A global benchmark study using affinity-based biosensors

J 2009

A global benchmark study using affinity-based biosensors

RICH, Rebecca L., Giuseppe A. PAPALIA, Petr SKLÁDAL, [from all world] [109 OTHER AUTHORS], David G. MYSZKA et. al.

Základní údaje

Originální název

A global benchmark study using affinity-based biosensors

Název česky

Globální srovnávací studie afinitních biosensor

Autoři

RICH, Rebecca L. (840 Spojené státy), Giuseppe A. PAPALIA (840 Spojené státy), Petr SKLÁDAL (203 Česká republika, garant), [from all world] [109 OTHER AUTHORS] (840 Spojené státy) a David G. MYSZKA (840 Spojené státy)

Vydání

Analytica Chimica Acta, Amsterdam, Elsevier Science Publishers, 2009, 0003-2670

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 3.757

Kód RIV

RIV/00216224:14310/09:00036491

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000263789500009

Klíčová slova česky

Biosensor; Protilátka; Biacore

Klíčová slova anglicky

Biosensor; Antibody; Biacore

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 28. 8. 2009 21:49, prof. RNDr. Petr Skládal, CSc.

Anotace

ORIG CZ

V originále

To explore the variability in biosensor studies, 150 participants from 20 countries were given the same protein samples and asked to determine kinetic rate constants for the interaction. We chose a protein system that was amenable to analysis using different biosensor platforms as well as by users of different expertise levels. The two proteins (a 50-kDa Fab and a 60-kDa glutathione S-transferase [GST] antigen) form a relatively high-affinity complex, so participants needed to optimize several experimental parameters, including ligand immobilization and regeneration conditions as well as analyte concentrations and injection/dissociation times. Although most participants collected binding responses that could be fit to yield kinetic parameters, the quality of a few data sets could have been improved by optimizing the assay design. Once these outliers were removed, the average reported affinity across the remaining panel of participants was 620 pM with a standard deviation of 980 pM. These results demonstrate that when this biosensor assay was designed and executed appropriately, the reported rate constants were consistent, and independent of which protein was immobilized and which biosensor was used.

Česky

Srovnání výsledků studia stejného neznámého afinitního páru protilátka-antigen použitím různých typů afinitních biosensorů.

Návaznosti

LC06030, projekt VaV

Název: Biomolekulární centrum

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Biomolekulární centrum

MSM0021622413, záměr

Název: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Proteiny v metabolismu a při interakci organismů s prostředím

Citovat

RICH, Rebecca L., Giuseppe A. PAPALIA, Petr SKLÁDAL, [from all world] [109 OTHER AUTHORS] a David G. MYSZKA. A global benchmark study using affinity-based biosensors. Analytica Chimica Acta. Amsterdam: Elsevier Science Publishers, 2009, roč. 386, č. 2, s. 194-216, 25 s. ISSN 0003-2670.

@article{842678,
   author = {Rich, Rebecca L. and Papalia, Giuseppe A. and Skládal, Petr and [109 other authors], [from all world] and Myszka, David G.},
   article_location = {Amsterdam},
   article_number = {2},
   keywords = {Biosensor; Antibody; Biacore},
   language = {eng},
   issn = {0003-2670},
   journal = {Analytica Chimica Acta},
   title = {A global benchmark study using affinity-based biosensors},
   url = {http://dx.doi.org/10.1016/j.ab.2008.11.021},
   volume = {386},
   year = {2009}
}

TY  - JOUR
ID  - 842678
AU  - Rich, Rebecca L. - Papalia, Giuseppe A. - Skládal, Petr - [109 other authors], [from all world] - Myszka, David G.
PY  - 2009
TI  - A global benchmark study using affinity-based biosensors
JF  - Analytica Chimica Acta
VL  - 386
IS  - 2
SP  - 194-216
EP  - 194-216
PB  - Elsevier Science Publishers
SN  - 00032670
KW  - Biosensor
KW  - Antibody
KW  - Biacore
UR  - http://dx.doi.org/10.1016/j.ab.2008.11.021
N2  - To explore the variability in biosensor studies, 150 participants from 20 countries were given the same protein samples and asked to determine kinetic rate constants for the interaction. We chose a protein system that was amenable to analysis using different biosensor platforms as well as by users of different expertise levels. The two proteins (a 50-kDa Fab and a 60-kDa glutathione S-transferase [GST] antigen) form a relatively high-affinity complex, so participants needed to optimize several experimental parameters, including ligand immobilization and regeneration conditions as well as analyte concentrations and injection/dissociation times. Although most participants collected binding responses that could be fit to yield kinetic parameters, the quality of a few data sets could have been improved by optimizing the assay design. Once these outliers were removed, the average reported affinity across the remaining panel of participants was 620 pM with a standard deviation of 980 pM. These results demonstrate that when this biosensor assay was designed and executed appropriately, the reported rate constants were consistent, and independent of which protein was immobilized and which biosensor was used.
ER  -

RICH, Rebecca L., Giuseppe A. PAPALIA, Petr SKLÁDAL, [from all world] [109 OTHER AUTHORS] a David G. MYSZKA. A global benchmark study using affinity-based biosensors. \textit{Analytica Chimica Acta}. Amsterdam: Elsevier Science Publishers, 2009, roč.~386, č.~2, s.~194-216, 25 s. ISSN~0003-2670.

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