Insights on the structure‐activity relationship of peptides derived from Sticholysin II-Reference-Cited by-同舟云学术

Insights on the structure‐activity relationship of peptides derived from Sticholysin II

Published:2018-02-16 Issue:5 Volume:110 Page:e23097
ISSN:2475-8817
Container-title:Peptide Science
language:en
Short-container-title:Peptide Science

Author:

Lima de Oliveira Aline¹²,Maffud Cilli Eduardo³,Ros Uris⁴,Crusca Jr Edson³,Lanio María Eliana⁴,Alvarez Carlos⁴⁵,Schreier Shirley⁵,Aguiar Pertinhez Thelma²⁶^ORCID,Spisni Alberto²

Affiliation:

1. Institute of Chemistry, University of BrasiliaBrasilia DF Brazil

2. Department of Medicine and SurgeryUnit of Biochemistry, University of ParmaParma Italy

3. Department of Biochemistry and Chemical TechnologyInstitute of Chemistry, São Paulo State UniversityAraraquara Brazil

4. Center for Protein Studies, Biology FacultyUniversity of HavanaHavana Cuba

5. Department of BiochemistryInstitute of Chemistry, University of São Paulo São Paulo Brazil

6. Transfusion Medicine Unit, AUSL ‐ IRCCS Reggio Emilia Italy

Funder

Conselho Nacional de Desenvolvimento Científico e Tecnológico

Fundação de Amparo à Pesquisa do Estado de São Paulo

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,Biophysics

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/bip.23097

Reference44 articles.

1. Cytolytic peptide and protein toxins from sea anemones (Anthozoa: Actiniaria)

2. Primary and secondary structure of a pore-forming toxin from the sea anemone, Actinia equina L., and its association with lipid vesicles

3. Mechanism of Membrane Permeabilization by Sticholysin I, a Cytolysin Isolated from the Venom of the Sea Anemone Stichodactyla helianthus

4. Sizing the Radius of the Pore Formed in Erythrocytes and Lipid Vesicles by the Toxin Sticholysin I from the Sea Anemone Stichodactyla helianthus

5. Pore formation by actinoporins, cytolysins from sea anemones

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1. Structural foundations of sticholysin functionality;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2021-10

2. Self-association and folding in membrane determine the mode of action of peptides from the lytic segment of sticholysins;Biochimie;2019-01

3. Dissecting the mechanism of action of actinoporins. Role of the N-terminal amphipathic α-helix in membrane binding and pore activity of sticholysins I and II;PLOS ONE;2018-08-30