Document Detail


Development of a Histidine-Targeted Spectrophotometric Sensor Using Ni(II)NTA Functionalized Au and Ag Nanoparticles.
MedLine Citation:
PMID:  22026818     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
An antibody-free diagnostic reagent has been developed based on the aggregation-induced colorimetric change of Ni(II)NTA functionalized colloidal gold and silver nanoparticles. This diagnostic strategy utilizes the high binding affinity of histidine-rich proteins with Ni(II)NTA to capture and crosslink the histidine-rich protein mimics with the silver and gold nanoparticles. In model studies, the aggregation behavior of the Ni(II)NTA nanoparticles was tested against synthetic targets including charged poly-amino acids (histidine, lysine, arginine, and aspartic acid) and mimics of Plasmodium falciparum histidine-rich protein 2 (pfHRP-II). Aggregation of the nanoparticle sensor was induced by all of the basic poly-amino acids including poly-L-histidine within the pH range (5.5-9.0) tested, which is likely caused by the coordination between the multivalent polymer target and Ni(II)NTA groups on multiple particles. The peptide mimics induced aggregation of the nanoparticles only near their pKa's with higher limits of detection. In addition, monomeric amino acids do not show any aggregation behavior, suggesting that multiple target binding sites are necessary for aggregation. Long term stability studies showed that gold but not silver nanoparticles remained stable and exhibited similar aggregation behavior after one month of storage at room temperature and 37oC. These results suggest that Ni(II)NTA gold nanoparticles could be further investigated for use as a sensor to detect histidine-rich proteins in biological samples.
Authors:
Joshua David Swartz; Christopher P Gulka; Frederick R Haselton; David W Wright
Related Documents :
18548688 - Preparation and properties of trypsin chemically attached to eedq activated styrene-met...
15375118 - Adaptive acid tolerance response of streptococcus sobrinus.
19608608 - Global transcriptional analysis of acid-inducible genes in streptococcus mutans: multip...
20178568 - Characterization of mler, a positive regulator of malolactic fermentation and part of t...
8987898 - Rapid gc analysis of cellular fatty acids for characterizing lactobacillus sake and lac...
15357958 - A library synthesis of 4-hydroxy-3-methyl-6-phenylbenzofuran-2-carboxylic acid ethyl es...
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-10-25
Journal Detail:
Title:  Langmuir : the ACS journal of surfaces and colloids     Volume:  -     ISSN:  1520-5827     ISO Abbreviation:  -     Publication Date:  2011 Oct 
Date Detail:
Created Date:  2011-10-26     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9882736     Medline TA:  Langmuir     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Elongator complex is critical for cell cycle progression and leaf patterning in Arabidopsis.
Next Document:  Molecular Typing of Mycobacterium Tuberculosis Isolates Circulating in Jiangsu Province, China.