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abFig. 2. AFM images of Z-Aib 6 -N (a) and Z-Aib 15 -N (b), both deposited on mica from the30:70 (v/v) water/methanol solvent mixture.Excimer emission can also be detected by time-resolved fluorescence measurements:Z-Aib 15 -N showed decay time components of ca. 60ns for the N chromophore embedded asa monomer in the aggregate and 87ns for the excimer. Interestingly, the excimer time decaywas also characterized by a short rise time component (≈3ns), associated to a negative preexponentialfactor that represents a measure of the dynamics of the nuclear motions leadingto excimer formation.AFM measurements were carried out on dried peptide films supported on mica andobtained by deposition of a 10μM 30:70 (v/v) water/methanol solvent mixture. Z-Aib 6 -N(Figure 2a) showed globular structures characteristics of a specific aggregation, driven byhydrophobic interactions and promoted by the presence of the aromatic groups. On thecontrary, Z-Aib 15 -N exhibited, more extensively than Z-Aib 12 -N, fibrillar structures severalmicrons long and about 100nm thick (Figure 2b), suggesting that in this case interchainpeptide interactions are the driving force that determines the morphology of the peptideaggregates. Both FTIR absorption spectroscopy and thioflavine test measurementsindicated that the filaments are formed by microfibrils generated by entwined peptidehelical chains.References1. Toniolo, C., Crisma, M., Formaggio, F., Peggion, C. Biopolymers (Pept.Sci.) 60, 396-419 (2001).2. Karle, I.L., Balaram, P. Biochemistry 29, 6747-6756 (1990).583
Proceedings of the 31 st European Peptide SymposiumMichal Lebl, Morten Meldal, Knud J. Jensen, Thomas Hoeg-Jensen (Editors)European Peptide Society, 2010Mapping Charge Delocalization in a Peptide Chain Triggeredby Oxidation of a Terminal Ferrocene MoietyVanessa Marcuzzo, Alessandro Donoli, Roberta Cardena,Alessandro Moretto, Claudio Toniolo, and Saverio SantiDepartment of Chemical Sciences, University of Padova, Padova, 35131, ItalyIntroductionElectron transfer is one of the most relevant processes in chemistry and biology. Longrangeelectron transfer (ET) through proteins and enzymes is a fundamental step for allliving organisms. The spatial organization of the electron donor and electron acceptor inpeptides and proteins, as well as the dynamics of the ET between them, critically dependson the structure-directing and charge-transmitting properties of hydrogen bonds. ETthrough peptide helices has attracted much attention because their assemblies are universalmotifs found in biological ET systems.Results and DiscussionTwo series of peptides of different length and rigidity, based on the strongly helicogenicα-aminoisobutyric acid (Aib) residue and containing a terminal ferrocene (Fc) unit,Fc−CO-(Aib) n −OMe (A n , n = 1−5, OMe, methoxy) and Z−(Aib) n −NH−Fc (B n , n = 1−5, Z,benzyloxycarbonyl), were prepared and investigated. We utilized the oxidation-statesensitive, spectroscopic tags of peptides, the CO and NH groups, to map chargedelocalization triggered by oxidation of the terminal ferrocene, induced and monitored byVis-IR-NIR spectroelectrochemistry. The rigid and well-defined 3 10 -helical structure of(Aib) n homo-peptides [1,2] is advantageous for the study of the distance dependence ofcharge delocalization. The orientation of the carbonyl groups in the 3 10 -helix produces adipole with the positive end at the N-terminus and the negative end at the C-terminus.Thus, the A n and B n peptides series are characterized by an opposite-direction macrodipoletowards the redox Fc/Fc + probe.0,720,68E 1/2(V vs SCE)0,640,600,560,520,480,441 2 3 4 5n-AibFig. 1. Redox potentials vs saturated calomel electrode (SCE) of the Z-(Aib) n -NHFc(n=1-5) peptide series recorded at a 0.5 mm diameter gold disk electrode in CH 2 Cl 2 with0.1 M nBu 4 NPF 6 as supporting electrolyte.584
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Peptides 2010Tales of PeptidesProce
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Peptides 2010Tales of PeptidesProce
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IntroductionWe had the distinct hon
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Scientific programIn planning the 3
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31 st EUROPEAN PEPTIDE SYMPOSIUMSep
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published by John Wiley & Sons as a
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The Josef Rudinger AwardThis award
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Young Investigators' SymposiumThe y
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xxiv
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Design of Peptidyl-Inhibitors for G
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Synthetic Antifreeze Glycopeptide A
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Synthesis and Oxidative Folding of
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Convergent Syntheses of Huprp106-12
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Bactericidal Activity of Small Beta
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Bradykinin Analogues Acylated on Th
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Antimicrobial Activity of Small 3-(
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Interaction of Curcumin with A-Synu
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Fluorescent and Luminescent Fusion
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Cellular Expression of the Human An
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2D IR Spectroscopy of Oligopeptides
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large, non-redundant subset of prot
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The aberrantly glucosylated peptide
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Table 1. Proline cis/trans ratios o
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Table 1. Yields, UV-vis absorption
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Table 1. Purity of the targeted tri
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processes are blocked. Interestingl
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(tb4 n ,1 m )MTII(tb1 n ,4 m )MTIIF
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Fig. 2. a) Part of the 400 MHz HR-M
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Once printed, the amino acid partic
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A) PSA, few seconds73B) PSA, 45 min
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short β strands. In contrast, nume
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neg. control Cs9-Rhd MM-218Fig. 2.
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Table 1. The general structure of t
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% ID in the liver 1 h p.i.100908070
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Peptidyl phosphoranes were first re
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obtained from the same sardines and
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MccJ25 variants were produced by si
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Fig. 2. Proposed signaling mechanis
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Table 1. mCD4-HS12 antiviral activi
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Proceedings of the 31 st European P
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Page 579 and 580: Proceedings of the 31 st European P
Page 629: Proceedings of the 31 st European P
Page 679 and 680: Subject index(S)-2-(1-adamantyl)gly
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chip 18chiral triazine condensing r
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heat stress 348helical conformation
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O-acyl isopeptide method 112obesity
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SH2-ligands 210short collagen-relat
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Author indexAboye, Teshome Leta 142
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Chi, Hongfang 480Chiche, Laurent 6C
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Geronikaki, Athina 444Gessmann, Ren
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Kostova, Kalina 528Kotzia, Georgia
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Nagata, Koji 162Nagayev, Igor Yu. 5
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Salvarese, Nicola 518Sammet, Benedi
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Vauquelin, Georges 138Veiga, Ana Sa
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