Partial poly(glutamic acid) ↔ poly(aspartic acid) exchange in layer-by-layer polyelectrolyte films. Structural alterations in the three-component architectures

Ana Maria Pilbat, Vincent Ball, Pierre Schaaf, Jean Claude Voegel, B. Szalontai

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

Layer-by-layer (LBL) polyelectrolyte films were constructed from poly(L-glutamic acid) (PGA) and poly(L-aspartic acid) (PAA) as polyanions, and from poly(L-lysine) (PLL) as the polycation. The terminating layer of the films was always PLL. According to attenuated total reflection Fourier transform infrared measurements, the PGA/PLL and PAA/PLL films, despite their chemical similarity, had largely different secondary structures. Extended β-sheets dominated the PGA/PLL films, while α-helices and intramolecular β-sheets dominated the PAA/PLL films. The secondary structure of the polyelectrolyte film affected the adsorption of human serum albumin (HSA) as well. HSA preserved its native secondary structure on the PGA/PLL film, but it became largely deformed on PAA/PLL films. Both PGA and PAA were able to extrude to a certain extent the other polyanion from the films, but the structural consequences were different. Adding PAA to a (PGA/PLL)5-PGA film resulted in a simple exchange and incorporation: PGA/PLL and PAA/PLL complexes coexisted with their unaltered secondary structures in the mixed film. The incorporation of PGA into a (PAA/PLL)5-PAA film was up to 50% and caused additional β-structure increase in the secondary structure of the film. The proportions of the two polyanions were roughly the same on the surfaces and in the interiors of the films, indicating practically free diffusion for both polyanions. The abundance of PAA/PLL and PGA/PLL domains on the film surfaces was monitored by the analysis of the amide I region of the infrared spectrum of a reporter molecule, HSA, adsorbed onto the three-component polyelectrolyte films.

Original languageEnglish
Pages (from-to)5753-5759
Number of pages7
JournalLangmuir
Volume22
Issue number13
DOIs
Publication statusPublished - Jun 20 2006

Fingerprint

aspartic acid
glutamic acid
Polyelectrolytes
Aspartic Acid
Phase locked loops
Prostaglandins A
Glutamic Acid
Ion exchange
Acids
albumins
Serum Albumin
serums
Infrared radiation
lysine

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Colloid and Surface Chemistry

Cite this

Partial poly(glutamic acid) ↔ poly(aspartic acid) exchange in layer-by-layer polyelectrolyte films. Structural alterations in the three-component architectures. / Pilbat, Ana Maria; Ball, Vincent; Schaaf, Pierre; Voegel, Jean Claude; Szalontai, B.

In: Langmuir, Vol. 22, No. 13, 20.06.2006, p. 5753-5759.

Research output: Contribution to journalArticle

@article{9fa1c94206a54fd39764c917ecc1e441,
title = "Partial poly(glutamic acid) ↔ poly(aspartic acid) exchange in layer-by-layer polyelectrolyte films. Structural alterations in the three-component architectures",
abstract = "Layer-by-layer (LBL) polyelectrolyte films were constructed from poly(L-glutamic acid) (PGA) and poly(L-aspartic acid) (PAA) as polyanions, and from poly(L-lysine) (PLL) as the polycation. The terminating layer of the films was always PLL. According to attenuated total reflection Fourier transform infrared measurements, the PGA/PLL and PAA/PLL films, despite their chemical similarity, had largely different secondary structures. Extended β-sheets dominated the PGA/PLL films, while α-helices and intramolecular β-sheets dominated the PAA/PLL films. The secondary structure of the polyelectrolyte film affected the adsorption of human serum albumin (HSA) as well. HSA preserved its native secondary structure on the PGA/PLL film, but it became largely deformed on PAA/PLL films. Both PGA and PAA were able to extrude to a certain extent the other polyanion from the films, but the structural consequences were different. Adding PAA to a (PGA/PLL)5-PGA film resulted in a simple exchange and incorporation: PGA/PLL and PAA/PLL complexes coexisted with their unaltered secondary structures in the mixed film. The incorporation of PGA into a (PAA/PLL)5-PAA film was up to 50{\%} and caused additional β-structure increase in the secondary structure of the film. The proportions of the two polyanions were roughly the same on the surfaces and in the interiors of the films, indicating practically free diffusion for both polyanions. The abundance of PAA/PLL and PGA/PLL domains on the film surfaces was monitored by the analysis of the amide I region of the infrared spectrum of a reporter molecule, HSA, adsorbed onto the three-component polyelectrolyte films.",
author = "Pilbat, {Ana Maria} and Vincent Ball and Pierre Schaaf and Voegel, {Jean Claude} and B. Szalontai",
year = "2006",
month = "6",
day = "20",
doi = "10.1021/la060454v",
language = "English",
volume = "22",
pages = "5753--5759",
journal = "Langmuir",
issn = "0743-7463",
publisher = "American Chemical Society",
number = "13",

}

TY - JOUR

T1 - Partial poly(glutamic acid) ↔ poly(aspartic acid) exchange in layer-by-layer polyelectrolyte films. Structural alterations in the three-component architectures

AU - Pilbat, Ana Maria

AU - Ball, Vincent

AU - Schaaf, Pierre

AU - Voegel, Jean Claude

AU - Szalontai, B.

PY - 2006/6/20

Y1 - 2006/6/20

N2 - Layer-by-layer (LBL) polyelectrolyte films were constructed from poly(L-glutamic acid) (PGA) and poly(L-aspartic acid) (PAA) as polyanions, and from poly(L-lysine) (PLL) as the polycation. The terminating layer of the films was always PLL. According to attenuated total reflection Fourier transform infrared measurements, the PGA/PLL and PAA/PLL films, despite their chemical similarity, had largely different secondary structures. Extended β-sheets dominated the PGA/PLL films, while α-helices and intramolecular β-sheets dominated the PAA/PLL films. The secondary structure of the polyelectrolyte film affected the adsorption of human serum albumin (HSA) as well. HSA preserved its native secondary structure on the PGA/PLL film, but it became largely deformed on PAA/PLL films. Both PGA and PAA were able to extrude to a certain extent the other polyanion from the films, but the structural consequences were different. Adding PAA to a (PGA/PLL)5-PGA film resulted in a simple exchange and incorporation: PGA/PLL and PAA/PLL complexes coexisted with their unaltered secondary structures in the mixed film. The incorporation of PGA into a (PAA/PLL)5-PAA film was up to 50% and caused additional β-structure increase in the secondary structure of the film. The proportions of the two polyanions were roughly the same on the surfaces and in the interiors of the films, indicating practically free diffusion for both polyanions. The abundance of PAA/PLL and PGA/PLL domains on the film surfaces was monitored by the analysis of the amide I region of the infrared spectrum of a reporter molecule, HSA, adsorbed onto the three-component polyelectrolyte films.

AB - Layer-by-layer (LBL) polyelectrolyte films were constructed from poly(L-glutamic acid) (PGA) and poly(L-aspartic acid) (PAA) as polyanions, and from poly(L-lysine) (PLL) as the polycation. The terminating layer of the films was always PLL. According to attenuated total reflection Fourier transform infrared measurements, the PGA/PLL and PAA/PLL films, despite their chemical similarity, had largely different secondary structures. Extended β-sheets dominated the PGA/PLL films, while α-helices and intramolecular β-sheets dominated the PAA/PLL films. The secondary structure of the polyelectrolyte film affected the adsorption of human serum albumin (HSA) as well. HSA preserved its native secondary structure on the PGA/PLL film, but it became largely deformed on PAA/PLL films. Both PGA and PAA were able to extrude to a certain extent the other polyanion from the films, but the structural consequences were different. Adding PAA to a (PGA/PLL)5-PGA film resulted in a simple exchange and incorporation: PGA/PLL and PAA/PLL complexes coexisted with their unaltered secondary structures in the mixed film. The incorporation of PGA into a (PAA/PLL)5-PAA film was up to 50% and caused additional β-structure increase in the secondary structure of the film. The proportions of the two polyanions were roughly the same on the surfaces and in the interiors of the films, indicating practically free diffusion for both polyanions. The abundance of PAA/PLL and PGA/PLL domains on the film surfaces was monitored by the analysis of the amide I region of the infrared spectrum of a reporter molecule, HSA, adsorbed onto the three-component polyelectrolyte films.

UR - http://www.scopus.com/inward/record.url?scp=33745761045&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33745761045&partnerID=8YFLogxK

U2 - 10.1021/la060454v

DO - 10.1021/la060454v

M3 - Article

C2 - 16768505

AN - SCOPUS:33745761045

VL - 22

SP - 5753

EP - 5759

JO - Langmuir

JF - Langmuir

SN - 0743-7463

IS - 13

ER -