Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 2 de 2
Filtrar
Mais filtros

Base de dados
Ano de publicação
Tipo de documento
Assunto da revista
País de afiliação
Intervalo de ano de publicação
1.
Chembiochem ; 23(20): e202200332, 2022 10 19.
Artigo em Inglês | MEDLINE | ID: mdl-35951442

RESUMO

Although viruses have been successfully repurposed as vaccines, antibiotics, and anticancer therapeutics, they also raise concerns regarding genome integration and immunogenicity. Virus-like particles and non-viral protein cages represent a potentially safer alternative but often lack desired functionality. Here, we investigated the utility of a new enzymatic bioconjugation method, called lysine acylation using conjugating enzymes (LACE), to chemoenzymatically modify protein cages. We equipped two structurally distinct protein capsules with a LACE-reactive peptide tag and demonstrated their modification with diverse ligands. This modular approach combines the advantages of chemical conjugation and genetic fusion and allows for site-specific modification with recombinant proteins as well as synthetic peptides with facile control of the extent of labeling. This strategy has the potential to fine-tune protein containers of different shape and size by providing them with new properties that go beyond their biologically native functions.


Assuntos
Lisina , Peptídeos , Lisina/metabolismo , Peptídeos/metabolismo , Proteínas Recombinantes/genética , Acilação , Antibacterianos
2.
ACS Chem Biol ; 16(5): 838-843, 2021 05 21.
Artigo em Inglês | MEDLINE | ID: mdl-33881303

RESUMO

Nanoparticle-based delivery systems have shown great promise for theranostics and bioimaging on the laboratory scale due to favorable pharmacokinetics and biodistribution. In this study, we examine the utility of a cage-forming variant of the protein lumazine synthase, which was previously designed and evolved to encapsulate biomacromolecular cargo. Linking antibody-binding domains to the exterior of the cage enabled binding of targeting immunoglobulins and cell-specific uptake of encapsulated cargo. Protein nanocages displaying antibody-binding domains appear to be less immunogenic than their unmodified counterparts, but they also recruit serum antibodies that can mask the efficacy of the targeting antibody. Our study highlights the strengths and limitations of a common targeting strategy for practical nanoparticle-based delivery applications.


Assuntos
Materiais Biocompatíveis/química , Complexos Multienzimáticos/química , Nanocápsulas/química , Anticorpos/química , Anticorpos/imunologia , Permeabilidade da Membrana Celular , Composição de Medicamentos , Liberação Controlada de Fármacos , Humanos , Imunoglobulinas/química , Imunoglobulinas/imunologia , Terapia de Alvo Molecular , Engenharia de Proteínas , Propriedades de Superfície , Distribuição Tecidual
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA