A three-dimensional CoNi-MOF nanosheet array-based immunosensor for sensitive monitoring of human chorionic gonadotropin with core–shell ZnNi-MOF@Nile Blue nanotags

The Analyst ◽  
2020 ◽  
Vol 145 (24) ◽  
pp. 8097-8103
Author(s):  
Wenbo Lu ◽  
Zi-Ang Chen ◽  
Ming Wei ◽  
Xiaowei Cao ◽  
Xuping Sun

A sandwich-type electrochemical immunosensor for HCG detection based on a CoNi-MOF nanosheet-array and Nile Blue@ZnNi-MOF spheres is successfully exploited.

RSC Advances ◽  
2014 ◽  
Vol 4 (42) ◽  
pp. 21891-21898 ◽  
Author(s):  
Yiming Liu ◽  
Wenjuan Guo ◽  
Xiaoli Qin ◽  
Xue Meng ◽  
Xiangwei Zhu ◽  
...  

GNPs/PB/GNPs and NP-Pd were prepared to immobilize Ab1 and HRP–Ab2 respectively and combined to construct a sandwich-type immunosensor for hCG.


2020 ◽  
Vol 36 (5) ◽  
pp. 498-500
Author(s):  
Elliot M. Levine ◽  
Carlos M. Fernandez ◽  
Angela McElwee

Human chorionic gonadotropin is generally used as a biomarker to identify invasive molar pregnancy. The extent of the disease (e.g., its staging) has not, however, relied on its sonographic description. A case is presented that can illustrate some diagnostically useful sonographic features of three-dimensional transvaginal sonography for this condition. The clinical imaging of this case initially suggested it to be a benign hydatidiform mole but ultimately was diagnosed as an invasive molar pregnancy, with human chorionic gonadotropin monitoring. Clinical imaging was used to help manage this patient, with the demonstration of trophoblastic invasion of the uterine wall. Although two-dimensional sonography is commonly used to diagnose molar pregnancy, three-dimensional sonography may offer a clinical advantage for the management of invasive molar pregnancy, which can occur in 15% of benign hydatidiform molar pregnancies.


RSC Advances ◽  
2014 ◽  
Vol 4 (102) ◽  
pp. 58460-58466 ◽  
Author(s):  
Syazana Abdullah Lim ◽  
Hiroyuki Yoshikawa ◽  
Eiichi Tamiya ◽  
Hartini Mohd Yasin ◽  
Minhaz Uddin Ahmed

This study describes a highly sensitive electrochemical immunosensor for the detection of human chorionic gonadotropin (hCG) that uses gold nanoparticles (AuNP) as the electrochemical label and graphene as electrode material.


2004 ◽  
Vol 2004 (1) ◽  
pp. 35-40 ◽  
Author(s):  
Yan Wang ◽  
Hong-Li Jiao ◽  
Jin-Zhu Zhang ◽  
Rong-Qiao He

Cell growth rate and production of monoclonal antibody (MAb) of hybridoma cells producing anti-human chorionic gonadotropin (hCG) MAb have been used as investigation criteria in double-mouthed rolling bottle (DMRB). Compared with T-flask cell culture, both of the cell number and MAb production increased by approximately 42.5% when the medium was supplemented with 5% fetal calf serum (FCS) and DMRB rotated at 2 turns per minute. Yield of MAb was experimentally related to the number of viable cells. Interestingly, MAb yield was four times as high as that cultured in T-flask in the first 24 hours, and about 75% yield of total MAb was secreted by 48 hours during the culture. It appears that the promoted cell growth and MAb yield are resulted from the three-dimensional growth of hybridoma cells under a suitably revolving condition.


1993 ◽  
Vol 14 (3) ◽  
pp. 291-311
Author(s):  
JOYCE W. LUSTBADER ◽  
DAVID L. YARMUSH ◽  
STEVEN BIRKEN ◽  
DAVID PUETT ◽  
ROBERT E. CANFIELD

2002 ◽  
Vol 366 (2) ◽  
pp. 415-422 ◽  
Author(s):  
Gilles FERRAT ◽  
Jean-Guillaume RENISIO ◽  
Xavier MORELLI ◽  
Jerry SLOOTSTRA ◽  
Rob MELOEN ◽  
...  

The X-ray structure of a ternary complex between human chorionic gonadotropin hormone (hCG) and two Fvs recognizing its α and β subunits has been recently determined. The Fvs recognize the elongated hCG molecule by its two ends, one being the Leu-12–Cys-29 loop of the α subunit. We have designed and synthesized a 17-amino-acid peptide (named PepH14) derived from the sequence of this antigenic loop with the purpose of mimicking its three-dimensional structure and its affinity for antibodies. We have determined the solution structure of PepH14 by homonuclear NMR spectroscopy and derived distance restraints. Comparison of this structure with that of the corresponding antigenic loop of α-hCG reveals strong conformational similarities. In particular, the two pairs of residues that establish crucial contacts with the Fv fragment share the same conformation in PepH14 and in the authentic hormone loop. We propose a three-dimensional model of interaction of PepH14 with a llama VHH (VHH-H14) fragment cloned from a single-chain llama immunoglobulin raised against α-hCG. This model has been constrained by the chemical shift variations of the H14 1HN and 15N resonances monitored upon binding with PepH14. Mapping of the backbone chemical shift variations on the VHH structure determined by NMR indicates that PepH14 binds to VHH-H14 and forms a complex using the three complementary determining regions (CDRs). They define a shallow groove encompassing residues Thr-31, Ala-56, Tyr-59 and Trp-104 which have been shown to be in conformational exchange [Renisio, Pérez, Czisch, Guenneugues, Bornet, Frenken, Cambillau and Darbon (2002) Proteins 47, 546–555] and also Phe-37 and Ala-50. This groove is close to the hydrophobic interface area observed between VH and VL domains in Fvs from classical antibodies, which explains the rather lateral binding of PepH14 on the VHH.


1981 ◽  
Vol 4 (3) ◽  
pp. 275-279 ◽  
Author(s):  
Tatsuhiro Sekiya ◽  
Y. Furuhashi ◽  
S. Goto ◽  
S. Kaseki ◽  
Y. Tomoda ◽  
...  

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