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Thursday, November 24, 2016
Monday, November 21, 2016
Thursday, November 10, 2016
Call For Paper
Bentham Science Publishers would like to invite you to submit your research paper for publishing in the Journal of
Thursday, November 3, 2016
Highlighted Artcile: Exploration of the Medicinal Peptide Space
Exploration of the Medicinal Peptide Space
Author(s):
Bert Gevaert, Sofie Stalmans, Evelien Wynendaele, Lien Taevernier, Nathalie Bracke, Matthias D'Hondt and Bart De Spiegeleer Pages 324 - 335 ( 12 )
Abstract:
The chemical properties of peptide medicines, known as the ‘medicinal peptide space’ is considered a multi-dimensional subset of the global peptide space, where each dimension represents a chemical descriptor. These descriptors can be linked to biofunctional, medicinal properties to varying degrees. Knowledge of this space can increase the efficiency of the peptide-drug discovery and development process, as well as advance our understanding and classification of peptide medicines.
For 245 peptide drugs, already available on the market or in clinical development, multivariate dataexploration was performed using peptide relevant physicochemical descriptors, their specific peptidedrug target and their clinical use. Our retrospective analysis indicates that clusters in the medicinal peptide space are located in a relatively narrow range of the physicochemical space: dense and empty regions were found, which can be explored for the discovery of novel peptide drugs.
Keywords:
Chemical space, drug discovery, drug market, peptide therapeutics, PCA.
Affiliation:
Drug Quality and Registration (DruQuaR) group, Department of Pharmaceutical Analysis, Faculty of Pharmaceutical Sciences, Ghent University, Ottergemsesteenweg 460, 9000 Ghent, Belgium
Graphical Abstract:
For More Information Please Visit Our Website Protein & Peptide Letters
Thursday, October 27, 2016
Most Cited Article: Novel Antimicrobial Peptides Isolated from Skin Secretions of the Mexican Frog Hyla eximia
Novel Antimicrobial
Peptides Isolated from Skin Secretions of the Mexican Frog Hyla eximia
Author(s):
Oscar Villa-Hernandez, Lorena
Hernandez-Orihuela, Maria del Carmen Rodriguez, Fernando Zamudio-Zuniga, Ruben
Castro-Franco, Victoria Pando and Cesar V.F. Batista Pages 1371 - 1378 (
8 )
Abstract:
In this work, we describe the original
characterization of peptides and proteins present in the skin secretions of the
Mexican amphibian Hyla eximia. To this purpose, a novel water/dark extraction
method, as well as the classic electrical stimulation procedure, was applied in
order to extract the skin secretion. Two novel antimicrobial peptides He-1 and
He-2 were sequenced. In addition, a molecular mass fingerprint revealed more
than one hundred different molecules. Eight peptides in homogeneous form were
assayed against five species of bacteria. Thereafter, the peptide He-2
demonstrated high antiparasitic activity against ookinete forms of malaria
parasites at low concentration.
Keywords:
Hyla eximia, antimicrobial peptides, mass
spectrometry
Affiliation:
Unidad de Proteomica, Instituto de
Biotecnologia-UNAM, Av. Universidad, 2001, Col. Chamilpa, CP 62210, Cuernavaca,
Mor, Mexico.
Tuesday, October 25, 2016
Thursday, October 13, 2016
Protein & Peptide Letters, Volume 23 - Number 7
Contents
Protein & Peptide Letters, Volume 23 - Number 7
Meet Our Regional Editor
, 23(7): 591Solange LAVIELLE.
DOI: 10.2174/092986652307160601174524
Designing, Expression and Immunological Characterization of a Chimeric Protein of Mycoplasma pneumoniae
, 23(7): 592 - 596Chen Chen, Qi Yong, Guo Jun, Pan Ying, Li Suqin, Li Jiameng, Chen Hongxia, Li Sumei, Li Yuexi and Wang Min.
DOI: 10.2174/0929866523666160502155414
A Comprehensive Proteomic Study of the Skin Secretions of the Frog Lithobates spectabilis
, 23(7): 597 - 611Griselda Demesa-Balderrama, Erika P. Meneses, Lorena Hernández-Orihuela, Victoria Pando- Robles, Maria C. Rodriguez, Carolina Barrientos-Salcedo, Manuel B. Aguilar and Cesar V F Batista.
DOI: 10.2174/0929866523666160505120853
PDZ Binding Domains, Structural Disorder and Phosphorylation: A Menage-a-trois Tailing Dcp2 mRNA Decapping Enzymes
, 23(7): 612 - 618Dilantha Gunawardana.
DOI: 10.2174/0929866523666160506151720
The Chemopreventive Peptide Lunasin Inhibits d-Galactose- Induced Experimental Cataract in Rats
, 23(7): 619 - 625Guangzhi Dai, Ping Zhang, Pei Ye, Miaoqing Zhang, Ning Han, Haoyue Shuai and Shuhua Tan.
DOI: 10.2174/0929866523666160505121047
Design and Development of Nanoemulsion Systems Containing Interferon Gamma
, 23(7): 626 - 638Elton B. Ribeiro, Adenilda C. Honorio-França, Eduardo L. França and Maria A G Soler.
DOI: 10.2174/0929866523666160502155249
N-Terminal Cys-Rich Region of a Rice Type 1 Metallothionein Independently Forms Metal-Thiolate Cluster
, 23(7): 639 - 644Soheila Ahmadi and Azar Shahpiri.
DOI: 10.2174/0929866523666160511150730
Evaluation of Moringa oleifera Seed Lectin as a Metal Remover in Aqueous Solutions
, 23(7): 645 - 649José H.E.S. Freitas, Keissy V. de Santana, Pollyanna M. da Silva, Maiara C. de Moura, Luana C.B.B. Coelho, Aline E. do Nascimento, Patrícia M.G. Paiva andThiago H Napoleao.
DOI: 10.2174/0929866523666160517123558
Anosmin 1 Interacts with the Prokineticin Receptor 2 In Vitro Indicating a Molecular Link Between Both Proteins in the Pathogenesis of Kallmann Syndrome
, 23(7): 650 - 655Verónica Murcia-Belmonte, Verónica Astillero-López and Pedro F Esteban.
DOI: 10.2174/0929866523666160517123331
The Influence of Ionizing Radiation on Exosome Composition, Secretion and Intercellular Communication
, 23(7): 656 - 663Karol Jelonek, Piotr Widlak and Monika Pietrowska.
DOI: 10.2174/0929866523666160427105138
Monday, October 10, 2016
Recently Published Issue of the Journal Current Protein & Peptide Science,16 Issue 6
Current Protein & Peptide Science publishes review articles on specific aspects involving proteins, peptides, and interactions between the enzymes, the binding interactions of hormones and their receptors; the properties of transcription factors and other molecules that regulate gene expression; the reactions leading to the immune response; the process of signal transduction; the structure and function of proteins involved in the cytoskeleton and molecular motors; the properties of membrane channels and transporters; and the generation and storage of metabolic energy. In addition, reviews of experimental studies of protein folding and design are given special emphasis. Manuscripts submitted to Current Protein and Peptide Science should cover a field by discussing research from the leading laboratories in a field and should pose questions for future studies. Original papers, research articles and letter articles/short communications are not considered for publication in Current Protein & Peptide Science.
Following are the articles from the journal Current Protein & Peptide Science, 16 Issue 6:
Article: Commentary: Drugs From Bugs
Author(s): Laszlo Otvos
Article: Integrase Interactor 1 in Health and Disease
Author(s): Supratik Das
Article: ADP-Ribosyltransferases and Poly ADP-Ribosylation
Author(s): Chao Liu and Xiaochun Yu
Article: The Aromatic Stacking Interactions Between Proteins and their Macromolecular Ligands
Author(s): Mohammad Mizanur Rahman, Ziyad Tariq Muhseen, Muhammad Junaid and Houjin Zhang
Article: Reshaping the Protein Folding Pathway by Osmolyte via its Effects on the Folding Intermediates
Author(s): Gurumayum Suraj Sharma, Tanveer Ali Dar and Laishram Rajendrakumar Singh
Article: The Role of Structural Flexibility and Stability in the Interaction of Serine Proteases with their Inhibitors
Author(s): Laszlo Graf, Tamas Molnar, Jozsef Kardos, Zoltan Gaspari and Gergely Katona
Article: Disintegrins from Snake Venoms and their Applications in Cancer Research and Therapy
Author(s): Jessica Kele Arruda Macedo, Jay W. Fox and Mariana de Souza Castro
Article: The Sactibiotic Subclass of Bacteriocins: An Update
Author(s): Harsh Mathur, Mary C. Rea, Paul D. Cotter, Colin Hill and R. Paul Ross
Article: Targeting EZH2 for Cancer Therapy: Progress and Perspective
Author(s): Chi Han Li and Yangchao Chen
Article: Erratum: The Polymorphic Nature of Membrane-Active Peptides from Biophysical and Structural Investigations
Author(s): Burkhard Bechinger and Christopher Aisenbrey
For details, please visit: http://bit.ly/1M5zTkP
courtesy by Bentham Insight
Friday, October 7, 2016
Major Article Contributions by some of the Indian Authors in Bentham Science Publishers Journal; Protein & Peptide Letters
Article Title:Antiangiogenic Function of Antithrombin is Dependent on its Conformational Variation: Implication for Other Serpins
Author(s): Asim Azhar, Poonam Singh, Qudsia Rashid, Asma Naseem, Mohammad Sazzad Khan and Mohamad Aman Jairajpuri
Abstract: Endogenous angiogenesis inhibitor that specifically decreases tumor cell proliferation can be used to treat cancer since angiogenesis is required at every step of tumor progression and metastasis. Endothelial cells are the main target for the antiangiogenic therapy because they are non-transformed and easily accessible to angiogenic inhibitors. Antithrombin functions as a principal plasma protein inhibitor of blood coagulation proteinases and belongs to the family of serine protease inhibitors (serpins) which have common mechanism of inhibition. Antithrombin acquires a potent antiangiogenic activity upon conversion of the native molecule to cleaved or latent conformation. Cleaved and latent preparations of bovine and human plasma derived antithrombin inhibited capillary endothelial cell proliferation and the growth of human SK-NAS neuroblastoma and Lewis lung carcinoma tumors in mice as compared to the native antithrombin. The native form of antithrombin binds with high affinity to vascular heparan sulfate proteoglycans containing a specific pentasaccharide sequence and it is this cofactor interaction that activated antithrombin to maximal rate of thrombin inhibition. Upon inhibitory complex formation with target proteinases the antithrombin undergoes stressed to relaxed transformation and lose their high affinity for pentasacchride. Low affinity relaxed conformation with reduced heparin binding like cleaved and latent are antiangiogenic but native high affinity heparin binding stressed conformation is not, indicating the critical importance of heparin affinity in antithrombin antiangiogenic function. Based on evidence of interactions of the endothelial cell growth factors bFGF (Basic fibroblast growth factor) and VEGF (vascular endothelial cell growth factor) with heparin like molecule in matrix, the possibility of antiangiogenic antithrombin to interfere with endothelial cell growth and angiogenesis through heparin mediated mechanism deserves serious consideration and investigation. It is also possible that cleaved and latent conformations with reduced affinity for heparins can also induce conformational change in the antithrombin which can open an epitope on the antithrombin surface for appropriate interactions on the endothelial surface for better antiangiogenic activity. This review illustrates the potential of antithrombin and other serpin family members as endogenous antiangiogenic proteins.
For more details, visit: http://benthamscience.com/journal/abstracts.php?journalID=ppl&articleID=103876
Article Title:X-Ray Structure of PTP1B in Complex with a New PTP1B Inhibitor
Author(s): M.V.V.V. Sekhar reddy, Chakshumathi Ghadiyaram, Sunil Kumar Panigrahi, Narasimha Rao Krishnamurthy, Subramanya Hosahalli, Arun P. Chandrasekharappa, Deepankar Manna, Sangamesh E. Badiger, Pramod K. Dubey and Lakshmi Narasu Mangamoori
Abstract: Protein tyrosine phosphatase 1B (PTP1B) is a prototype non receptor cytoplasmic PTPase enzyme that has been implicated in regulation of insulin and leptin signaling pathways. Studies on PTP1B knockout mice and PTP1B antisense treated mice suggested that inhibition of PTP1B would be an effective strategy for the treatment of type II diabetes and obesity. Here we report the X-ray structure of PTP1B in complex with compound IN1834-146C (PDB ID 4I8N). The crystals belong to P3121 space group with cell dimensions (a = b = 87.89 Å, c = 103.68 Å) diffracted to 2.5 Å. The crystal structure contained one molecule of protein in the asymmetric unit and was solved by molecular replacement method. The compound engages both catalytic site and allosteric sites of PTP1B protein. We described the molecular interaction of the compound with the active site residues of PTP1B in this crystal structure report.
For more details, visit: http://benthamscience.com/journal/abstracts.php?journalID=ppl&articleID=114408
Article Title:The Solubility and Stability of Amino Acids in Biocompatible Ionic Liquids
Author(s): T. Vasantha, Awanish Kumar, Pankaj Attri, Pannuru Venkatesu and R.S. Rama Devi
Abstract: In recent years, ionic liquids (ILs) represent a new class of biocompatible co-solvents for biomolecules. In this work, we report the apparent transfer free energies ( ΔG’tr) for six amino acids (AA) from water to aqueous solutions of six ammonium based ILs (diethylammonium acetate (DEAA), diethylammonium sulfate (DEAS), triethyl ammonium acetate (TEAA), triethylammonium sulfate (TEAS), triethylammonium dihydrogen phosphate (TEAP), and trimethylammonium acetate (TMAA)) through solubility measurements, as a function of IL concentration at 298.15 K under atmospheric pressure. Salting-out effect was found for AA in aqueous IL solutions with increasing IL concentrations. In addition, we observed positive values of Δ G’tr for AA from water to ILs, indicating that the interactions between ILs and AA are unfavorable. From the obtained results, we found that the selected ammonium based ILs act as stabilizers for the structure of AA.
For more details, visit: http://benthamscience.com/journal/abstracts.php?journalID=ppl&articleID=113378
Article Title:Purification and Biophysical Characterization of an 11S Globulin from Wrightia tinctoria Exhibiting Hemagglutinating Activity
Author(s): Pramod Kumar, Dipak N. Patil, Anshul Chaudhary, Shailly Tomar, Dinesh Yernool, Nirpendra Singh, Pushpanjali Dasauni, Suman Kundu and Pravindra Kumar
Abstract: Wrightia tinctoria globulin (WTG), one of the major seed storage proteins, was isolated for the first time from seeds of the medicinal plant. WTG was extracted and purified to homogeneity in two steps using anion-exchange and size-exclusion chromatographies. On an SDS–PAGE gel under non-reducing conditions, a major band of ~56 kDa was observed; under reducing conditions, however, two major polypeptides, one with molecular weight ~32-34 kDa and the other with molecular weight ~22-26 kDa were observed. Intact mass determination by MALDI-TOF supported this observation. The N-terminal amino acid sequence of WTG matched in NCBI database with an expressed sequence tag obtained from the c-DNA of developing embryo m-RNA of Wrightia tinctoria. The EST sequence was further substantiated by partial de novo internal sequencing using MALDI-TOF/TOF. The high sequence homology with seed storage protein 11S globulin confirmed that WTG is a type of 11S globulin. Circular dichroism analysis showed that the secondary structure of WTG consists predominantly of β-sheets (44.2%) and moderate content of α-helices (10.3%). WTG showed hemagglutinating property indicating that the protein may possess lectin-like activity. WTG was crystallized at 20 °C by the vapour diffusion method using PEG 400 as precipitant. The crystals belonged to the orthorhombic space group P212121 with cell dimensions of a=109.9Å, b=113.2Å and c=202.2Å with six molecules per asymmetric unit. Diffraction data were collected to a resolution of 2.2Å under cryocondition. Preliminary structure solution of WTG indicated the possibility of a hexameric assembly in its asymmetric unit.
For more details, visit: http://benthamscience.com/journal/abstracts.php?journalID=ppl&articleID=108419
courtesy by Bentham Insight
