ane Bisgaard} and Mos{\`e} Rossi and Sabato D'Auria",
year = "2008",
month = "4",
day = "1",
doi = "10.1002/bip.20908",
language = "English",
volume = "89",
pages = "284--291",
journal = "Biopolymers",
issn = "0006-3525",
publisher = "John Wiley and Sons Inc.",
number = "4",

}

Time-resolved fluorescence spectroscopy and molecular dynamics simulations point out the effects of pressure on the stability and dynamics of the porcine odorant-binding protein. / Staiano, Maria; Saviano, Michele; Herman, Petr; Grycznyski, Zygmunt; Fini, Carlo; Varriale, Antonio; Parracino, Antonietta; Kold, Ane Bisgaard; Rossi, Mosè; D'Auria, Sabato.

In: Biopolymers, Vol. 89, No. 4, 01.04.2008, p. 284-291.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Time-resolved fluorescence spectroscopy and molecular dynamics simulations point out the effects of pressure on the stability and dynamics of the porcine odorant-binding protein

AU - Staiano, Maria

AU - Saviano, Michele

AU - Herman, Petr

AU - Grycznyski, Zygmunt

AU - Fini, Carlo

AU - Varriale, Antonio

AU - Parracino, Antonietta

AU - Kold, Ane Bisgaard

AU - Rossi, Mosè

AU - D'Auria, Sabato

PY - 2008/4/1

Y1 - 2008/4/1

N2 - The effects of hydrostatic pressure on the structure and stability of porcine odorant-binding protein (pOBP) in the presence and absence of the odorant molecule 2-isobutyl-3-methoxypyrazine (IBMP) were studied by steady-state and time-resolved fluorescence spectroscopy as well as by molecular dynamics simulation. The authors found that the application of moderate values of hydrostatic pressure to pOBP solutions perturbed the microenvironment of Trp16 and disrupted its highly quenched complex with Met.39 In addition, compared with the protein in the absence of IBMP, the MD simulations experiments carried out at different pressures highlighted the role of this ligand in stabilizing the Trp16/Met39 interaction even at 2000 bar. The obtained results will assist for the tailoring of this protein as specific sensing element in a new class of fluorescence-based biosensors for the detection of explosives.

AB - The effects of hydrostatic pressure on the structure and stability of porcine odorant-binding protein (pOBP) in the presence and absence of the odorant molecule 2-isobutyl-3-methoxypyrazine (IBMP) were studied by steady-state and time-resolved fluorescence spectroscopy as well as by molecular dynamics simulation. The authors found that the application of moderate values of hydrostatic pressure to pOBP solutions perturbed the microenvironment of Trp16 and disrupted its highly quenched complex with Met.39 In addition, compared with the protein in the absence of IBMP, the MD simulations experiments carried out at different pressures highlighted the role of this ligand in stabilizing the Trp16/Met39 interaction even at 2000 bar. The obtained results will assist for the tailoring of this protein as specific sensing element in a new class of fluorescence-based biosensors for the detection of explosives.

KW - Biosensors

KW - Frequency-domain

KW - Molecular dynamics

KW - Proteins

KW - Stability

KW - Time-resolved fluorescence

UR - http://www.scopus.com/inward/record.url?scp=42949170494&partnerID=8YFLogxK

U2 - 10.1002/bip.20908

DO - 10.1002/bip.20908

M3 - Article

C2 - 18098179

AN - SCOPUS:42949170494

VL - 89

SP - 284

EP - 291

JO - Biopolymers

JF - Biopolymers

SN - 0006-3525

IS - 4

ER -