Unknown

Dataset Information

0

Dual Self-Assembled Nanostructures from Intrinsically Disordered Protein Polymers with LCST Behavior and Antimicrobial Peptides.


ABSTRACT: Antimicrobial peptides (AMPs) have attracted great interest as they constitute one of the most promising alternatives against drug-resistant infections. Their amphipathic nature not only provides them antimicrobial and immunomodulatory properties but also the ability to self-assemble into supramolecular nanostructures. Here, we propose their use as self-assembling domains to drive hierarchical organization of intrinsically disordered protein polymers (IDPPs). Using a modular approach, hybrid protein-engineered polymers were recombinantly produced, thus combining designer AMPs and a thermoresponsive IDPP, an elastin-like recombinamer (ELR). We exploited the ability of these AMPs and ELRs to self-assemble to develop supramolecular nanomaterials by way of a dual-assembly process. First, the AMPs trigger the formation of nanofibers; then, the thermoresponsiveness of the ELRs enables assembly into fibrillar aggregates. The interplay between the assembly of AMPs and ELRs provides an innovative molecular tool in the development of self-assembling nanosystems with potential use for biotechnological and biomedical applications.

SUBMITTER: Acosta S 

PROVIDER: S-EPMC7558458 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

Dual Self-Assembled Nanostructures from Intrinsically Disordered Protein Polymers with LCST Behavior and Antimicrobial Peptides.

Acosta Sergio S   Ye Zhou Z   Aparicio Conrado C   Alonso Matilde M   Rodríguez-Cabello José Carlos JC  

Biomacromolecules 20200812 10


Antimicrobial peptides (AMPs) have attracted great interest as they constitute one of the most promising alternatives against drug-resistant infections. Their amphipathic nature not only provides them antimicrobial and immunomodulatory properties but also the ability to self-assemble into supramolecular nanostructures. Here, we propose their use as self-assembling domains to drive hierarchical organization of intrinsically disordered protein polymers (IDPPs). Using a modular approach, hybrid pro  ...[more]

Similar Datasets

| S-EPMC10884422 | biostudies-literature
| S-EPMC4352815 | biostudies-literature
| S-EPMC10715794 | biostudies-literature
| S-EPMC11841035 | biostudies-literature
| S-EPMC10739243 | biostudies-literature
| S-EPMC4618764 | biostudies-literature
| S-EPMC4066902 | biostudies-literature
| S-EPMC9780108 | biostudies-literature
| S-EPMC6399351 | biostudies-literature
| S-EPMC9417027 | biostudies-literature