Change of the Protein p53 Electrochemical Signal According to
its Structural Form - Quick and Sensitive Distinguishing of
Native, Denatured, and Aggregated Form of the

J 2006

Change of the Protein p53 Electrochemical Signal According to its Structural Form - Quick and Sensitive Distinguishing of Native, Denatured, and Aggregated Form of the "Guardian of the Genome"

POTĚŠIL, David, Radka MIKELOVÁ, Vojtěch ADAM, René KIZEK, Richard PRŮŠA et. al.

Základní údaje

Originální název

Change of the Protein p53 Electrochemical Signal According to its Structural Form - Quick and Sensitive Distinguishing of Native, Denatured, and Aggregated Form of the "Guardian of the Genome"

Název česky

Změna elektrochemického signálu proteinu P53 podle jeho strukturní formy - rychlé a citlivé rozlišení nativní, denaturované a agregované formy -Strážce genomu.

Autoři

POTĚŠIL, David (203 Česká republika), Radka MIKELOVÁ (203 Česká republika, garant), Vojtěch ADAM (203 Česká republika), René KIZEK (203 Česká republika) a Richard PRŮŠA (203 Česká republika)

Vydání

The Protein Journal, 2006, 1572-3887

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10405 Electrochemistry

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 0.962

Kód RIV

RIV/00216224:14310/06:00015697

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000237826800003

Klíčová slova anglicky

p53; .ow injection analysis; electrochemical detection; structural changes; carbon

Štítky

.ow injection analysis, Carbon, electrochemical detection, p53, structural changes

Změněno: 26. 5. 2006 09:35, Ing. Radka Mikelová, Ph.D.

Anotace

ORIG CZ

V originále

Presence of mutated and/or structurally modi.ed (e.g., denatured, aggregated) protein p53 form is associated with several disorders such as Alzheimers disease, Parkinsons disease, prion diseases, and many types of tumours. The aim of this work was to distinguish native, denatured and aggregated form of full-length p53 by .ow injection analysis coupled with electrochemical detector (FIA-ED). Firstly FIA-ED method used for protein native form determination was optimized (detection limit 45.8 amol per 5 ll injection; 3_S/N). In addition the technique was applied to identify p53 structural forms (denatured and aggregated). It was found out that denatured form provides about three times higher electrochemical response (protein structure unfolding, approach of more electroactive centers - aminoacid residues - towards electrode surface) in comparison with native form. On the other hand, aggregated form o.ers lower response (steric eclipse of electroactive protein parts) when compared with the signal of native form. The obtained data show that we are not only able to sensitively determine native, denatured, and aggregated structural forms of p53 protein but also to distinguish them.

Česky

Změna elektrochemického signálu proteinu P53 podle jeho strukturní formy - rychlé a citlivé rozlišení nativní, denaturované a agregované formy -Strážce genomu.

Návaznosti

GP525/04/P132, projekt VaV

Název: Studium obranných mechanismů rostlin při stresu způsobeném těžkými kovy

Citovat

POTĚŠIL, David, Radka MIKELOVÁ, Vojtěch ADAM, René KIZEK a Richard PRŮŠA. Change of the Protein p53 Electrochemical Signal According to its Structural Form - Quick and Sensitive Distinguishing of Native, Denatured, and Aggregated Form of the "Guardian of the Genome". The Protein Journal. 2006, roč. 25, č. 1, s. 23-32. ISSN 1572-3887.

@article{636131,
   author = {Potěšil, David and Mikelová, Radka and Adam, Vojtěch and Kizek, René and Průša, Richard},
   article_number = {1},
   keywords = {p53; .ow injection analysis; electrochemical detection; structural changes; carbon},
   language = {eng},
   issn = {1572-3887},
   journal = {The Protein Journal},
   title = {Change of the Protein p53 Electrochemical Signal According to its Structural Form - Quick and Sensitive Distinguishing of Native, Denatured, and Aggregated Form of the "Guardian of the Genome"},
   volume = {25},
   year = {2006}
}

TY  - JOUR
ID  - 636131
AU  - Potěšil, David - Mikelová, Radka - Adam, Vojtěch - Kizek, René - Průša, Richard
PY  - 2006
TI  - Change of the Protein p53 Electrochemical Signal According to its Structural Form - Quick and Sensitive Distinguishing of Native, Denatured, and Aggregated Form of the "Guardian of the Genome"
JF  - The Protein Journal
VL  - 25
IS  - 1
SP  - 23-32
EP  - 23-32
SN  - 15723887
KW  - p53
KW  - .ow injection analysis
KW  - electrochemical detection
KW  - structural changes
KW  - carbon
N2  - Presence of mutated and/or structurally modi.ed (e.g., denatured, aggregated) protein p53 form is associated with several disorders such as Alzheimers disease, Parkinsons disease, prion diseases, and many types of tumours. The aim of this work was to distinguish native, denatured and aggregated form of full-length p53 by .ow injection analysis coupled with electrochemical detector (FIA-ED). Firstly FIA-ED method used for protein native form determination was optimized (detection limit 45.8 amol per 5 ll injection; 3_S/N). In addition the technique was applied to identify p53 structural forms (denatured and aggregated). It was found out that denatured form provides about three times higher electrochemical response (protein structure unfolding, approach of more electroactive centers - aminoacid residues - towards electrode surface) in comparison with native form. On the other hand, aggregated form o.ers lower response (steric eclipse of electroactive protein parts) when compared with the signal of native form. The obtained data show that we are not only able to sensitively determine native, denatured, and aggregated structural forms of p53 protein but also to distinguish them.
ER  -

POTĚŠIL, David, Radka MIKELOVÁ, Vojtěch ADAM, René KIZEK a Richard PRŮŠA. Change of the Protein p53 Electrochemical Signal According to its Structural Form - Quick and Sensitive Distinguishing of Native, Denatured, and Aggregated Form of the ''Guardian of the Genome''. \textit{The Protein Journal}. 2006, roč.~25, č.~1, s.~23-32. ISSN~1572-3887.

Podrobný výpis o publikaci