Abstract:
:Melittin, a major component of bee venom, is a water-soluble toxic peptide of which a various biological effects have been identified to be useful in anti-tumor therapy. In addition, Melittin also has anti-parasitic, anti-bacterial, anti-viral, and anti-inflammatory activities. Therefore, it is a very attractive therapeutic candidate for human diseases. However, melittin induces extensive hemolysis, a severe side effect that dampens its future development and clinical application. Thus, studies of melittin derivatives and new drug delivery systems have been conducted to explore approaches for optimizing the efficacy of this compound, while reducing its toxicity. A number of reviews have focused on each side, respectively. In this review, we summarize the research progress on the anti-tumor effects of melittin and its derivatives, and discuss its future potential clinical applications.
journal_name
Curr Protein Pept Scijournal_title
Current protein & peptide scienceauthors
Lyu C,Fang F,Li Bdoi
10.2174/1389203719666180612084615subject
Has Abstractpub_date
2019-01-01 00:00:00pages
240-250issue
3eissn
1389-2037issn
1875-5550pii
CPPS-EPUB-91070journal_volume
20pub_type
杂志文章,评审abstract::The field of bioinformatics has become a major part of the drug discovery pipeline playing a key role in improvement and acceleration of this time and money consuming process. Here we review the application of the informational spectrum method (ISM), a virtual spectroscopy method for structure/function analysis of pro...
journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
pub_type: 杂志文章,评审
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
pub_type: 杂志文章,评审
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
pub_type: 杂志文章,评审
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journal_title:Current protein & peptide science
pub_type: 杂志文章,评审
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更新日期:2006-04-01 00:00:00
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journal_title:Current protein & peptide science
pub_type: 杂志文章,评审
doi:10.2174/138920311796957667
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
pub_type: 杂志文章,评审
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更新日期:2006-02-01 00:00:00
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journal_title:Current protein & peptide science
pub_type: 杂志文章,评审
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journal_title:Current protein & peptide science
pub_type: 杂志文章,评审
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journal_title:Current protein & peptide science
pub_type: 杂志文章,评审
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
pub_type: 杂志文章,评审
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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journal_title:Current protein & peptide science
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abstract::For several decades the specificity of proteases has been presented as an active site divided into subsites, using the nomenclature of Schechter & Berger from 1967 (S1, S2... for subsites of the active site; P1, P2... for residues of the substrate occupying the corresponding subsites). At early stages of the research ...
journal_title:Current protein & peptide science
pub_type: 杂志文章,评审
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journal_title:Current protein & peptide science
pub_type: 杂志文章,评审
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journal_title:Current protein & peptide science
pub_type: 杂志文章,评审
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journal_title:Current protein & peptide science
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更新日期:2015-01-01 00:00:00
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journal_title:Current protein & peptide science
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