Bolaamphiphilic Bis-Dehydropeptide Hydrogels as Potential Drug Release Systems

Autor: Carolina Amorim, Sérgio R. S. Veloso, Elisabete M. S. Castanheira, Loic Hilliou, Renato B. Pereira, David M. Pereira, José A. Martins, Peter J. Jervis, Paula M. T. Ferreira

Publikováno v: Gels, Vol 7, Iss 2, p 52 (2021)

The self-assembly of nanometric structures from molecular building blocks is an effective way to make new functional materials for biological and technological applications. In this work, four symmetrical bolaamphiphiles based on dehydrodipeptides (p

Externí odkaz: https://doaj.org/article/61e6f46349194c53bce9dab46dceceb7

Conformation of dehydropentapeptides containing four achiral amino acid residues – controlling the role of L-valine

Autor: Michał Jewgiński, Joanna Krzciuk-Gula, Maciej Makowski, Rafał Latajka, Paweł Kafarski

Publikováno v: Beilstein Journal of Organic Chemistry, Vol 10, Iss 1, Pp 660-666 (2014)

Structural studies of pentapeptides containing an achiral block, built from two dehydroamino acid residues (ΔZPhe and ΔAla) and two glycines, as well as one chiral L-Val residue were performed using NMR spectroscopy. The key role of the L-Val resid

Externí odkaz: https://doaj.org/article/3a91b5dfb0404ae1a0dcea34d4ec85dc

Evaluation of a model photo-caged dehydropeptide as a stimuli-responsive supramolecular hydrogel

Autor: Paula M. T. Ferreira, David M. Pereira, Renato B. Pereira, Peter J. Jervis, Loic Hilliou, José A. Martins

Publikováno v: Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Nanomaterials
Volume 11
Issue 3
Nanomaterials, Vol 11, Iss 704, p 704 (2021)

Short peptides capped on the N-terminus with aromatic groups are often able to form supramolecular hydrogels, via self-assembly, in aqueous media. The rheological properties of these readily tunable hydrogels resemble those of the extracellular matri

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c445317c3b01eab4beb96df23a2b4ba0
https://hdl.handle.net/1822/72634

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Characterization of the interaction of the antifungal and cytotoxic cyclic glycolipopeptide hassallidin with sterol-containing lipid membranes

Autor: Jouni Jokela, Anu Humisto, Knut Teigen, Perttu Permi, Kaarina Sivonen, Lars Herfindal, Matti Wahlsten

Publikováno v: Biochimica et Biophysica Acta-Biomembranes

Hassallidins are cyclic glycolipopeptides produced by cyanobacteria and other prokaryotes. The hassallidin structure consists of a peptide ring of eight amino acids where a fatty acid chain, additional amino acids, and sugar moieties are attached. Ha

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14939fa91f0c24115783122adcf38509
https://pubmed.ncbi.nlm.nih.gov/31226245