Enhanced Intracellular Delivery of Quantum Dot and Adenovirus Nanoparticles Triggered by Acidic pH via Surface Charge Reversal

2008 ◽  
Vol 19 (4) ◽  
pp. 797-801 ◽  
Author(s):  
Hyejung Mok ◽  
Ji Won Park ◽  
Tae Gwan Park
2006 ◽  
Vol 17 (4) ◽  
pp. 920-927 ◽  
Author(s):  
James B. Delehanty ◽  
Igor L. Medintz ◽  
Thomas Pons ◽  
Florence M. Brunel ◽  
Philip E. Dawson ◽  
...  

2015 ◽  
Vol 39 (1) ◽  
pp. 279-286 ◽  
Author(s):  
Junyu Zhang ◽  
Fang-Xing Xiao ◽  
Guangcan Xiao ◽  
Bin Liu

CdS QD sensitized TiO2 nanobelt nanostructures were fabricated by a facile self-assembly approach and the photocatalytic performance of the well-defined hybrid heterostructure was systematically probed.


2009 ◽  
Author(s):  
James B. Delehanty ◽  
Christopher E. Bradburne ◽  
Igor L. Medintz ◽  
Dorothy Farrell ◽  
Thomas Pons ◽  
...  

2021 ◽  
Author(s):  
Atefeh Ghorbani ◽  
Justin John King ◽  
Mani Larijani

Activation-induced cytidine deaminase (AID) is a member of the apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like (APOBEC) family of cytidine deaminases. AID mutates immunoglobulin loci to initiate secondary antibody diversification. The APOBEC3 (A3) sub-branch mutates viral pathogens in the cytosol and acidic endosomal compartments. Accordingly, AID functions optimally near neutral pH, while most A3s are acid-adapted (optimal pH 5.5-6.5). To gain a structural understanding for this pH disparity, we constructed high-resolution maps of AID catalytic activity vs pH. We found AID’s optimal pH was 7.3 but it retained most (>70%) of the activity at pH 8. Probing of ssDNA-binding residues near the catalytic pocket, key for bending ssDNA into the pocket (e.g R25) yielded mutants with altered pH preference, corroborating previous findings that the equivalent residue in APOBEC3G (H216) underlies its acidic pH preference. AID from bony fish exhibited more basic optimal pH (pH 7.5-8.1) and several R25-equivalent mutants altered pH preference. Comparison of pH optima across the AID/APOBEC3 family revealed an inverse correlation between positive surface charge and overall catalysis.  The paralogue with the most robust catalytic activity (APOBEC3A) has the lowest surface charge, most acidic pH preference, while the paralogue with the most lethargic catalytic rate (AID) has the most positive surface charge and highest optimal pH. We suggest one possible mechanism is through surface charge dictating an overall optimal pH that is different from the optimal pH of the catalytic pocket microenvironment. These findings illuminate an additional structural mechanism that regulates AID/APOBEC3 mutagenesis.


2012 ◽  
Vol 7 (6) ◽  
pp. 1143-1151 ◽  
Author(s):  
Eric Chau ◽  
Justin F. Galloway ◽  
Antoinette Nelson ◽  
Patrick N. Breysse ◽  
Denis Wirtz ◽  
...  

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