ParaPep: a web resource for experimentally validated antiparasitic peptide sequences and their structures

Mehta, Divya; Anand, Paras; Kumar, Vineet; Joshi, Anshika; Mathur, Deepika; Singh, Sandeep; Tuknait, Abhishek; Chaudhary, Kumardeep; Gautam, Shailendra K.; Gautam, Ankur; Varshney, Grish C.; Raghava, Gajendra P. S.

doi:10.1093/database/bau051

Cited by 65 publications

(43 citation statements)

References 26 publications

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“…. Peptides containing various therapeutic properties have been discovered67891011121314151617181920 and their number is increasing with time21. Owing to their applicability, a number of bioinformatics platforms have been developed to assist peptide therapeutics22232425262728.…”

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confidence: 99%

PEPlife: A Repository of the Half-life of Peptides

Mathur

Prakash

Anand

et al. 2016

Sci Rep

110

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Short half-life is one of the key challenges in the field of therapeutic peptides. Various studies have reported enhancement in the stability of peptides using methods like chemical modifications, D-amino acid substitution, cyclization, replacement of labile aminos acids, etc. In order to study this scattered data, there is a pressing need for a repository dedicated to the half-life of peptides. To fill this lacuna, we have developed PEPlife (http://crdd.osdd.net/raghava/peplife), a manually curated resource of experimentally determined half-life of peptides. PEPlife contains 2229 entries covering 1193 unique peptides. Each entry provides detailed information of the peptide, like its name, sequence, half-life, modifications, the experimental assay for determining half-life, biological nature and activity of the peptide. We also maintain SMILES and structures of peptides. We have incorporated web-based modules to offer user-friendly data searching and browsing in the database. PEPlife integrates numerous tools to perform various types of analysis such as BLAST, Smith-Waterman algorithm, GGSEARCH, Jalview and MUSTANG. PEPlife would augment the understanding of different factors that affect the half-life of peptides like modifications, sequence, length, route of delivery of the peptide, etc. We anticipate that PEPlife will be useful for the researchers working in the area of peptide-based therapeutics.

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mentioning

confidence: 99%

PEPlife: A Repository of the Half-life of Peptides

Mathur

Prakash

Anand

et al. 2016

Sci Rep

110

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“…Their antimicrobial activity is mainly ascribed to their ability to disrupt membrane integrity. Some AMPs have also internal targets . AMPs are oligopeptides with a varying number (from five to over a hundred) of amino acids.…”

Section: Discussionmentioning

confidence: 99%

Isolation and characterization of an anti‐leishmanial disintegrin from Cerastes cerastes venom

Allane

Oussedik-Oumehdi

Harrat

et al. 2017

J Biochem & Molecular Tox

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Investigating new antimicrobial and antiparasitic components from Viperidae venoms represents an alternative therapeutic strategy. In this study, we report the characterization of a disintegrin isolated from Cerastes cerastes venom, exhibiting antiparasitic activity on Leishmania infantum promastigotes. Indeed, isolated disintegrin, referred to Disintegrin_Cc, induced 84.75% of parasiticidal activity and deep morphological alterations on the parasites. SDS-PAGE analysis indicated that this disintegrin was homogenous. This dimeric disintegrin of 14,193.97 Da contains an RGD domain and four intramolecular disulfide bridges. It presents a high percentage of identity with other related snake disintegrins. Predicted 3D structure indicated that this peptide shares partial homology with well-known active antimicrobial peptides. Disintegrin_Cc inhibited 80% of arachidonic acid-induced platelet aggregation. The obtained results suggest that the isolated molecule plays a dual role as a disintegrin and as an anti-leishmanial compound. This component could be useful as a drug in the treatment of leishmaniasis.

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“…Peptides have been reported as key players in diverse fields like immunotherapeutic [1][2][3][4][5][6][7], disease biomarkers [8][9][10], antibacterial [11][12][13][14][15], antiviral [16][17][18][19][20], anticancer [21][22][23][24][25], antiparasitic [26][27][28][29][30], antihypertensive [31][32][33] drugs owing to their properties such as cell-penetration [34], stability [35][36][37] and low toxicity [38,39]. Besides these areas, peptides are rapidly gaining the attention of researchers in the field of nanobiotechnology [40][41][42][43] by virtue of their property to self-assembly into well-defined nanostructures.…”

Section: Introductionmentioning

confidence: 99%

SAPdb: A database of nanostructures formed by self-assembly of short peptides

Mathur

Kaur

Raghava

2019

Preprint

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Nanostructures generated by self-assembly of peptides yield nanomaterial that have many therapeutic applications including drug delivery and biomedical engineering due to their low cytotoxicity and higher uptake by targeted cells owing to their high affinity and specificity towards cell surface receptors. Despite promising implications of this rapidly expanding field, there is no dedicated resource to study peptide nanostructures. This study endeavors to create a dedicated repository of short peptides, which may prove to be the best models to study ordered nanostructures formed by peptide self-assembly. SAPdb has a repertoire of 637 entries of experimentally validated nanostructures formed by self-assembling of dipeptides and tripeptides.Each entry encompasses information about the terminal and non-terminal modifications in the peptide sequence, the technique used to study self-assembly, the stability of the nanostructure, type of nanostructure formed and conditions like pH, temperature and solvent required for the self-assembly of the peptide. User-friendly browsing, searching and analysis modules are integrated for easy retrieval and comparison of data and examination of properties. We anticipate SAPdb to be a valuable repository for researchers engaged in the burgeoning arena of nanobiotechnology.

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ParaPep: a web resource for experimentally validated antiparasitic peptide sequences and their structures

Cited by 65 publications

References 26 publications

PEPlife: A Repository of the Half-life of Peptides

PEPlife: A Repository of the Half-life of Peptides

Isolation and characterization of an anti‐leishmanial disintegrin from Cerastes cerastes venom

SAPdb: A database of nanostructures formed by self-assembly of short peptides

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