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1.
Biomacromolecules ; 24(11): 4646-4652, 2023 11 13.
Artigo em Inglês | MEDLINE | ID: mdl-37792488

RESUMO

Thiol-reactive Michael acceptors are commonly used for the formation of chemically cross-linked hydrogels. In this paper, we address the drawbacks of many Michael acceptors by introducing pyridazinediones as new cross-linking agents. Through the use of pyridazinediones and their mono- or dibrominated analogues, we show that the mechanical strength, swelling ratio, and rate of gelation can all be controlled in a pH-sensitive manner. Moreover, we demonstrate that the degradation of pyridazinedione-gels can be induced by the addition of thiols, thus providing a route to responsive or dynamic gels, and that monobromo-pyridazinedione gels are able to support the proliferation of human cells. We anticipate that our results will provide a valuable and complementary addition to the existing toolkit of cross-linking agents, allowing researchers to tune and rationally design the properties of biomedical hydrogels.


Assuntos
Hidrogéis , Compostos de Sulfidrila , Humanos , Hidrogéis/química , Compostos de Sulfidrila/química , Reagentes de Ligações Cruzadas/química
2.
Chem Commun (Camb) ; 59(72): 10749-10752, 2023 Sep 07.
Artigo em Inglês | MEDLINE | ID: mdl-37602809

RESUMO

The group 7 complexes [M(κ3-2,6-(R2PO)2C5H3N)(CO)2L][BArF4] [M = Mn, R = iPr, L = THF; M = Re, R = tBu, L = vacant site] undergo in crystallo solid-gas reactivity with CO to form the products of THF substitution or CO addition respectively. There is a large, local, adaptive change of [BArF4] anions for M = Mn, whereas for M = Re the changes are smaller and also remote to the site of reactivity.

3.
Biochem Biophys Res Commun ; 387(1): 153-7, 2009 Sep 11.
Artigo em Inglês | MEDLINE | ID: mdl-19577540

RESUMO

An intein is a polypeptide that interrupts the functional domains of a protein, called the exteins. The intein can facilitate its own excision from the exteins, concomitant with the ligation of the exteins, in a process called protein splicing. The alpha subunit of the ribonucleotide reductase of the extreme thermophile Pyrococcus abyssi is interrupted by three inteins in separate insertion sites. Each intein can facilitate protein splicing when over-expressed in Escherichia coli, with affinity domains serving as the exteins. The influence of the N-terminal flanking residue on the efficiency of splicing is specific to each intein. Each intein has a different downstream nucleophilic residue, and cannot tolerate substitution to a residue of lesser or equal nucleophilicity. The influence of the conserved penultimate His also differs between the inteins.


Assuntos
Inteínas , Processamento de Proteína , Pyrococcus abyssi/enzimologia , Ribonucleotídeo Redutases/metabolismo
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