59490-39-0Relevant academic research and scientific papers
Embedding and Positioning of Two FeII4L4 Cages in Supramolecular Tripeptide Gels for Selective Chemical Segregation
Kieffer, Marion,Garcia, Ana M.,Haynes, Cally J. E.,Kralj, Slavko,Iglesias, Daniel,Nitschke, Jonathan R.,Marchesan, Silvia
, p. 7982 - 7986 (2019)
An unreported d,l-tripeptide self-assembled into gels that embedded FeII4L4 metal–organic cages to form materials that were characterized by TEM, EDX, Raman spectroscopy, rheometry, UV/Vis and NMR spectroscopy, and circular dichroism. The cage type and concentration modulated gel viscoelasticity, and thus the diffusion rate of molecular guests through the nanostructured matrix, as gauged by 19F and 1H NMR spectroscopy. When two different cages were added to spatially separated gel layers, the gel–cage composite material enabled the spatial segregation of a mixture of guests that diffused into the gel. Each cage selectively encapsulated its preferred guest during diffusion. We thus present a new strategy for using nested supramolecular interactions to enable the separation of small molecules.
Self-Assembly of an Amino Acid Derivative into an Antimicrobial Hydrogel Biomaterial
Garcia, Ana M.,Lavendomme, Roy,Kralj, Slavko,Kurbasic, Marina,Bellotto, Ottavia,Cringoli, Maria C.,Semeraro, Sabrina,Bandiera, Antonella,De Zorzi, Rita,Marchesan, Silvia
, p. 1880 - 1886 (2020/02/05)
N-(4-Nitrobenzoyl)-Phe self-assembled into a transparent supramolecular hydrogel, which displayed high fibroblast and keratinocyte cell viability. The compound showed a mild antimicrobial activity against E. coli both as a hydrogel and in solution. Single
In Situ Switching of Site-Selectivity with Light in the Acetylation of Sugars with Azopeptide Catalysts
Eckhardt, André K.,Erb, Frederik R.,Herold, Dominik,Kind, Jonas,Niedek, Dominik,Schreiner, Peter R.,Seitz, Alexander,Thiele, Christina M.,Topp, Christopher,Wende, Raffael C.
, (2020/02/04)
We present a novel concept for the in situ control of site-selectivity of catalytic acetylations of partially protected sugars using light as external stimulus and oligopeptide catalysts equipped with an azobenzene moiety. The isomerizable azobenzene-peptide backbone defines the size and shape of the catalytic pocket, while the π-methyl-l-histidine (Pmh) moiety transfers the electrophile. Photoisomerization of the E- to the Z-azobenzene catalyst (monitored via NMR) with an LED (λ = 365 nm) drastically changes the chemical environment around the catalytically active Pmh moiety, so that the light-induced change in the catalyst shape alters site-selectivity. As a proof of principle, we employed (4,6-O-benzylidene)methyl-α-d-pyranosides, which provide a change in regioselectivity from 2:1 (E) to 1:5 (Z) for the monoacetylated products at room temperature. The validity of this new catalyst-design concept is further demonstrated with the regioselective acetylation of the natural product quercetin. In situ irradiation NMR spectroscopy was used to quantify photostationary states under continuous irradiation with UV light.
Design, synthesis and SAR studies of tripeptide analogs with the scaffold 3-phenylpropane-1,2-diamine as aminopeptidase N/CD13 inhibitors
Shang, Luqing,Fang, Hao,Zhu, Huawei,Wang, Xuejian,Wang, Qiang,Mu, Jiajia,Wang, Binghe,Kishioka, Shiroh,Xu, Wenfang
experimental part, p. 2775 - 2784 (2009/08/15)
Aminopeptidase N (APN), belonged to metalloproteinase, is an essential peptidase involved in the process of tumor invasion and metastasis. A series of tripeptide analogs with the scaffold 3-phenylpropane-1,2-diamine were designed, synthesized and evaluate
Stabilizing and destabilizing effects of phenylalanine → F 5-phenylalanine mutations on the folding of a small protein
Woll, Matthew G.,Hadley, Erik B.,Mecozzi, Sandro,Gellman, Samuel H.
, p. 15932 - 15933 (2007/10/03)
We report a systematic evaluation of phenylalanine-to-pentafluorophenylalanine (Phe → F5-Phe) mutants for the 35-residue chicken villin headpiece subdomain (c-VHP), the hydrophobic core of which features a cluster of three Phe side chains (residues 6, 10, and 17). Phe → F5-Phe mutations are interesting because aryl-perfluoroaryl interactions of optimal geometry are intrinsically more favorable than aryl-aryl interactions and because perfluoroaryl units are more hydrophobic than are analogous aryl units. One mutant, Phe-10 → F5-Phe, provides enhanced tertiary structural stability relative to the native sequence. The other six mutants analyzed caused a decrease in stability. Copyright
