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Titolo:
X-ray scattering studies of maquette peptide monolayers. 1. Reflectivity and grazing incidence diffraction at the air/water interface
Autore:
Strzalka, J; Chen, XX; Moser, CC; Dutton, PL; Ocko, BM; Blasie, JK;
Indirizzi:
Univ Penn, Dept Chem, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 Dept Chem, Philadelphia, PA 19104 USA Univ Penn, Dept Biochem & Biophys, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 & Biophys, Philadelphia, PA 19104 USA Brookhaven Natl Lab, Dept Phys, Upton, NY 11973 USA Brookhaven Natl Lab Upton NY USA 11973 ab, Dept Phys, Upton, NY 11973 USA
Titolo Testata:
LANGMUIR
fascicolo: 26, volume: 16, anno: 2000,
pagine: 10404 - 10418
SICI:
0743-7463(200012)16:26<10404:XSSOMP>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROFILE STRUCTURES; PROTEIN; SURFACE; MULTILAYERS; SCAFFOLD; DESIGN; FILMS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Strzalka, J Univ Penn, Dept Chem, Box 141, Philadelphia, PA 19104 USA UnivPenn Box 141 Philadelphia PA USA 19104 phia, PA 19104 USA
Citazione:
J. Strzalka et al., "X-ray scattering studies of maquette peptide monolayers. 1. Reflectivity and grazing incidence diffraction at the air/water interface", LANGMUIR, 16(26), 2000, pp. 10404-10418

Abstract

We present isotherm and X-ray reflectivity (XR) measurements from Langmuirmonolayers of a de novo synthetic di-alpha -helical peptide; consisting oftwo identical 31-residue, mostly alpha -helical peptide units joined by a disulfide bond at their amino-termini. Fitting the XR data to slab models shows that the dihelices lie in the plane of the interface at low pressures. The monolayers were insufficiently stable for study at high pressures, butLangmuir films based on a derivative of the peptide alkylated at its aminotermini permitted investigations over a larger range of pressures. We observed an orientational transition, in which the alpha -helices begin by lying in the plane of the interface at low surface pressures and orient themselves approximately normal to the interface at high pressures. We draw the same conclusions from the XR data when we analyze it using box refinement, aniterative, model-independent method for recovering structure from XR data. Mixtures of these palmitoylated peptides with a fatty acid (palmitic acid)or a phospholipid (DLPE) behaved similarly. None of the systems produced peaks in the grazing incidence diffraction signal indicative of long-range ordering of the upright a-helices. Off-specular in-plane scattering measurements based on the difference signal between the peptide/DLPE mixture and pure DLPE suggest that the peptide achieves only liquidlike order within the plane. We discuss the implications and prospects for future work on designed peptide monolayers incorporating prosthetic groups that could be used to study electron transfer in proteins and provide a basis for biomolecular electronics applications.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 10:05:04