Small Molecule- and Amino Acid-Induced Aggregation of Gold Nanoparticles

Langmuir ◽  
2013 ◽  
Vol 29 (25) ◽  
pp. 7661-7673 ◽  
Author(s):  
Hesham M. Zakaria ◽  
Akash Shah ◽  
Michael Konieczny ◽  
Joan A. Hoffmann ◽  
A. Jasper Nijdam ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Amino Acid ◽  
Small Molecule ◽  
Induced Aggregation

Label-free test kit for d-amino acid analysis by 1,4-benzenediboronic-acid-induced aggregation of gold nanoparticles

2020 ◽  
Vol 12 (26) ◽  
pp. 3404-3410
Author(s):  
Yan Zeng ◽  
Peng Qi ◽  
Dun Zhang
Keyword(s):  
Gold Nanoparticles ◽  
Amino Acid ◽  
Amino Acid Analysis ◽  
Label Free ◽  
Test Kit ◽  
Precision And Accuracy ◽  
Induced Aggregation

We proposed a label-free kit test for d-amino acid analysis by 1,4-benzenediboronic-acid-induced aggregation of gold nanoparticles, providing an effective and selective quantification of DAAs with excellent precision and accuracy in bacterial samples.

Influence of pH and aurate/amino acid ratios on the tuneable optical features of gold nanoparticles and nanoclusters

2017 ◽  
Vol 532 ◽  
pp. 601-608 ◽  
Author(s):  
Edit Csapó ◽  
Ditta Ungor ◽  
Zoltán Kele ◽  
Péter Baranyai ◽  
Andrea Deák ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Amino Acid ◽  
Influence Of Ph

Detection of pH-induced aggregation of “smart” gold nanoparticles with photothermal optical coherence tomography

2013 ◽  
Vol 38 (21) ◽  
pp. 4429 ◽  
Author(s):  
Peng Xiao ◽  
Qingyun Li ◽  
Yongjoon Joo ◽  
Jutaek Nam ◽  
Sekyu Hwang ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Optical Coherence Tomography ◽  
Optical Coherence ◽  
Induced Aggregation

Determination of Amino Acid Residues Responsible for Specific Interaction of Protein Kinases with Small Molecule Inhibitors

2018 ◽  
Vol 52 (3) ◽  
pp. 478-487 ◽  
Author(s):  
D. A. Karasev ◽  
A. V. Veselovsky ◽  
A. A. Lagunin ◽  
D. A. Filimonov ◽  
B. N. Sobolev
Keyword(s):  
Amino Acid ◽  
Protein Kinases ◽  
Small Molecule ◽  
Small Molecule Inhibitors ◽  
Specific Interaction ◽  
Amino Acid Residues

scholarly journals Colloidal Capsules Assembled from Gold Nanoparticles Using Small-Molecule Hydrophobic Cross-linkers

Langmuir ◽  
2019 ◽  
Vol 35 (52) ◽  
pp. 17037-17045
Author(s):  
Yijia Zhang ◽  
Wafa Abidi ◽  
Jacob M. Berlin
Keyword(s):  
Gold Nanoparticles ◽  
Small Molecule

scholarly journals A small-molecule inhibitor of BamA impervious to efflux and the outer membrane permeability barrier

2019 ◽  
Vol 116 (43) ◽  
pp. 21748-21757 ◽  
Author(s):  
Elizabeth M. Hart ◽  
Angela M. Mitchell ◽  
Anna Konovalova ◽  
Marcin Grabowicz ◽  
Jessica Sheng ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Small Molecule ◽  
Cytoplasmic Membrane ◽  
Multidrug Resistant ◽  
Resistant Bacteria ◽  
Permeability Barrier ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Bam Complex ◽  
Induced Aggregation

The development of new antimicrobial drugs is a priority to combat the increasing spread of multidrug-resistant bacteria. This development is especially problematic in gram-negative bacteria due to the outer membrane (OM) permeability barrier and multidrug efflux pumps. Therefore, we screened for compounds that target essential, nonredundant, surface-exposed processes in gram-negative bacteria. We identified a compound, MRL-494, that inhibits assembly of OM proteins (OMPs) by the β-barrel assembly machine (BAM complex). The BAM complex contains one essential surface-exposed protein, BamA. We constructed a bamA mutagenesis library, screened for resistance to MRL-494, and identified the mutation bamAE470K. BamAE470K restores OMP biogenesis in the presence of MRL-494. The mutant protein has both altered conformation and activity, suggesting it could either inhibit MRL-494 binding or allow BamA to function in the presence of MRL-494. By cellular thermal shift assay (CETSA), we determined that MRL-494 stabilizes BamA and BamAE470K from thermally induced aggregation, indicating direct or proximal binding to both BamA and BamAE470K. Thus, it is the altered activity of BamAE470K responsible for resistance to MRL-494. Strikingly, MRL-494 possesses a second mechanism of action that kills gram-positive organisms. In microbes lacking an OM, MRL-494 lethally disrupts the cytoplasmic membrane. We suggest that the compound cannot disrupt the cytoplasmic membrane of gram-negative bacteria because it cannot penetrate the OM. Instead, MRL-494 inhibits OMP biogenesis from outside the OM by targeting BamA. The identification of a small molecule that inhibits OMP biogenesis at the cell surface represents a distinct class of antibacterial agents.

scholarly journals A 13-mer peptide straddling the leucine33/proline33 polymorphism in glycoprotein IIIa does not define the PLA1 epitope

Blood ◽  
1991 ◽  
Vol 77 (9) ◽  
pp. 1964-1969 ◽  
Author(s):  
F Flug ◽  
R Espinola ◽  
LX Liu ◽  
C SinQuee ◽  
R DaRosso ◽  
...  
Keyword(s):  
Amino Acid ◽  
Polyclonal Antibodies ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Adenosine Diphosphate ◽  
Enzyme Linked Immunosorbent Assay ◽  
Amino Acid Polymorphism ◽  
Glycoprotein Iiia ◽  
Polymerase Chain ◽  
Induced Aggregation

Abstract We confirm the recent report (J Clin Invest 83:1778, 1989) of a polymorphism at amino acid 33 of platelet GPIIIa associated with the PLA1/PLA2 phenotype by using the polymerase chain reaction on cDNA derived from platelet RNA, using the base-pair primers 105–129 and 452- 428. Platelet cDNA from three PLA2-homozygous individuals, when digested with Nci I, gave two bands of 256 bp and 91 bp, whereas eight PLA1 cDNAs gave a single band of 347 bp. Two 13-mer amino acid peptides straddling the amino acid polymorphism: SDEALP (L/P) GSPRCD were synthesized for epitope studies. Two mouse polyclonal antibodies were raised: one against the PLA1-associated peptide, the other against the PLA2 peptide. Both antibodies react with either peptide, as well as with both PLA1 and PLA2 platelets. The PLA1 peptide did not block the binding of two different human anti-PLA1 antibodies to the 100-Kd GPIIIa band on immunoblot of platelet extracts; neither did it block the binding of the same antibodies to PLA1-platelet extracts in an enzyme-linked immunosorbent assay. Further studies were performed on the PLA1 epitope following subtilisin digestion of purified GPIIIa. A 55-Kd fragment was obtained that retained the PLA1 epitope as well as the first 13 N-terminal amino acids of GPIIIa. Reduction of the 55-Kd fragment resulted in loss of the PLA1 epitope with production of a 67- Kd, 21-Kd, and 10-Kd band on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The 55-Kd band does not react with LK-2, a monoclonal antibody versus GPIIIa that inhibits adenosine diphosphate, collagen, epinephrine, and thrombin-induced aggregation. Thus, the PLA1 epitope is conformation-induced, resides on an N-terminal 55-Kd fragment composed of two or more peptides held together by -SH bonds, and is not required for platelet aggregation.

scholarly journals Small molecule-decorated gold nanoparticles for preparing antibiofilm fabrics

2020 ◽  
Vol 2 (6) ◽  
pp. 2293-2302
Author(s):  
Le Wang ◽  
Michal Natan ◽  
Wenshu Zheng ◽  
Wenfu Zheng ◽  
Shaoqin Liu ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Small Molecule ◽  
Coating Technology ◽  
Ultrasound Assisted

By using ultrasound-assisted coating technology, we modified fabrics with N_Au NPs to fabricate antibiofilm fabrics.

Visual detection of arginine based on the unique guanidino group-induced aggregation of gold nanoparticles

2013 ◽  
Vol 764 ◽  
pp. 78-83 ◽  
Author(s):  
Wendan Pu ◽  
Huawen Zhao ◽  
Chengzhi Huang ◽  
Liping Wu ◽  
Dan Xu
Keyword(s):  
Gold Nanoparticles ◽  
Visual Detection ◽  
Induced Aggregation ◽  
Guanidino Group
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