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
Year

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 homepage with DOI
    • Publisher's version/PDF cannot be used
  • Classification
    ​ yellow

Publications in this journal

  • Protein and Peptide Letters 09/2015; 22(9). DOI:10.2174/092986652209150805120852
  • Protein and Peptide Letters 08/2015; 22(10):861-861. DOI:10.2174/092986652210150821170543
  • [Show abstract] [Hide abstract]
    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 stereoselective and asymmetric syntheses.
    Protein and Peptide Letters 08/2015; 22(8). DOI:10.2174/0929866522666150206170716
  • [Show abstract] [Hide abstract]
    ABSTRACT: Former data of our workgroup indicated that the accumulation of oxidized amino acids (meta- and ortho-tyrosine) due to oxidative stress may play an important role in the impaired insulininduced vasoactive properties of different arterial segments. There are evidences, that incorporation of these amino acids into cellular proteins leads to certain hormonal resistances, which might be restored by supplementation with the physiologic isoform, para-tyrosine. Rats in the control group were kept on a regular diet, rats in the cholesterol-fed group received high-fat diet, while the third group of rats received high-fat diet with para-tyrosine supplementation for 16 weeks. Plasma cholesterol level was significantly higher in the cholesterol-fed group, while the level of cholesterol in the cholesterol+para-tyrosine group did not differ significantly from that of the controls. Plasma level of insulin after glucose stimulation was decreased in the cholesterol-fed group, while that in the para-tyrosine supplemented group did not differ significantly from the controls. Vascular para-, meta- and ortho-tyrosine content was measured with HPLC. Elevated vascular meta-tyrosine/para-tyrosine ratio of cholesterol fed rats could be avoided by para-tyrosine supplementation. Vascular response of the thoracic aorta to insulin and liraglutide was assessed by a DMT multi-myograph. Cholesterol feeding resulted in vascular insulin-and liraglutide resistance, which was restored by para-tyrosine supplementation. Incorporation of the oxidative stress induced pathological tyrosine isoforms leads to vascular-hormone-resistances. We show that the physiological amino acid para-tyrosine is capable of restoring hypercholesterolemia-induced increased meta-tyrosine content of the vascular wall, thus attenuating functional vascular damage.
    Protein and Peptide Letters 08/2015; 22(8). DOI:10.2174/0929866522666150610093039
  • Protein and Peptide Letters 08/2015; 22(8). DOI:10.2174/092986652208150713103922
  • [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 08/2015; 22(8).
  • Protein and Peptide Letters 06/2015; 22(7). DOI:10.2174/092986652207150617172554
  • [Show abstract] [Hide abstract]
    ABSTRACT: In our present investigation, the unfolding and refolding of β-glucosidase (BGL-Al) from sweet almond was investigated using tryptophan (Trp) fluorescence spectroscopy. When the unfolding of BGL-Al was induced by guanidium chloride (GdnHCl) and monitored using biological activity as well as Trp fluorescence spectroscopic measurement, we observed that the denaturation of BGL-Al could be easily induced by low concentration of GdnHCl and the enzyme was completely inactivated at 1.0 M GdnHCl. Higher unfolding in the presence of reducing agent revealed that the protein perhaps containing multiple di-sulfide bonds indicating a reason of high stability against unfolding by GdnHCl. Refolding results suggested that the protein refolded with high yield from 1 M GdnHCl denatured state, however, refolded with negligible yield from completely unfolded state. The kinetic studies of BGL-Al refolding unravel a two phase refolding process with calculated t1/2 (refolding half time) of 1.8 and 33 min, respectively. When 8-Anilino-1-naphthalenesulfonic acid (ANS) was used as extrinsic fluorophore, we found that the surface hydrophobicity of BGL-Al was continuously decreased during GdnHCl-mediated unfolding. The surface hydrophobicity of the protein was calculated to be as high as 128.32. Acrylamide quenching study demonstrated that Trp residues of BGL-Al are mostly and hence they must be located either on the surface or in the crevices accessible by quenchers.
    Protein and Peptide Letters 06/2015; 22(7). DOI:10.2174/0929866522666150511151818
  • Protein and Peptide Letters 05/2015; 22(6). DOI:10.2174/092986652206150525123559
  • Protein and Peptide Letters 05/2015; 22(5). DOI:10.2174/092986652205150509211119
  • Protein and Peptide Letters 04/2015; 22(4). DOI:10.2174/092986652204150409104657
  • [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
  • [Show abstract] [Hide abstract]
    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
  • [Show abstract] [Hide abstract]
    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;
  • [Show abstract] [Hide abstract]
    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). DOI:10.2174/0929866522666150302124953
  • [Show abstract] [Hide abstract]
    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
  • [Show abstract] [Hide abstract]
    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
  • Protein and Peptide Letters 02/2015; 22(3). DOI:10.2174/092986652203150223145043