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In silico screening of potential plant peptides against the non-structural proteins of dengue virus.
J Vector Borne Dis
April 2024
Saveetha School of Engineering, SIMATS, Thandalam, Chennai, India.
Background Objectives: Peptides isolated from different sources of plants have the advantages of specificity, lower toxicity, and increased therapeutic effects; hence, it is necessary to search for newer antivirals from plant sources for the treatment of dengue viral infections.
Methods: In silico screening of selected plant peptides against the non-structural protein 1, NS3 protease domain (NS2B-NS3Pro) with the cofactor and ATPase/helicase domain (NS3 helicase domain/NS3hel) of dengue virus was performed. The physicochemical characteristics of the peptides were calculated using Protparam tools, and the allergenicity and toxicity profiles were assessed using allergenFP and ToxinPred, respectively.
Restraint of VP1 Protein of Foot and Mouth Disease Virus using Specific Antiviral Peptides: an Investigation.
Arch Razi Inst
October 2023
Department of Microbiology, Faculty of Veterinary Medicine, Lorestan University, Khorramabad, Iran.
Foot and mouth diseases are among the important threats in the animal husbandry industry which lead to huge economic losses. In this regard, the current project aimed to inhibit the VP1 protein of foot and mouth disease viruses using specific peptides. For this purpose, a wide range of potential antiviral peptides were collected from the database.
View Article and Find Full Text PDFNew circulin macrocyclic polypeptides from Chassalia parvifolia.
J Nat Prod
February 2000
Laboratory of Drug Discovery Research and Development, Developmental Therapeutics Program, Division of Cancer Treatment and Diagnosis, National Cancer Institute, Frederick Cancer Research and Development Center, Frederick, MD 21702-1201, USA.
Four new macrocyclic polypeptides were isolated and identified from an extract of the tropical tree Chassalia parvifolia. Circulins C-F are 29-30 amino acid cyclic peptides in which the entire primary amino acid chain is covalently cyclized via peptide bonds. Their structures were deduced from a combination of FABMS analyses, N-terminal Edman degradation, endoproteinase digestion, and amino acid analyses.
View Article and Find Full Text PDFAn unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides.
Proc Natl Acad Sci U S A
August 1999
Department of Microbiology and Immunology, Vanderbilt University, A-5119 MCN, 1161 21st Avenue South, Nashville, TN 37232-2363, USA.
Four macrocyclic cystine-knot peptides of 29-31 residues, kalata, circulin A and B (CirA and CirB), and cyclopsychotride, have been isolated from coffee plants but have undetermined physiological functions. These macrocycles and 10 of their analogs prepared by chemical synthesis were tested against nine strains of microbes. Kalata and CirA were specific for the Gram-positive Staphylococcus aureus with a minimum inhibition concentration of approximately 0.
View Article and Find Full Text PDFInhibition of the trehalose-P synthase of mycobacteria by various antibiotics.
Arch Biochem Biophys
November 1996
Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock 72205, USA.
A number of antibiotics were tested as potential inhibitors of the purified trehalose-P synthase of Mycobacterium smegmatis. Of about 30 compounds tested, 4 (cathomycin, circulin, diumycin, and moenomycin) were active against this enzyme. Thus each of these compounds inhibited the formation of trehalose-P by the purified trehalose-P synthase when either UDP-glucose or GDP-glucose was used as the glucosyl donor.
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