Search results
Search for "cell compatibility" in Full Text gives 4 result(s) in Beilstein Journal of Organic Chemistry.
Synthesis and bioactivity of pyrrole-conjugated phosphopeptides
Beilstein J. Org. Chem. 2022, 18, 159–166, doi:10.3762/bjoc.18.17
- , despite that 4a bears ᴅ-phosphoserine and 2g bears ᴅ-phosphotyrosine. This result likely warrants further investigation on 4a. Another dipyrrole-conjugated peptide, 6b, was also selected for further study as a comparison to 4a since it shows good cell compatibility at 200 μM. We also compared the cell
- contributes to the cell death caused by 1 over days 2 and 3. These results together indicate the drastic morphological changes of phosphopeptides upon the addition of ALP may serve as a useful indicator to predict the cell compatibility or cytotoxicity of phosphopeptides. Conclusion In summary, this work
Enzyme-instructed morphological transition of the supramolecular assemblies of branched peptides
Beilstein J. Org. Chem. 2020, 16, 2709–2718, doi:10.3762/bjoc.16.221
- biomaterials, especially in cellular environment. Thus, we decided to further explore the molecular space and cell compatibility of enzyme-responsive branched peptides. Here, we report the use of an enzymatic reaction to cleave the branch off branched peptides for inducing the morphological transition of the
- concentrations, exhibit the same morphological appearances, agreeing with the statement that the nanofibers likely are made of Nap-ffky. Cytotoxicity, cell lysates, and protein delivery We investigated the cell compatibility of 1 and 2 by incubation with two kinds of mammalian cells, HeLa and Saos-2 cells, using
Synthesis and evaluation of the biostability and cell compatibility of novel conjugates of nucleobase, peptidic epitope, and saccharide
Beilstein J. Org. Chem. 2015, 11, 1352–1359, doi:10.3762/bjoc.11.145
- .11.145 Abstract This article reports the synthesis of a new class of conjugates containing a nucleobase, a peptidic epitope, and a saccharide and the evalution of their gelation, biostability, and cell compatibility. We demonstrate a facile synthetic process, based on solid-phase peptide synthesis of
- (stargazin) [14] and LGFNI is from a synapse associated protein 102 (SAP102) [15]. We connected these two functional peptide sequences with a nucleobase, and saccharide (or not). After investigating the gelation, biostability, and cell-compatibility properties of these conjugates (1–8), we found that all the
- slightly increased in the treatment of the mixture of 1 + 8 (about 3% left) with proteinase K, comparing to the case of 8 incubated with proteinase K at 24 h. This result is consistent with TEM investigations showing that there are weak interactions between 1 and 8. Cell compatibility Cell compatibility is
Synthesis of novel conjugates of a saccharide, amino acids, nucleobase and the evaluation of their cell compatibility
Beilstein J. Org. Chem. 2014, 10, 2406–2413, doi:10.3762/bjoc.10.250
- synthesis of a novel type of conjugate of three fundamental biological build blocks (i.e., saccharide, amino acids, and nucleobase) and their cell compatibility. The facile synthesis starts with the synthesis of nucleobase and saccharide derivatives, then uses solid-phase peptide synthesis (SPPS) to build
- conjugates of saccharide–amino acids–nucleobase (SAN), like the previously reported conjugates of nucleobase–amino acids–saccharide (NAS) and nucleobase–saccharide–amino acids (NSA), are mammalian cell compatible. Keywords: cell compatibility; nucleobase; peptides; saccharide; Introduction As a result of
- (NSA) [19] are able to self-assemble to form supramolecular hydrogels and exhibit promising biological functions, such as promoting the development of zygotes [20]. Moreover, both NAS- and NSA-type conjugates exhibit excellent cell compatibility. Except for a few known motifs (naphthalene [21][22
Other Beilstein-Institut Open Science Activities
