Advances in the Study of Structural Modification and Biological Activities of Anoplin

Wu, Ye; Huang, Rui; Jin, Jinmei; Zhang, Lijun; Hong, Zhang; Chen, Hongzhuan; Chen, Lili; Luan, Xin

doi:10.3389/fchem.2020.00519

Cited by 20 publications

(14 citation statements)

References 80 publications

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“…The membrane interaction of anoplin was verified using lipid monolayers imaged using atomic force microscopy and X-ray spectromicroscopy [ 59 ]. Owing to its simple structure and a broad spectrum of biological and pharmacological activity, anoplin has attracted research interest in terms of chemical manipulation and structural modification, to modulate its activity and bioavailability, as recently reviewed [ 60 ]. Particularly, the C-N terminal dimerization of anoplin not only showed superior stability and performance when compared with the parent peptide but also and importantly, enhanced inner membrane permeability and DNA binding ability [ 61 ].…”

Section: Cell-penetrating Peptides From Animal Venoms and Toxinsmentioning

confidence: 99%

“…Particularly, the C-N terminal dimerization of anoplin not only showed superior stability and performance when compared with the parent peptide but also and importantly, enhanced inner membrane permeability and DNA binding ability [ 61 ]. These improved properties and performance of structurally modified anoplin have inspired the design of self-assembling anoplin derivatives for selective and sustained antibiosis [ 62 ], as well as conceived in situ tumor microenvironment-induced self-assembly of polymer–anoplin conjugates to attack solid tumors and analogous with other peptide-functionalized nanoconjugates [ 60 , 63 ].…”

Section: Cell-penetrating Peptides From Animal Venoms and Toxinsmentioning

confidence: 99%

“…The first CPP sequences were characterized and derived from the transactivator of transcription from HIV-1 (Tat protein), the antennapedia (Antp) homeodomain from Drosophila and VP22 from Herpes simplex virus type I, almost three decades ago. For instance, CPPs such as Tat [48][49][50][51][52][53][54][55][56][57][58][59][60] (residues 48-60, GRKKRRQRRRPPQ) and penetratin (Antp [43][44][45][46][47][48][49][50][51][52][53][54][55][56][57][58] , RQIKIWFQNRRMKWKK), which are short-derived fragments from TAT protein and Drosophila Antp, respectively, were able to translocate across the plasma membrane of eukaryotic cells and set the stage for the development of a new class of non-viral vectors for the intracellular delivery of compounds and, therefore, converted into archetypal CPPs [19,20]. Since these initial discoveries, the field of CPPs has expanded into a prolific field of research.…”

Section: Introductionmentioning

confidence: 99%

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Cell-Penetrating Peptides Derived from Animal Venoms and Toxins

Rádis‐Baptista

2021

Toxins

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Cell-penetrating peptides (CPPs) comprise a class of short polypeptides that possess the ability to selectively interact with the cytoplasmic membrane of certain cell types, translocate across plasma membranes and accumulate in the cell cytoplasm, organelles (e.g., the nucleus and mitochondria) and other subcellular compartments. CPPs are either of natural origin or de novo designed and synthesized from segments and patches of larger proteins or designed by algorithms. With such intrinsic properties, along with membrane permeation, translocation and cellular uptake properties, CPPs can intracellularly convey diverse substances and nanomaterials, such as hydrophilic organic compounds and drugs, macromolecules (nucleic acids and proteins), nanoparticles (nanocrystals and polyplexes), metals and radionuclides, which can be covalently attached via CPP N- and C-terminals or through preparation of CPP complexes. A cumulative number of studies on animal toxins, primarily isolated from the venom of arthropods and snakes, have revealed the cell-penetrating activities of venom peptides and toxins, which can be harnessed for application in biomedicine and pharmaceutical biotechnology. In this review, I aimed to collate examples of peptides from animal venoms and toxic secretions that possess the ability to penetrate diverse types of cells. These venom CPPs have been chemically or structurally modified to enhance cell selectivity, bioavailability and a range of target applications. Herein, examples are listed and discussed, including cysteine-stabilized and linear, α-helical peptides, with cationic and amphipathic character, from the venom of insects (e.g., melittin, anoplin, mastoparans), arachnids (latarcin, lycosin, chlorotoxin, maurocalcine/imperatoxin homologs and wasabi receptor toxin), fish (pardaxins), amphibian (bombesin) and snakes (crotamine and cathelicidins).

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Section: Cell-penetrating Peptides From Animal Venoms and Toxinsmentioning

confidence: 99%

Section: Cell-penetrating Peptides From Animal Venoms and Toxinsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Cell-Penetrating Peptides Derived from Animal Venoms and Toxins

Rádis‐Baptista

2021

Toxins

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“…To overcome the drawbacks of AMPs in relation to their efficacy, in vivo stability, toxicity, and expensive large-scale production, new strategies have been focusing on designing synthetic mimics and developing new delivery systems [15,[27][28][29][30]. Moreover, new strategies have been developed for molecular modifications and many peptides have been studied intensively, such as histatin-5 [29], lactoferricins [31], and anoplin [32].…”

Section: Discussionmentioning

confidence: 99%

In Silico Predicted Antifungal Peptides: In Vitro and In Vivo Anti-Candida Activity

Ciociola

Magliani

Simone

et al. 2021

JoF

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It has been previously demonstrated that synthetic antibody-derived peptides could exert a significant activity in vitro, ex vivo, and/or in vivo against microorganisms and viruses, as well as immunomodulatory effects through the activation of immune cells. Based on the sequence of previously described antibody-derived peptides with recognized antifungal activity, an in silico analysis was conducted to identify novel antifungal candidates. The present study analyzed the candidacidal and structural properties of in silico designed peptides (ISDPs) derived by amino acid substitutions of the parent peptide KKVTMTCSAS. ISDPs proved to be more active in vitro than the parent peptide and all proved to be therapeutic in Galleria mellonella candidal infection, without showing toxic effects on mammalian cells. ISDPs were studied by circular dichroism spectroscopy, demonstrating different structural organization. These results allowed to validate a consensus sequence for the parent peptide KKVTMTCSAS that may be useful in the development of novel antimicrobial molecules.

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“…PMAP-37 has potent antimicrobial activity against both Grampositive (such as B. megaterium and S. aureus) and especially Gram-negative bacteria (such as E. coli, S. typhimurium, and P. aeruginosa) (38). Generally, the antimicrobial activity of AMPs is enhanced by modifying the primary and secondary structures of AMPs in a certain range to increase the net charge of AMPs, prolong their α-helix, and increase their hydrophobicity (85)(86)(87)(88). PMAP-37 (R13-I) and PMAP-37 (K20/27-I) are two analogs with substitutions of isoleucine for arginine at position 13 and isoleucine for lysine at positions 20 and 27, resulting in increased hydrophobicity of PMAP-37.…”

Section: Antibacterial Activity Of Pmap-37mentioning

confidence: 99%

Porcine Myeloid Antimicrobial Peptides: A Review of the Activity and Latest Advances

et al. 2021

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Traditional antibiotics have made great contributions to human health and animal husbandry since the discovery of penicillin in 1928, but bacterial resistance and drug residues are growing threats to global public health due to the long-term uncontrolled application of antibiotics. There is a critical need to develop new antimicrobial drugs to replace antibiotics. Antimicrobial peptides (AMPs) are distributed in all kingdoms of life, presenting activity against pathogens as well as anticancer, anti-inflammatory, and immunomodulatory activities; consequently, they have prospects as new potential alternatives to antibiotics. Porcine myeloid antimicrobial peptides (PMAPs), the porcine cathelicidin family of AMPs, have been reported in the literature in recent years. PMAPs have become an important research topic due to their strong antibacterial activity. This review focuses on the universal trends in the biochemical parameters, structural characteristics and biological activities of PMAPs.

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Advances in the Study of Structural Modification and Biological Activities of Anoplin

Cited by 20 publications

References 80 publications

Cell-Penetrating Peptides Derived from Animal Venoms and Toxins

Cell-Penetrating Peptides Derived from Animal Venoms and Toxins

In Silico Predicted Antifungal Peptides: In Vitro and In Vivo Anti-Candida Activity

Porcine Myeloid Antimicrobial Peptides: A Review of the Activity and Latest Advances

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