2019
DOI: 10.1016/j.biomaterials.2019.119286
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Targeted delivery of antimicrobial peptide by Cry protein crystal to treat intramacrophage infection

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Cited by 38 publications
(56 citation statements)
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“…We have previously reported the advantages of the Cry3Aa platform in the immobilization of enzymes and for the delivery of antimicrobial peptides due to its exceptional stability (Heater et al, 2018(Heater et al, , 2019Nair et al, 2015;Yang et al, 2019). Herein we demonstrated the utilization of the crystal-forming domain of Cry3Aa protein to directly produce 3ADI-Mb protein particles in Bt cells for myoglobin delivery.…”
Section: Discussionmentioning
confidence: 97%
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“…We have previously reported the advantages of the Cry3Aa platform in the immobilization of enzymes and for the delivery of antimicrobial peptides due to its exceptional stability (Heater et al, 2018(Heater et al, , 2019Nair et al, 2015;Yang et al, 2019). Herein we demonstrated the utilization of the crystal-forming domain of Cry3Aa protein to directly produce 3ADI-Mb protein particles in Bt cells for myoglobin delivery.…”
Section: Discussionmentioning
confidence: 97%
“…One important feature of any drug delivery system, particularly for peptide-or protein-based therapeutics, is the ability of the carriers to confer protection to their cargos. We have previously demonstrated that the framework of Cry3Aa could enhance the stability of its protein cargo (Heater et al, 2018(Heater et al, , 2019Nair et al, 2015;Yang et al, 2019). We therefore hypothesized that the 3ADI-Mb particle should also be able to stabilize its fused Mb partner.…”
Section: Production and Characterization Of 3a-mb And 3adi-mbmentioning
confidence: 99%
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“…The mechanism of antibacterial action is related to their ability to adjust membrane permeability, which destructs the membrane structure of the pathogen. One particular property that makes AMPs effective towards multidrug‐resistant bacteria strains (Yang et al, 2019) is in its wide‐scale multitargeted action (Joo et al, 2016; Zharkova et al, 2019). Usually, AMPs exhibit a net positive charge with a high ratio of hydrophobic amino acids that allows peptides to selectively bind to negatively charged bacterial membranes (Lei et al, 2019; Zhen et al, 2019) to either disrupt the membrane (Kumar et al, 2018), or to enter the bacterium and inhibit intracellular functions (Yazici et al, 2016).…”
Section: Introductionmentioning
confidence: 99%