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Table 1. Pharmacological properties of the new AVP analogues (IU/mg or pA 2 )AnalogueUterotonic invitrono Mg 2+ActivityPressorAntidiuretic60 min. (200 min.)AVP a 17 412 465[Mpa 1 ]AVP a 27-63 346-370 1300-1745[D-Arg 8 ]VP a 0.4 4.1 114-257[Mpa 1 ,D-Arg 8 ]VP a 1.5-5.1 ~0.39 800-50 000 b[Val 4 ]AVP a - 32 738 c[Adg 2 ]AVP I 1.90 0
Proceedings of the 31 st European Peptide SymposiumMichal Lebl, Morten Meldal, Knud J. Jensen, Thomas Hoeg-Jensen (Editors)European Peptide Society, 2010C H 3Interaction of Curcumin with α-Synuclein and Its Relationshipto Curcumin’s Ability to Inhibit Fibril DepositAnna Marchiani 1 , Stefano Mammi 1 , Isabella Tessari 2 , Luigi Bubacco 2 ,Sandra Monti 3 , Francesco Manoli 3 , and Paolo Ruzza 11 Institute of Biomolecular Chemistry of CNR, Padova Unit, and Department of ChemicalSciences, University of Padova, Padova, 35131, Italy; 2 Department of Biology,University of Padova, Padova, 35131, Italy; 3 Institute of Organic Synthesisand Photoreactivity (ISOF) of CNR, Bologna, 40129, ItalyIntroductionLewy bodies and Lewy neurites in the brain constitute the main histopathological featuresof Parkinson’s disease (PD), and are composed of amyloid-like fibrils that contain mainly asmall protein named α-synuclein (AS). The aggregation of AS in the brain has beenimplicated as a critical step in the development of the disease. Therefore, the current searchfor disease-modifying drugs is focused on molecules that can act on the process of ASdeposition in the brain.Curcumin, a constituent of the Indian spice Turmeric, has been demonstrated to bindOHOOHOH 3 CFig. 1. Chemical structure of theketo-enol form of curcumin.OOHAβ amyloid and prevent oligomerization of Aβmonomers onto amyloid β-sheets in Alzheimer’sdisease (AD) [1].Reasoning that oligomerization kinetics andmechanism of amyloid formation seems to be similar inPD and AD, we evaluated the use of curcumin toprevent AS aggregation and/or to reduce AS fibrilformation.Curcumin has low solubility in aqueous solutionand its soluble portion undergoes rapid degradation atphysiological pH. Recently, the use of serum albuminas carrier for curcumin has been reported, implying thatthis protein has the ability to stabilize curcumin [2].Results and DiscussionThe kinetics of curcumin degradation were investigated analyzing the change in theabsorption around 420 nm in different environments. Results confirm the degradation ofcurcumin in buffer solution, while the decay in the presence of either BSA or AS isnegligible. These results clearly highlight the ability of AS to interact with and stabilizecurcumin.The curcumin binding to AS was evaluated by the quenching of tyrosine fluorescence.AS (1 µM in 20 mM phosphate buffer, pH 6.8) was titrated with aliquots of curcumin(0.8 mM in ethanol). The binding constant (K a = 6.34×10 4 M -1 ) and the number of bindingsites (n = 0.95) for curcumin on AS were determined from the following equation [3]F − Flog 0 = log Ka + nlog[curc]Fwhere F 0 and F represent the initial and observed fluorescence values, respectively.A K a value of 1.30±0.32×10 5 M -1 was calculated using a nonlinear least-squarescomputer fit to the equation based on 1:1 binding stoichiometry [4],( FS−100)2F = [( KaP+ KaL+ 1) − ( KaP+ KaL+ 1) − 4KaPL]+ 1002KaPwhere F and F s represent the observed and saturation fluorescence values,respectively, and P and L the total AS and curcumin concentrations, respectively.AS emission lifetimes were measured by TCSPC (Time Correlated Single PhotonCounting) in a 15 µM solution in phosphate buffer at pH 6.8 in the absence and presence ofcurcumin at various concentrations. The protein decay was biexponential with τ 1 = 0.85 nsand τ 2 = 2.2 ns. The biexponential decay was not affected by the addition of 2 eq. (τ 1 = 0.85ns, τ 2 = 2.1 ns) or 5 eq. (τ 1 = 0.78 ns, τ 2 = 2.05 ns) of curcumin.434
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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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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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