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Titolo:
Metal complexation with Langmuir monolayers of histidyl peptide lipids
Autore:
Huo, Q; Sui, GD; Zheng, Y; Kele, P; Leblanc, RM; Hasegawa, T; Nishijo, J; Umemura, J;
Indirizzi:
Univ Miami, Ctr Supramol Sci, Dept Chem, Coral Gables, FL 33124 USA Univ Miami Coral Gables FL USA 33124 ept Chem, Coral Gables, FL 33124 USA Kobe Pharmaceut Univ, Higashinada Ku, Kobe, Hyogo 6588558, Japan Kobe Pharmaceut Univ Kobe Hyogo Japan 6588558 Kobe, Hyogo 6588558, Japan Kyoto Univ, Inst Chem Res, Kyoto 6110011, Japan Kyoto Univ Kyoto Japan 6110011 Univ, Inst Chem Res, Kyoto 6110011, Japan
Titolo Testata:
CHEMISTRY-A EUROPEAN JOURNAL
fascicolo: 22, volume: 7, anno: 2001,
pagine: 4796 - 4804
SICI:
0947-6539(20011119)7:22<4796:MCWLMO>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
GROWTH-MODULATING TRIPEPTIDE; AIR-WATER-INTERFACE; L-LYSINE; MOLECULAR RECOGNITION; AIR/WATER INTERFACE; AQUEOUS DIPEPTIDES; AMINO-ACIDS; COPPER(II); PLASMA; ZINC;
Keywords:
air-water interface; metal complexation; monolayers; peptides; surface chemistry;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Leblanc, RM Univ Miami, Ctr Supramol Sci, Dept Chem, 1301 Mem Dr Cox 315, Coral Gables, FL 33124 USA Univ Miami 1301 Mem Dr Cox 315 Coral Gables FL USA 33124 4 USA
Citazione:
Q. Huo et al., "Metal complexation with Langmuir monolayers of histidyl peptide lipids", CHEM-EUR J, 7(22), 2001, pp. 4796-4804

Abstract

Langmuir monolayers made from peptide-lipid molecules represent a novel direction in the research areas of biomimetic interfaces and two-dimensional supramolecular chemistry. Peptide structures and molecular recognition activities toward other guest molecules have been the focus of previous study. This study reports the investigation of metal complexation to histidine-containing peptide lipids in the organized Langmuir, Langmuir-Schaefer, or Langmuir-Blodgett films. Three peptide lipids PEPI-PEP3. with a histidine amino acid incorporated in the middle of the peptide, were designed and synthesized, The monolayer structures and metal-binding activities of each peptidelipid and their 1:1:1 molar ratio mixture were studied by thermodynamic and spectroscopic techniques. It was found that hard Lewis acid type metal cations such as K+ and Mg2+, and borderline or soft metal cations such as Zn2, Cu2+. and Cd2+ exhibit clearly different binding activity toward peptide-lipid monolayers. The conformational changes of peptides upon binding withCu2+, and Zn2+ were partially revealed by FT-IR spectroscopic studies. Furthermore. by adding a fluorescent-probe lipid to the peptide monolayer, dramatic fluorescence change was observed when Cu2+ or Zn2+ bound to the Langmuir and Langmuir-Schaefer films of peptide-lipid monolayers. Metal-protein complexation plays a crucial role in the function and activity of proteins and enzymes. Investigation of metal complexation to organized peptide Langmuir monolayers may provide an alternative approach for the development of artificial metalloproteins and novel supramolecular systems or materials.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 23:54:43