Surface chemistry and spectroscopic studies of the native phenylalanine dehydrogenase Langmuir monolayer at the air/aqueous NaCl interface

Rafael Leonardo Cruz Gomes da Silva, Shiv K. Sharma, Suraj Paudyal, Keenan J. Mintz, Luciano Caseli, Roger M. Leblanc

Research output: Contribution to journalArticle

Abstract

This study investigates the main aspects of the surface behavior of the native phenylalanine dehydrogenase (PheDH) enzyme at the air/aqueous interface employing a saline subphase to induce the enzyme surface activity. Surface chemistry experiments were performed in order to determine the surface packing and stability of the formed layer, while spectroscopic experiments provided information regarding its secondary structure conformation. It was found that the PheDH enzyme forms a fluid film, which is quite homogeneous throughout its entire compression, being stable for long periods of time with no significant evidence of aggregates or irreversible domains during interfacial compression/decompression processes. The main secondary structures of the interfacial PheDH film were accessed via in situ reflectance-absorbance infrared spectroscopy, indicating a majority presence of α-helices, which were maintained after the film transfer to solid muscovite supports. The immobilized films presented a homogeneous and regular deposition, with controlled roughness and a mean thickness in the range of 8–10 nm.

Original languageEnglish (US)
Pages (from-to)458-466
Number of pages9
JournalJournal of Colloid And Interface Science
Volume560
DOIs
StatePublished - Feb 15 2020

Fingerprint

Surface chemistry
Monolayers
Enzymes
Air
Conformations
Infrared spectroscopy
Compaction
Surface roughness
Experiments
Fluids
Oxidoreductases
phenylalanine oxidase

Keywords

  • Langmuir monolayer
  • Langmuir-Blodgett film
  • Phenylalanine dehydrogenase
  • Reflectance-absorbance infrared spectroscopy
  • Surface chemistry

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Biomaterials
  • Surfaces, Coatings and Films
  • Colloid and Surface Chemistry

Cite this

Surface chemistry and spectroscopic studies of the native phenylalanine dehydrogenase Langmuir monolayer at the air/aqueous NaCl interface. / da Silva, Rafael Leonardo Cruz Gomes; Sharma, Shiv K.; Paudyal, Suraj; Mintz, Keenan J.; Caseli, Luciano; Leblanc, Roger M.

In: Journal of Colloid And Interface Science, Vol. 560, 15.02.2020, p. 458-466.

Research output: Contribution to journalArticle

da Silva, Rafael Leonardo Cruz Gomes ; Sharma, Shiv K. ; Paudyal, Suraj ; Mintz, Keenan J. ; Caseli, Luciano ; Leblanc, Roger M. / Surface chemistry and spectroscopic studies of the native phenylalanine dehydrogenase Langmuir monolayer at the air/aqueous NaCl interface. In: Journal of Colloid And Interface Science. 2020 ; Vol. 560. pp. 458-466.
@article{e0affecd1cdd4bf89eb723532e0be74e,
title = "Surface chemistry and spectroscopic studies of the native phenylalanine dehydrogenase Langmuir monolayer at the air/aqueous NaCl interface",
abstract = "This study investigates the main aspects of the surface behavior of the native phenylalanine dehydrogenase (PheDH) enzyme at the air/aqueous interface employing a saline subphase to induce the enzyme surface activity. Surface chemistry experiments were performed in order to determine the surface packing and stability of the formed layer, while spectroscopic experiments provided information regarding its secondary structure conformation. It was found that the PheDH enzyme forms a fluid film, which is quite homogeneous throughout its entire compression, being stable for long periods of time with no significant evidence of aggregates or irreversible domains during interfacial compression/decompression processes. The main secondary structures of the interfacial PheDH film were accessed via in situ reflectance-absorbance infrared spectroscopy, indicating a majority presence of α-helices, which were maintained after the film transfer to solid muscovite supports. The immobilized films presented a homogeneous and regular deposition, with controlled roughness and a mean thickness in the range of 8–10 nm.",
keywords = "Langmuir monolayer, Langmuir-Blodgett film, Phenylalanine dehydrogenase, Reflectance-absorbance infrared spectroscopy, Surface chemistry",
author = "{da Silva}, {Rafael Leonardo Cruz Gomes} and Sharma, {Shiv K.} and Suraj Paudyal and Mintz, {Keenan J.} and Luciano Caseli and Leblanc, {Roger M.}",
year = "2020",
month = "2",
day = "15",
doi = "10.1016/j.jcis.2019.10.086",
language = "English (US)",
volume = "560",
pages = "458--466",
journal = "Journal of Colloid and Interface Science",
issn = "0021-9797",
publisher = "Academic Press Inc.",

}

TY - JOUR

T1 - Surface chemistry and spectroscopic studies of the native phenylalanine dehydrogenase Langmuir monolayer at the air/aqueous NaCl interface

AU - da Silva, Rafael Leonardo Cruz Gomes

AU - Sharma, Shiv K.

AU - Paudyal, Suraj

AU - Mintz, Keenan J.

AU - Caseli, Luciano

AU - Leblanc, Roger M.

PY - 2020/2/15

Y1 - 2020/2/15

N2 - This study investigates the main aspects of the surface behavior of the native phenylalanine dehydrogenase (PheDH) enzyme at the air/aqueous interface employing a saline subphase to induce the enzyme surface activity. Surface chemistry experiments were performed in order to determine the surface packing and stability of the formed layer, while spectroscopic experiments provided information regarding its secondary structure conformation. It was found that the PheDH enzyme forms a fluid film, which is quite homogeneous throughout its entire compression, being stable for long periods of time with no significant evidence of aggregates or irreversible domains during interfacial compression/decompression processes. The main secondary structures of the interfacial PheDH film were accessed via in situ reflectance-absorbance infrared spectroscopy, indicating a majority presence of α-helices, which were maintained after the film transfer to solid muscovite supports. The immobilized films presented a homogeneous and regular deposition, with controlled roughness and a mean thickness in the range of 8–10 nm.

AB - This study investigates the main aspects of the surface behavior of the native phenylalanine dehydrogenase (PheDH) enzyme at the air/aqueous interface employing a saline subphase to induce the enzyme surface activity. Surface chemistry experiments were performed in order to determine the surface packing and stability of the formed layer, while spectroscopic experiments provided information regarding its secondary structure conformation. It was found that the PheDH enzyme forms a fluid film, which is quite homogeneous throughout its entire compression, being stable for long periods of time with no significant evidence of aggregates or irreversible domains during interfacial compression/decompression processes. The main secondary structures of the interfacial PheDH film were accessed via in situ reflectance-absorbance infrared spectroscopy, indicating a majority presence of α-helices, which were maintained after the film transfer to solid muscovite supports. The immobilized films presented a homogeneous and regular deposition, with controlled roughness and a mean thickness in the range of 8–10 nm.

KW - Langmuir monolayer

KW - Langmuir-Blodgett film

KW - Phenylalanine dehydrogenase

KW - Reflectance-absorbance infrared spectroscopy

KW - Surface chemistry

UR - http://www.scopus.com/inward/record.url?scp=85074497703&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85074497703&partnerID=8YFLogxK

U2 - 10.1016/j.jcis.2019.10.086

DO - 10.1016/j.jcis.2019.10.086

M3 - Article

C2 - 31677813

AN - SCOPUS:85074497703

VL - 560

SP - 458

EP - 466

JO - Journal of Colloid and Interface Science

JF - Journal of Colloid and Interface Science

SN - 0021-9797

ER -