Assembly modes of hexaphenylalanine variants as function of the charge states of their terminal ends(10 views visite) Diaferia C, Balasco N, Altamura D, Sibillano T, Gallo E, Roviello V, Giannini C, Morelli G, Vitagliano L, Accardo A
Keywords Parole chiave: Not available. Non disponibili.
Affiliations Affiliazioni: *** IBB - CNR ***
Department of Pharmacy, Research Centre on Bioactive Peptides (CIRPeB), University of Naples "Federico II", Via Mezzocannone 16, 80134, Naples, Italy. antonella.accardo@unina.it.
Institute of Biostructures and Bioimaging (IBB), CNR, Via Mezzocannone 16, 80134, Naples, Italy.
Institute of Crystallography (IC), CNR, Via Amendola 122, 70126, Bari, Italy.
Analytical Chemistry for the Environment and CeSMA (Advanced Metrologic Service Center), University of Naples "Federico II", Corso Nicolangelo Protopisani, 80146, Naples, Italy.
References Riferimenti: Not available. Non disponibili.
Assembly modes of hexaphenylalanine variants as function of the charge states of their terminal ends
The ability of peptides to self-assemble represents a valuable tool for the development of biomaterials of biotechnological and/or biomedical interest. Diphenylalanine homodimer (FF) and its analogues are among the most promising systems in this field. The longest Phe-based building block hitherto characterized is pentaphenylalanine (F5). We studied the aggregation propensity and the structural/morphological features of assemblies of zwitterionic hexaphenylalanine H+-F6-O- and of three variants characterized by different charged states of the terminal ends (Ac-F6-Amide, H+-F6-Amide and Ac-F6-O-). As previously observed for PEGylated hexaphenylalanine (PEG8-F6), all F6 variants show a strong tendency to form β-rich assemblies in which the structural motif is constituted by antiparallel β-strands in the cross-β framework. Extensive replica exchange molecular dynamics simulations carried out on a pairs of F6 peptides indicate that the antiparallel β-structure of the final assemblies is likely dictated by the preferred association modes of the individual chains in the very early stages of the aggregation process. Our data suggest that even very small F6 peptides are properly pre-organized and prone to the build-up of the final assembly.
Assembly modes of hexaphenylalanine variants as function of the charge states of their terminal ends
Chattopadhyay A, Cogdell R, Crespo-hernandez CE, Datta A, De A, Haacke S, Hariharan M, Helliwell J, Hughes A, Improta R, Jones M, Joseph J, Karsili T, Kohler B, Krishnan R, Kuriakose A, L , M , Markovitsi D, Medhi H, Periyasamy G, Pradeepkumar PI, Roy Chowdhury P, Sarangi M, Schapiro I, Schertler GFX, Schlichting I, Segarra-marti J, Swaminathan R, V , V , Van Grondelle R, Venkatraman RK, Venkatramani R, Watts A * Light induced charge and energy transport in nucleic acids and proteins: general discussion(121 visite) Faraday Discuss (ISSN: 1359-6640print, 1359-6640linking), 2018 Apr 1; 207: 153-180. Impact Factor:4.194 DettagliEsporta in BibTeXEsporta in EndNote
Giuffrida M-, Tomasello F, Caraci F, Pandini G, Chiechio S, Battaglia G, De Bona P, Pappalardo G, Vigneri R, Nicoletti F, Rizzarelli E, Copani AG * A new function for beta-amyloid monomers(236 visite) Society For Neuroscience Abstract Viewer And Itinerary Planner, 2011; 41: N/D-N/D. Impact Factor:0 DettagliEsporta in BibTeXEsporta in EndNote
Bruni AC, Bernardi L, Colao R, Rubino E, Smirne N, Frangipane F, Terni B, Curcio SA, Mirabelli M, Clodomiro A, Di Lorenzo R, Maletta R, Anfossi M, Gallo M, Geracitano S, Tomaino C, Muraca MG, Leotta A, Lio SG, Pinessi L, Rainero I, Sorbi S, Nee L, Milan G, Pappata S, Postiglione A, Abbamondi N, Forloni G, St George Hyslop P, Rogaeva E, Bugiani O, Giaccone G, Foncin JF, Spillantini MG, Puccio G * Worldwide distribution of PSEN1 Met146Leu mutation: A large variability for a founder mutation(409 visite) Neurology (ISSN: 0028-3878, 1526-632x, 1526-632xelectronic), 2010 Mar 9; 74(10): 798-806. Impact Factor:8.017 DettagliEsporta in BibTeXEsporta in EndNote
Aloj L, Aurilio M, Rinaldi V, D'Ambrosio L, Tesauro D, Peitl PK, Maina T, Mansi R, Von Guggenberg E, Joosten L, Sosabowski JK, Breeman WA, De Blois E, Koelewijn S, Melis M, Waser B, Beetschen K, Reubi JC, De Jong M * The EEE project(387 visite) Proc Int Cosm Ray Conf Icrc Universidad Nacional Autonoma De Mexico, 2007; 5(HEPART2): 977-980. Impact Factor:0 DettagliEsporta in BibTeXEsporta in EndNote
Testino G, Leone S, Fagoonee S, Del Bas JM, Rodriguez B, Puiggros F, Marine S, Rodriguez MA, Morina D, Armengol L, Caimari A, Arola L, Cimini FA, Barchetta I, Carotti S, Bertoccini L, Baroni MG, Vespasiani-gentilucci U, Cavallo MG, Morini S, Nelson JE, Roth CL, Wilson LA, Yates KP, Aouizerat B, Morgan-stevenson V, Whalen E, Hoofnagle A, Mason M, Gersuk V, Yeh MM, Kowdley KV, Lee SM, Jun DW, Cho YK, Jang KS, Kucukazman M, Ata N, Dal K, Yeniova AO, Kefeli A, Basyigit S, Aktas B, Akin KO, Agladioglu K, Ure OS, Topal F, Nazligul Y, Beyan E, Ertugrul DT, Catena C, Cosma C, Camozzi V, Plebani M, Ermani M, Sechi LA, Fallo F, Goto Y, Ray MB, Mendenhall CL, French SW, Gartside PS Serum vitamin A deficiency and increased intrahepatic expression of cytokeratin antigen in alcoholic liver disease(433 visite) Hepatology (ISSN: 1827-1669electronic, 0026-4806linking), 1988 Sep; 83120693611123109(5): 1019-1026. Impact Factor:0.913 DettagliEsporta in BibTeXEsporta in EndNote
722 Records (652 escludendo Abstract e Conferenze). Impact factor totale: 2907.039 (2662.062 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 3087.937 (2783.335 escludendo Abstract e Conferenze).
Last modified by Ultima modifica di Marco Comerci on in data Wednesday 02 December 2020, 18:09:09 10 views visite. Last view on Ultima visita in data Tuesday 02 February 2021, 12:48:13