guest ::
| Home > Publications database > Differences in activity of actinoporins are related with the hydrophobicity of their N-terminus. > print |
| Home > Publications database > Differences in activity of actinoporins are related with the hydrophobicity of their N-terminus. > print |
| 001 | 127406 | ||
| 005 | 20240228140925.0 | ||
| 024 | 7 | _ | |a 10.1016/j.biochi.2015.06.024 |2 doi |
| 024 | 7 | _ | |a pmid:26134716 |2 pmid |
| 024 | 7 | _ | |a 0300-9084 |2 ISSN |
| 024 | 7 | _ | |a 1638-6183 |2 ISSN |
| 024 | 7 | _ | |a altmetric:4240160 |2 altmetric |
| 037 | _ | _ | |a DKFZ-2017-03429 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 540 |
| 100 | 1 | _ | |a Ros, Uris |b 0 |
| 245 | _ | _ | |a Differences in activity of actinoporins are related with the hydrophobicity of their N-terminus. |
| 260 | _ | _ | |a Paris [u.a.] |c 2015 |b Elsevier |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1508844428_29223 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a Actinoporins are pore-forming toxins (PFT) produced by sea anemones with molecular mass around 20 kDa and high affinity for sphingomyelin. The most studied atinoporins are sticholysins I and II (StI/StII) from Stichodactyla helianthus, equinatoxin II (EqtII) from Actinia equina, and fragaceatoxin C (FraC) from Actinia fragacea. Their N-terminal sequences encompassing residues 1-30 seem to be the best candidates for pore formation. This segment comprises an amphipathic α-helix preceded by a more or less hydrophobic segment, depending on the toxin, of around 10 amino acid residues. Although it is clear that the N-terminal is the most variable sequence in this protein family, the role of their hydrophobic segment in not fully understood. Here we show a comparison of StI, StII, EqtII, and FraC activities with that of their respective N-terminal synthetic peptides. The hemolytic and permeabilizing activity of the peptides reproduce qualitatively the behavior of their respective parental proteins and are particularly related to the hydrophobicity of the corresponding 1-10 segment. Furthermore, the dendrogram analysis of actinoporins' N-terminal sequence allows relating differences in alignment with differences in activity among the four toxins. We have also evaluated the penetration depth of the N-terminal segment of StI and StII by using Trp-containing peptide-analogs. Our data suggest that the N-terminus of StII is more deeply buried into the hydrophobic core of the bilayer than that of StI. We hypothesize that the highest activity of StII could be ascribed to a larger hydrophobic continuum, an uninterrupted sequence of non-charged mainly hydrophobic amino acid residues, of its N-terminus promoting a highest ability to partially insert in the membrane core. Moreover, as we show for four related peptides that a higher hydrophobicity contributes to increase the activity, we reinforce the notion that this property must be taken into account to design new potent membranotropic agents. |
| 536 | _ | _ | |a 312 - Functional and structural genomics (POF3-312) |0 G:(DE-HGF)POF3-312 |c POF3-312 |f POF III |x 0 |
| 588 | _ | _ | |a Dataset connected to CrossRef, PubMed, |
| 650 | _ | 7 | |a Peptides |2 NLM Chemicals |
| 700 | 1 | _ | |a Rodríguez-Vera, Wendy |b 1 |
| 700 | 1 | _ | |a Pedrera, Lohans |b 2 |
| 700 | 1 | _ | |a Valiente, Pedro A |b 3 |
| 700 | 1 | _ | |a Cabezas, Sheila |b 4 |
| 700 | 1 | _ | |a Lanio, María E |b 5 |
| 700 | 1 | _ | |a García-Sáez, Ana J |0 P:(DE-HGF)0 |b 6 |
| 700 | 1 | _ | |a Alvarez, Carlos |b 7 |
| 773 | _ | _ | |a 10.1016/j.biochi.2015.06.024 |g Vol. 116, p. 70 - 78 |0 PERI:(DE-600)2011725-5 |p 70 - 78 |t Biochimie |v 116 |y 2015 |x 0300-9084 |
| 909 | C | O | |o oai:inrepo02.dkfz.de:127406 |p VDB |
| 910 | 1 | _ | |a Deutsches Krebsforschungszentrum |0 I:(DE-588b)2036810-0 |k DKFZ |b 6 |6 P:(DE-HGF)0 |
| 913 | 1 | _ | |a DE-HGF |l Krebsforschung |1 G:(DE-HGF)POF3-310 |0 G:(DE-HGF)POF3-312 |2 G:(DE-HGF)POF3-300 |v Functional and structural genomics |x 0 |4 G:(DE-HGF)POF |3 G:(DE-HGF)POF3 |b Gesundheit |
| 914 | 1 | _ | |y 2015 |
| 915 | _ | _ | |a Nationallizenz |0 StatID:(DE-HGF)0420 |2 StatID |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0300 |2 StatID |b Medline |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0310 |2 StatID |b NCBI Molecular Biology Database |
| 915 | _ | _ | |a JCR |0 StatID:(DE-HGF)0100 |2 StatID |b BIOCHIMIE : 2015 |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0200 |2 StatID |b SCOPUS |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0600 |2 StatID |b Ebsco Academic Search |
| 915 | _ | _ | |a Peer Review |0 StatID:(DE-HGF)0030 |2 StatID |b ASC |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0199 |2 StatID |b Thomson Reuters Master Journal List |
| 915 | _ | _ | |a WoS |0 StatID:(DE-HGF)0110 |2 StatID |b Science Citation Index |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)0150 |2 StatID |b Web of Science Core Collection |
| 915 | _ | _ | |a WoS |0 StatID:(DE-HGF)0111 |2 StatID |b Science Citation Index Expanded |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)1030 |2 StatID |b Current Contents - Life Sciences |
| 915 | _ | _ | |a DBCoverage |0 StatID:(DE-HGF)1050 |2 StatID |b BIOSIS Previews |
| 915 | _ | _ | |a IF < 5 |0 StatID:(DE-HGF)9900 |2 StatID |
| 920 | 1 | _ | |0 I:(DE-He78)B160-20160331 |k B160 |l Membranbiophysik |x 0 |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a I:(DE-He78)B160-20160331 |
| 980 | _ | _ | |a UNRESTRICTED |
| Library | Collection | CLSMajor | CLSMinor | Language | Author |
|---|