76177-10-1Relevant academic research and scientific papers
Tuning the molecular weight of polymeric amphiphiles as a tool to access micelles with a wide range of enzymatic degradation rates
Slor, Gadi,Papo, Nitsan,Hananel, Uri,Amir, Roey J.
supporting information, p. 6875 - 6878 (2018/06/26)
Enyzme-responsive polymeric assemblies hold great potential for biomedical applications due to the over-expression of disease-associated enzymes, which can be utilized to activate such systems only in afflicted tissues. Herein we demonstrate that the overall molecular weight of polymeric amphiphiles, which have the same hydrophilic/hydrophobic ratio, can be tuned to create polymeric micelles with an extreme range of degradation rates. This approach expands the available set of molecular parameters that can be adjusted to tune the degradation rate of polymeric assemblies, paving new possibilities for rational design of polymeric systems with controlled degradation rates.
Mixing End Groups in Thiol-Ene/Yne Reactions as a Simple Approach toward Multienzyme-Responsive Polymeric Amphiphiles
Harnoy, Assaf J.,Papo, Nitsan,Slor, Gadi,Amir, Roey J.
, p. 2582 - 2587 (2018/11/30)
Taking advantage of the high fidelity of thiol-ene and thiol-yne chemistries, we used mixtures of thiols to prepare degradable PEG-dendron amphiphiles functionalized with two different types of enzymatically cleavable end groups. By tuning the feed ratios of the two thiols, we achieved mixtures of hybrids with statistically different ratios of end groups. Studies of the disassembly of statistically mixed hybrids showed that these amphiphiles have higher degrees of response when incubated with each of the activating enzymes, whereas a greater degree of selectivity was observed for a control mixture of two distinct amphiphiles, which required the presence of both types of enzyme to undergo complete disassembly. The potential to introduce different end groups by using a mixture of thiols in an efficient single thiol-ene or thiol-yne step opens the way for simple modification of various ene- or yne-containing polymers and tailoring of their structural and functional properties.
Solvent-free tandem synthesis of 2-thiazolines and 2-oxazolines catalyzed by a copper catalyst
Li, Xiangnan,Zhou, Baoyue,Zhang, Jin,She, Mengyao,An, Shujuan,Ge, Haixia,Li, Cong,Yin, Bing,Li, Jianli,Shi, Zhen
experimental part, p. 1626 - 1632 (2012/05/04)
Tandem reactions of nitriles with 2-aminoethanethiol hydrochloride or amino alcohols in the presence of a catalytic amount of cupric methacrylate (Cu II2L4, L = methacrylate) were employed to prepare 2-thiazolines and 2-ox
CORROSION PROTECTION COATINGS
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, (2010/08/03)
The present invention relates to new coating materials for corrosion control.
Straightforward microwave-assisted synthesis of 2-thiazolines using Lawesson's reagent under solvent-free conditions
Seijas, Julio A.,Vázquez-Tato, M. Pilar,Crecente-Campo, José
, p. 9280 - 9285 (2008/12/21)
2-Thiazolines are synthesized from carboxylic acids and 1,2-aminoalcohols in the presence of Lawesson's reagent under solventless conditions. The developed method is valid for either substituted or unsubstituted aminoalcohols and a wide variety of aromatic, heteroaromatic and aliphatic carboxylic acids; thus it constitutes a general synthetic method for these kinds of compounds. The role of Lawesson's reagent is dual: to transform the 1,2-aminoalcohol into 1,2-aminothiol and to activate its reaction with the carboxylic acid leading to the formation of a thiazoline ring, all in one pot.
3-Acyl-1,3-diaryltriazenes as neutral and selective acylating agents
?tefane, Bogdan,Ernigoj, Urh,Ko?evar, Marijan,Polanc, Slovenko
, p. 6659 - 6662 (2007/10/03)
New 3-acyl-1,3-diaryltriazenes have been prepared and their reactions with amino compounds have been studied. Reactions proceed rapidly under mild conditions to give the corresponding N-acyl products. Reagents enable chemoselective acylation of aliphatic primary and secondary amines in the presence of other acylable functional groups.
Cysteinyl peptide inhibitors of Bacillus cereus zinc β-lactamase
Bounaga, Sakina,Galleni, Moreno,Laws, Andrew P,Page, Michael I
, p. 503 - 510 (2007/10/03)
Several cysteinyl peptides have been synthesised and shown to be reversible competitive inhibitors of the Bacillus cereus metallo-β-lactamase. The pH dependence of pKi indicates that the thiol anion displaces hydroxide ion from the active site zinc(II). D,D-Peptides bind to the enzyme better than other diastereoisomers, which is compatible with the predicted stereochemistry of the active site.
