38862-24-7Relevant articles and documents
Polymer vesicles containing small vesicles within interior aqueous compartments and pH-responsive transmembrane channels
Chiu, Hsin-Cheng,Lin, Yue-Wen,Huang, Yi-Fong,Chuang, Chih-Kai,Chern, Chorng-Shyan
, p. 1875 - 1878 (2008)
(Figure Presented) Multivesicle assemblies with pH-responsive transmembrane channels in the vesicle walls (see picture) were made by two-step double emulsion of copolymers comprising acrylic acid and acrylate of 1,2-distearoyl-rac-glycerol. These assemblies mimic eukaryotic cells, which contain functional organelles within the cell walls.
Elaboration of densely functionalized polylactide nanoparticles from N-acryloxysuccinimide-based block copolymers
Handke, Nadege,Trimaille, Thomas,Luciani, Elsa,Rollet, Marion,Delair, Thierry,Verrier, Bernard,Bertin, Denis,Gigmes, Didier
, p. 1341 - 1350 (2011)
Poly(N-acryloxysuccinimide) (PNAS) and poly(N-acryloxysuccinimide-co-N- vinylpyrrolidone) (P(NAS-co-NVP)) of adjustable molecular weights and narrow polydispersities were prepared by nitroxide-mediated polymerization (NMP) in N,N-dimethylformamide in the presence of free SG1 (N-tert-butyl-N-1- diethylphosphono-(2,2-dimethylpropyl) nitroxide), with MAMA-SG1 (N-(2-methylpropyl)-N-(1-diethylphosphono-2,2-dimethylpropyl) -O-(2-carboxylprop-2-yl)hydroxylamine) alkoxyamine as initiator. The reactivity ratios of NAS and NVP were determined to be rNAS = 0.12 and r NVP = 0, indicating a strong alternating tendency for the P(NAS-co-NVP) copolymer. NAS/NVP copolymerization was then performed from a SG1-functionalized poly(D,L-lactide) (PLA-SG1) macro-alkoxyamine as initiator, leading to the corresponding PLA-b-P(NAS-co-NVP) block copolymer, with similar NAS and NVP reactivity ratios as mentioned above. The copolymer was used as a surface modifier for the PLA diafiltration and nanoprecipitation processes to achieve nanoparticles in the range of 450 and 150 nm, respectively. The presence of the functional/hydrophilic P(NAS-co-NVP) block, and particularly the N-succinimidyl (NS) ester moieties at the particle surface, was evidenced by ethanolamine derivatization and zeta potential measurements.
Thermo-responsive shell cross-linked PMMA-b-P(NIPAAm-co-NAS) micelles for drug delivery
Chang, Cong,Wei, Hua,Wu, De-Qun,Yang, Bin,Chen, Ni,Cheng, Si-Xue,Zhang, Xian-Zheng,Zhuo, Ren-Xi
, p. 333 - 340 (2011)
Thermo-responsive amphiphilic poly(methyl methacrylate)-b-poly(N- isopropylacrylamide-co-N-acryloxysuccinimide) (PMMA-b-P(NIPAAm-co-NAS)) block copolymer was synthesized by successive RAFT polymerizations. The uncross-linked micelles were facilely prepared by directly dissolving the block copolymer in an aqueous medium, and the shell cross-linked (SCL) micelles were further fabricated by the addition of ethylenediamine as a di-functional cross-linker into the micellar solution. Optical absorption measurements showed that the LCST of uncross-linked and cross-linked micelles was 31.0 °C and 40.8 °C, respectively. Transmission electron microscopy (TEM) showed that both uncross-linked and cross-linked micelles exhibited well-defined spherical shape in aqueous phase at room temperature, while the SCL micelles were able to retain the spherical shape with relatively smaller dimension even at 40 °C due to the cross-linked structure. In vitro drug release study demonstrated a slower and more sustained drug release behavior from the SCL micelles at high temperature as compared with the release profile of uncross-linked micelles, indicating the great potential of SCL micelles developed herein as novel smart carriers for controlled drug release.
Effective inhibitors of hemagglutination by influenza virus synthesized from polymers having active ester groups. Insight into mechanism of inhibition
Mammen,Dahmann,Whitesides
, p. 4179 - 4190 (1995)
Highly effective sialic acid-containing inhibitors of influenza virus X- 31 were synthesized using poly[N-(acryoyloxy)succinimide] (pNAS), a polymer preactivated by incorporation of active ester groups. Polymers containing two and three different components were prepared by sequential reaction of pNAS with two and three amines, respectively. This preparation of co- and terpolymers was synthetically more efficient than methods involving copolymerization of different monomers and gave polymers that were more easily compared than those generated by copolymerization. Polymers in this study (prepared from a single batch of pNAS) had a constant degree of polymerization (DP ? 2000) and probably had a distribution of components that was more random than analogous polymers prepared by copolymerization. Use of C-glycosides of sialic acid made it possible to investigate inhibition by different polymers at temperatures ranging from 4 to 36°C without artifacts due to the hydrolytic action of neuraminidase. The inhibitors were, in general, more effective at 36 °C than at 4 °C. The hemagglutination (HAI) assay was used to measure the value of the inhibition constant K(i)/(HAI) each polymer. The value of K(i)/(HAI) for the two-component polymer containing 20% sialic acid on a polyacrylamide backbone at 4 °C was 4 nM (in terms of the sialic acid moieties present in solution) and was approximately 50-fold more effective than the best inhibitors previously described and 25-fold more effective than the best naturally occurring inhibitor. The most effective inhibitor synthesized in this work contained 10% benzyl amine and 20% sialic acid on a polyacrylamide backbone, and its value of K(i)/(HAI) was 600 pM at 36 °C. Approximately 100 polymers that differed in one or two components were assayed to distinguish between two limiting mechanisms for inhibition of the interaction between the surfaces of virus and erythrocytes: high-affinity binding through polyvalency, and steric stabilization. The results suggest that both mechanisms play an important role. The system comprising polyvalent inhibitors of agglutination of erythrocytes by influenza provides a system that may be useful as a model for inhibitors of other pathogen-host interactions, a large number of which are themselves polyvalent.
Efficient Amino-Sulfhydryl Stapling on Peptides and Proteins Using Bifunctional NHS-Activated Acrylamides
Silva, Maria J. S. A.,Faustino, Hélio,Coelho, Jaime A. S.,Pinto, Maria V.,Fernandes, Adelaide,Compa?ón, Ismael,Corzana, Francisco,Gasser, Gilles,Gois, Pedro M. P.
supporting information, p. 10850 - 10857 (2021/04/15)
Widely used reagents in the peptide functionalization toolbox, Michael acceptors and N-hydroxysuccinimide (NHS) activated esters, are combined in NHS-activated acrylamides for efficient chemoselective amino-sulfhydryl stapling on native peptides and proteins. NHS-activated acrylamides allow for a fast functionalization of N-terminal cysteines (k2=1.54±0.18×103 M?1 s?1) under dilute aqueous conditions, enabling selectivity over other nucleophilic amino acids. Additionally, the versatility of these new bioconjugation handles was demonstrated in the cross-linking of in-chain or C-terminal cysteines with nearby lysine residues. NHS-activated acrylamides are compatible with the use of other cysteine selective reagents, allowing for orthogonal dual-modifications. This strategy was successfully applied to the late-stage functionalization of peptides and proteins with a PEG unit, fluorescent probe, and cytotoxic agent. The level of molecular control offered by NHS-activated acrylamides is expected to promote amino-sulfhydryl stapling technology as a powerful strategy to design functional bioconjugates.
A GENETICALLY ENCODED, PHAGE-DISPLAYED CYCLIC PEPTIDE LIBRARY AND METHODS OF MAKING THE SAME
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Paragraph 0094; 00117-00119; 00158; 00163, (2020/12/07)
Embodiments of the present disclosure pertain to methods of selecting cyclic peptides that bind to a target by transforming a phage display library with a plurality of nucleic acids into bacterial host cells, where the nucleic acids include phage coat protein genes with a combinatorial region that encodes at least one cysteine and at least one non-canonical amino acid. The transformation results in the production of phage particles with phage coat proteins where the cysteine and the non-canonical amino acid couple to one another to form a cyclic peptide library. Phage particles are then screened against the desired target to select bound cyclic peptides. Amino acid sequences of the selected cyclic peptides are then identified. Additional embodiments pertain to methods of constructing a phage display library that encodes the cyclic peptides. Further embodiments of the present disclosure pertain to the produced cyclic peptides, phage display libraries and phage particles.
