Protein and Peptide Letters Journal Impact Factor & Information

Publisher: Bentham Science Publishers

Journal description

Protein and Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merits rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function. Protein and Peptide Letters will focus on: Structure Studies, Recombinant Expression, Drug Design, Chemical Synthesis, Function, Pharmacology, Enzymology, Immunology, Biotechnology, Protein Engineering, Protein Folding, Sequencing, Molecular Recognition, Purification and Analysis.

Current impact factor: 1.74

Impact Factor Rankings

2015 Impact Factor Available summer 2015
2013 / 2014 Impact Factor 1.735
2012 Impact Factor 1.994
2011 Impact Factor 1.942
2010 Impact Factor 1.849
2009 Impact Factor 1.755
2008 Impact Factor 1.281
2007 Impact Factor 1.097
2006 Impact Factor 1.13
2005 Impact Factor 0.84
2004 Impact Factor 0.776
2003 Impact Factor 0.46
2002 Impact Factor 0.622
2001 Impact Factor 0.504
2000 Impact Factor 0.468
1999 Impact Factor 0.557
1998 Impact Factor 0.68

Impact factor over time

Impact factor

Additional details

5-year impact 1.71
Cited half-life 3.60
Immediacy index 0.49
Eigenfactor 0.01
Article influence 0.35
Website Protein and Peptide Letters website
Other titles Protein and peptide letters (Online)
ISSN 0929-8665
OCLC 60638050
Material type Document, Periodical, Internet resource
Document type Internet Resource, Computer File, Journal / Magazine / Newspaper

Publisher details

Bentham Science Publishers

  • Pre-print
    • Author can archive a pre-print version
  • Post-print
    • Author cannot archive a post-print version
  • Restrictions
    • 12 months embargo
  • Conditions
    • Author's pre-print on author's personal website, institutional repository and open access repository
    • Author's post-print on author's personal website, institutional repository, open access repository, PubMed Central and arXiv
    • Non-Commercial
    • Published source must be acknowledged
    • Must link to journal home page with DOI
    • Publisher's version/PDF cannot be used
  • Classification
    ​ yellow

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: Bacterial vaginosis is a common reproductive infection in which commensal vaginal lactobacilli are displaced by a mixed population of pathogenic bacteria. Bacterial vaginosis increases susceptibility to HIV, and it has been suggested that host innate immune responses to pathogenic bacteria contribute to enhanced infection, yet the cellular mechanisms mediating the increased HIV susceptibility remain uncharacterized. We evaluated the HIV-enhancing effects of bacterial vaginosis by inoculating endocervical epithelia with Atopobium vaginae, a bacterial vaginosis-associated bacteria, and assaying secreted factors for HIV-enhancing activity. When epithelia and A. vaginae were cocultured, we observed increased HIV-enhancing activity mediated by secreted low molecular weight factors. From this complex mixture we identified several upregulated host proteins, which functioned in combination to enhance HIV infection. These studies suggest that the host immune response to bacterial vaginosis-associated bacteria results in the release of HIV-enhancing factors. The combined activity of bacterial vaginosis-induced proteins likely mediates HIV enhancement.
    Protein and Peptide Letters 03/2015; 22(999). DOI:10.2174/0929866522666150309155735
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    ABSTRACT: Intrinsically disordered proteins or such domains in globular proteins are believed to be playing important roles in protein functions by virtue of their ability to adapt themselves to requirements of different binding partners and thereby accord high specificity to the interaction. Eukaryotic ribosomal stalk is made up of a supramolecular assembly of P0, P1 and P2 proteins. In Plasmodium falciparum, homo-oligomers of P2 are also seen which seem to be involved in many non-ribosomal functions of the protein in the parasite, and in all of these the protein interacts with different interactors. Here we show by extensive 15N NMR relaxation studies that the C-terminal stretch of about 45 residues of the protein always remains as a flexible disordered domain, regardless of the state of association of the protein. The relaxation behaviors and the derived rotational correlation times for this portion of the protein are essentially the same in the presence of different concentrations of urea which produce different mixtures of PfP2 oligomers in rapid exchange, whereas the rest of the protein shows substantial variations with urea concentration in the relaxation behaviors. In other words, the C-terminal domain behaves as if it were an independent intrinsically disordered peptide. This would augment the notion that the C-terminal domain of PfP2 would be acting as a scavenger for different interactors depending upon the different functions of the protein inside the parasite.
    Protein and Peptide Letters 03/2015; 22(999). DOI:10.2174/0929866522666150306161348
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    ABSTRACT: A thermostable oxidant- and SDS-stable uricase was produced from a newly isolated B. firmus DWD-33. Maximum enzyme productivity was obtained in medium containing 0.8% maltose and 1.2% soybean powder as carbon and nitrogen sources, respectively. Enzyme purification increased the specific activity to 24-fold with 27% recovery and molecular weight of 33.5 kDa. As compared with other microbial uricases, the pure enzyme showed high thermostability and other unique characters. The Vmax was 387 µM/min, the turnover number (Kcat) was 21.8×103 s-1 and the catalytic efficiency (Kcat /Km) was 2.76×108 s-1M-1. The enzyme was stable at pH 7.0-10.0 and up to 70 ºC. The optimal reaction temperature and pH of enzyme were 50 ºC and pH 8.0, respectively. Mg2+ significantly enhanced the enzymatic activity, while Hg2+, EDTA and o-phenanthroline greatly suppressed the activity. Mg2+ might be the uricase cofactor as the enzyme activity was restored after its addition to EDTA-chelated enzyme. The enzyme inhibition by the copper-chelating agent 2,9-dimethyl-1,10-phenanthroline suggests that this enzyme is a cuprouricase-type. The purified uricase retained 72 and 82% of its original activity even after incubation with 0.5% H2O2 and 0.5% SDS for 6 h, respectively. The application of enzyme in the in vitro measurement of uric acid in human sera was promising and none of uric acid analogs was a competitive substrate for enzyme, indicative of the high specificity of uricase with respect to uric acid measurement in vitro. The reaction can be applied in clinical laboratory for 10 min only due to the absorbances are lineary related to uric acid concentration up to 500 µM.
    Protein and Peptide Letters 03/2015;
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    ABSTRACT: The "A proliferation inducing ligand" protein (APRIL) is a cytokine over-expressed in many transformed and tumoral cells acting onto two distinct receptors of the Tumoral Necrosis Factor B cell maturation antigen (BCMA) and the transmembrane activator and calcium modulator and cyclophilin ligand interactor (TACI). We herein describe, through a detailed computational approach, the molecular interactions between TACI and its ligands APRIL and another structurally similar protein called B-cell activating factor (BAFF) by means of molecular dynamics. Dynamical analysis suggests R84 and D85 residues from TACI as possible mutation candidates, yielding increased affinity between TACI and APRIL. The association of computational simulations, site directed mutagenesis and peptide design could be a powerful tool, driving to better in vitro experiments. Our results contribute to the elucidation of APRIL signaling and help clarify the effects of blocking interaction between APRIL and its receptors through the use of particular peptides.
    Protein and Peptide Letters 03/2015; 22(5).
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    ABSTRACT: Liver-targeting peptide CSPⅠ-plus modified rEndostatin (rES-CSP) has a missense mutation of aspartic acid to asparagine at position 113. We compared the structure and in vitro biological activity of wild-type and mutant D113NrES-CSP. D113NrES-CSP exhibited the changes of protein secondary structure and a reduced bioactivity. With the aim to clarify the structure-function relationships featuring the fuse protein rES-CSP, the three-dimensional structural models of wild-type and mutant D113NrES-CSP were constructed by template-based modeling approach. To evaluate the effect of the single mutation on rES-CSP stability, the molecular dynamic simulation was used to reveal the structural and dynamic characteristics. Analysis on the bioactivity were conducted using a number of validated in vitro assays including proliferation, migration, cell cycle and apoptosis in HepG2 cells. Results showed that the mutant rES-CSP reduce the stability and loss of function, and the wild-type rES-CSP could both bind to the normal liver cells Chang's and the hepatoma cells HepG2 but significantly higher than non-targeted rEndostatin. rES-CSP could inhibit the proliferation of hepatoma cells in a dose-dependent manner, and increase the proportion of G1 phase, reduce the proportion of S phase, promote the apoptosis on hepatoma cells. These results make a further complement of the mechanisms by which the fuse protein rES-CSP would provide a feasible and convenient approach to produce liver-targeting drugs for treatment of the liver disease.
    Protein and Peptide Letters 03/2015; 22(5). DOI:10.2174/0929866522666150302125218
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    ABSTRACT: This report describes the purification of an aspartic protease (salpichroin) from ripe fruits of Salpichroa origanifolia (Solanaceae) starting with precipitation using organic solvents and anion-exchange chromatography with 32.1% recovery and 13.4-fold purification. SDS-PAGE and zymograms of this enzyme showed a single band corresponding to an apparent molecular mass of approximately 32 kDa. The biochemical and kinetic characterization of the pure enzyme showed an acidic behavior with an optimal pH value around 3.0-4.5 with hemoglobin and 5.5-6.0 with casein. Salpichroin activity was inhibited by pepstatin but not by phenylmethylsulfonyl fluoride, E-64, EDTA or 1,10-phenanthroline, thus suggesting an aspartic protease behavior. Salpichroin hydrolyzed natural substrates, such as casein and hemoglobin, with high specific activity. Kinetic studies conducted with the synthetic peptide H-Pro-Thr-Glu-Phe-p-(NO2)-Phe-Arg-Leu-OH showed lower affinity (Km 494 µM) than other representative aspartic proteases. By investigating the cleavage of oxidized insulin β-chain to establish the hydrolytic specificity of salpichroin, we found six cleavage sites on the substrate of peptide bonds similar to those of chymosin. MALDI-TOF(/TOF)-MS of the tryptic in-gel digest of salpichroin showed that the isolated protease shared homologous sequences with other plant proteases of the A1 aspartic protease family. This is the first report concerning the isolation and biochemical characterization of an aspartic protease isolated from Salpichroa origanifolia fruits.
    Protein and Peptide Letters 03/2015; 22(4). DOI:10.2174/0929866522666150302111059
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    ABSTRACT: Antithrombin inhibits blood coagulation through the interaction with serine proteases in both intrinsic and extrinsic pathways. In addition, antithrombin also shows anti-inflammatory properties, which are independent of its effects on coagulation. This work shows for the first time the cloning and sequencing of antithrombin from a snake species. This predicted protein is composed by 430 amino acids and presents about 64.5% sequence identity to human antithrombin. Biacore experiments revealed that the binding affinity of Bothrops jararaca snake antithrombin to heparin was ~30 times higher than that of human antithrombin. Furthermore, Bothrops jararaca antithrombin is more effective in preventing acute inflammation induced by carrageenan when compared to human antithrombin. Hence, the results showed herein suggest that Bothrops jararaca antithrombin can play a key role in the control of acute inflammation and that this molecule might be used as a pharmacological tool and as a prototype for drug development.
    Protein and Peptide Letters 02/2015; 22(5). DOI:10.2174/0929866522666150216150704
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    ABSTRACT: PP2A is a serine/threonine phosphatase critical to a number of physiological and developmental processes. In this manuscript, we show that a peptide, specifically blocking the caspase-9/PP2A interaction, DPT-C9h, induces apoptosis in primary tumour B cells isolated from peripheral blood mononuclear cells or bone marrow of chronic lymphocytic leukemia (CLL) patients, but not on B cells obtained from healthy donors (HD). Moreover, in both CLL patients and HD, DPT-C9h does not induce apoptosis on T- and NK-cells and monocytes. Our results strongly suggest that DPT-C9h peptide has tumour specificity and that caspase-9/PP2Ac interaction constitutes a novel therapeutic approach for the treatment in CLL patients.
    Protein and Peptide Letters 02/2015; 22(6). DOI:10.2174/0929866522666150216115352
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    ABSTRACT: Most published articles always applied a certain model or arithmetic to only a certain dataset. Considering the avalanche of biological data generated in the post-genomic age, this type of research shows many shortcomings and ineffective characters, because it is always have difficulties to apply the same model to different dataset. So we proposed a multifunctional ensemble classifier which combines several individual classifiers. Each of them was trained in different parameter system which was extracted from a training system. The final outcomes were combined through a weighted voting system. This classifier was conducted on several strictly constructed biological dataset. Based on the testing result from three different types of biological dataset, this new predictor can deal with more sweeping range of biological data, and receives more efficient and robust results in comparison with other published methods tentatively.
    Protein and Peptide Letters 02/2015; 22(999). DOI:10.2174/0929866522666150209151344
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    ABSTRACT: The central nervous system (CNS) of Aplysia is a fascinating source to identify and characterize neuropeptides and neurotransmitters because of offering many useful divergent and convergent neuronal aggregates. Here, two neuropeptides were isolated from the extract of CNS of the northwest pacific sea hare, Aplysia kurodai, using HPLC system for fractionation and the anterior byssus retractor muscle (ABRM) of the Mytilis edulis as the bioassay system. Purified peptides, myomodulin A (MMA) and E (MME), were determined by amino acid sequencing and molecular mass analysis. MMA showed a potentiating effect at 100 nM or lower, on the contrary, an inhibitory effect at higher doses from 100 nM on phasic contraction elicited by repetitive electrical stimulation on the ABRM of Mytilus. However, MME only inhibited phasic contraction with all examined concentrations. MME revealed 100 times more potent activity than that of MMA on the relaxing catch-tension of ABRM stimulated by acetylcholine. Both MMA and MME potently stimulated a response on the crop and penial retractor muscle of the African giant snail, Achatina fulica, compared with other known mollusks neuropeptides. These results suggest that MMA and MME may be broadly distributed in CNS of Aplysia to function a neuromodulatory role controlled via excitatory and inhibitory neurons, and may be involved in the digestive and reproductive activity in other mollusk.
    Protein and Peptide Letters 02/2015; 22(4). DOI:10.2174/0929866522666150209125800
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    ABSTRACT: α-Synuclein form amyloid deposits in the dopaminergic neurons; a process that is believed to contribute to the Parkinson's disease. An emerging theme in amyloid research is the hypothesis that the toxic species produced during amyloid formation share common physic-chemical features and exert their effects by common modes. This prompted the idea that molecules able to inhibit a protein aggregation process may cross-react with other amyloidogenic proteins, interfering in their fibrils formation. We investigate the ability of the heptapeptide H-Arg-Lys-Val-MePhe-Tyr-Thr-Trp-OH, an inhibitor of Aβ-peptide aggregation, to cross-react with α-synuclein interfering with its fibril formation. The influence of the MePhe topography on the interaction with α-synuclein has also been evaluated, replacing the MePhe residue with either Phe or the conformationally restricted Tic residues. Peptides interact with good affinity with the α-synuclein monomer, promoting its aggregation process. This work provides the basis for the development of new drugs based on peptidomimetics able to modify the oligomers - mature fibrils equilibrium towards this last species.
    Protein and Peptide Letters 02/2015; 22(4). DOI:10.2174/0929866522666150209142649
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    ABSTRACT: Recent studies have shown that angiotensin-converting enzyme 2 (ACE2)/Ang-(1-7)/Mas axis activation is able to improve metabolic profile, enhances glucose tolerance and insulin sensitivity, improves metabolic parameters and counteracts deleterious effects of Ang II. But the effects of endogenous ACE 2 activation in the metabolic profile of mice are unknown. Methods: Male mice aged 12 weeks were treated with the ACE 2 activator, (diminazene aceturate, DIZE, 1 mg/kg/day, gavage) or saline (control) for 30 days. Glucose tolerance and insulin sensitivity tests, and blood analysis were performed. Epididymal ACE2, ACE, angiotensinogen, acetyl-CoA carboxylase (ACC) and fatty acid synthase (FAS) were measured by quantitative RT-PCR. Results: ACE 2 activation treatment lowered body weight (DIZE vs control) (28.69 vs 30.28g, P < 0.001), serum cholesterol (140,0 vs 177.5; P < .05), and serum triglyceride (75,00 vs 165,0; P < .05), as well as the epididymal (0.008 vs 0.016; P < .05); and retroperitoneal (0.0024 vs. 0.0068; P < .01) adipose tissue weights. These effects were associated with significant increase in epididymal ACE 2 and a decrease in ACE and angiotensinogen (AGT) expression. Additionally, DIZE decreased adipogenesis-related genes as ACC (P<.01) and FAS (P<0.001) mRNA expression. Conclusion: In summary, these results indicate that activation of ACE2 by oral DIZE treatment improves metabolic profile and reduces fat deposition in mice, decreasing lipogenesis markers thereby opening a new perspective for metabolic disorders pharmacotherapy.
    Protein and Peptide Letters 02/2015; 22(4). DOI:10.2174/0929866522666150209125401
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    ABSTRACT: Several studies have reported differences in physiological and pathological phenotypes between different strains of experimental mice, such as environment-based behavior, skin damage, damage in response to toxins and nervous system injury. However, the mechanisms underlying these differences have not yet been fully elucidated. We have been studying the function of kallikrein-related peptidases (KLKs), serine proteases known to serve a variety of functions. In this study, we focused on differences in KLKs between C57BL/6 mice and 129 mice. Among 13 KLKs genes examined, 12 KLKs showed differences in the mRNA coding region sequence and 7 KLKs showed different deduced amino acid sequences of their proteins when comparing C57BL/6 and 129 mice. KLK6 protein from 129 mice had six amino acid differences compared with that from C57BL/6 mice. KLK6 protein from 129 mice showed reduced SDS-PAGE mobility compared with that from C57BL/6 mice. Moreover, recombinant KLK6 protein from 129 mice had a higher optimum pH and >15 times higher hydrolytic enzymatic activity for several substrates than that from C57BL/6 mice. These results suggest that KLKs may contribute to the genetic basis of the differences between mouse strains.
    Protein and Peptide Letters 02/2015; 22(3). DOI:10.2174/0929866522666150209113108
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    ABSTRACT: Ofloxacin (OFX) and moxifloxacin (MOX) are the most promising second line drugs for tuberculosis treatment. Although the primary mechanism of action of OFX and MOX are gyrase inhibition, other possible mechanisms cannot be ruled out. Being the functional moiety of cell, the proteins act as primary targets for developing drugs, diagnostics and therapeutics. In this study we have investigated the proteomic changes of Mycobacterium tuberculosis isolates induced by OFX and MOX by applying comparative proteomic approaches based on two-dinensional gel electrophoresis (2DE) along with matrix assisted laser desorption ionisation time of flight mass spectrometry (MALDI TOF/TOF-MS) and bioinformatic tools. The findings are likely to provide new understanding of OFX and MOX mechanisms that might be helpful in exploring new diagnostics and drug targets. Our study explored eleven proteins (Rv2889c, Rv2623, Rv0952, Rv1827, Rv1932, Rv0054, Rv1080c, Rv3418c, Rv3914, Rv1636 and Rv0009) that were overexpressed in the presence of drugs. Among them, Rv2623, Rv1827 and Rv1636 were identified as proteins with unknown function. InterProScan and molecular docking revealed that the conserved domain of hypothetical proteins interact with OFX and MOX which indicate a probable inhibition/modulation of the functioning of these proteins by both drugs, which might be overexpressed to overcome this effect.
    Protein and Peptide Letters 02/2015; 22(4). DOI:10.2174/0929866522666150209113708
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    ABSTRACT: Mono or di-substituted prolines, namely proline chimeras of natural or synthetic origin, carry the side chain of other specific amino acids on the pyrrolidine ring. Thus, proline chimeras are useful tools for a wide range of chemical and biological applications as chiral synthons or building blocks for peptidomimetic design. We focused our attention on domoic acid and kainic acid and we report here a concise and up to date review on their stereo selective and asymmetric syntheses.
    Protein and Peptide Letters 02/2015;
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    ABSTRACT: Differently than the 4-methylbenzhydrylamine-resin (MBHAR) which contains a methyl group coupled to the phenylmethylamine-functionalized copoly(styrene-divinilbenzene) structure, alternative resins containing the electron-donating 4-tert-butyl- (BUBHAR) or the electron-withdrawing 2-chloro- (ClBHAR) and 2,4-chloro- (diClBHAR) groups were developed as potential supports for α-carboxamide peptide synthesis. Initially, a time-course investigation of HF cleavage reaction (0 ºC) with these resins bearing the vasoconstrictor angiotensin II (AngII, DRVYIHPF) or its Gly8-AngII analogue revealed that the peptide-BUBHAR linkage is much more labile than those with ClBHAR or diClBHAR. HF cleavage times of near 2 h or longer than 24 h were needed for complete removal of peptide chains from these two classes of resin, respectively. By including MBHAR and benzhydrylamine-resins (BHAR) in this comparative study, the decreasing order of acid stability of the peptidyl-resin linkage was diClBHAR ClBHAR BHAR MBHAR ~ BUBHAR. The same stability order was observed for the HCl/propionic acid hydrolysis reaction (130ºC) with the Phe- or Gly-resins. These findings thus suggest that ClBHAR and diClBHAR are not appropriate for use in peptide synthesis. Nevertheless, these supports could still be tested as stationary phases for affinity chromatography. When placed into more apolar solvents, the beads of all of these resins exhibited a greater swelling (as measured by a microscope) or higher mobility of the polymer matrix (as measured with EPR experiments using spin-labeled beads). Moreover, under the latter approach, BUBHAR displayed a comparatively higher solvation degree than did MBHAR (in DCM, DMF and NMP), with slightly higher peptide synthesis yields as well.
    Protein and Peptide Letters 02/2015; 22(5). DOI:10.2174/0929866522666150206170329
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    ABSTRACT: Antimicrobial peptides (AMPs) represent a large and ubiquitous group of peptides. The current crisis in antibiotic therapy has led to an intensified search for new antimicrobial agents. In this regard, scorpion venom constitutes a rich source of biologically active peptides including AMPs. In the present study, the purification of a novel peptide with antimicrobial activity against the Gram-negative bacteria Klebsiella pneumoniae is described. This antimicrobial peptide, named Cm38, was purified from Centruroides margaritatus scorpion venom using a two-step chromatographic strategy using C8 and C18 columns. This toxin inhibits the proliferation of the Gram-negative bacteria Klebsiella pneumoniae with a Minimal Inhibitory Concentration (MIC) of 64 μM. An analysis of the N-terminal sequence of Cm38 revealed a close structural relationship to Cn11, a Na+-channel modulator toxin previously isolated from Centruroides noxius scorpion venom. Therefore, to test Cm38 for effects on ion channels, we measured its effects on action potential firing in cultured dorsal root ganglion neurons. Cm38 depolarized and increased action potential firing in a subset of neurons tested. The present work reports a new peptide related to Cn11 with antimicrobial properties that is also active in neurons.
    Protein and Peptide Letters 02/2015; 22(2):164-72. DOI:10.2174/092986652202150128143048
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    ABSTRACT: It has long been known that amyloid ß protein (Aß) plays a key role in Alzheimer's Disease (AD) and in Down Syndrome cognitive decline. Recent findings have shown that soluble forms of Aß (mostly Aß oligomers; Aßo), rather than insoluble forms (fibrils and plaques), are associated with memory impairments in early stages of AD. Since synaptic plasticity and oscillatory network activity are required for memory formation, consolidation and retrieval, numerous attempts have been made to establish whether or not Aßo-induced alterations in synaptic plasticity and oscillatory network activity cause memory impairment. Despite a wealth of uncorrelated experimental evidence, such a relationship remains elusive. Furthermore, the specific cellular mechanisms underlying these disruptions remain to be determined. This review will discuss recent findings about the cellular and network mechanisms involved in Aßo-induced alterations of network oscillations and synaptic plasticity that could be responsible for the learning and memory impairments observed in early AD. Additionally, we will review some of the signal transduction pathways involved in these deleterious effects, which are revealing promising therapeutic targets to ease Aßo-induced brain dysfunction and treat AD.
    Protein and Peptide Letters 02/2015; 22(4). DOI:10.2174/0929866522666150202112154
  • Article: Editorial:.
    Protein and Peptide Letters 02/2015; 22(2):103.