• Je něco špatně v tomto záznamu ?

Selective chromogenic and fluorogenic peptide substrates for the assay of cysteine peptidases in complex mixtures

TA. Semashko, EA. Vorotnikova, VF. Sharikova, KS. Vinokurov, YA. Smirnova, YE. Dunaevsky, MA. Belozersky, B. Oppert, EN. Elpidina, IY. Filippova,

. 2014 ; 449 (-) : 179-87.

Jazyk angličtina Země Spojené státy americké

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc15008419

This study describes the design, synthesis, and use of selective peptide substrates for cysteine peptidases of the C1 papain family, important in many biological processes. The structure of the newly synthesized substrates is Glp-Xaa-Ala-Y (where Glp=pyroglutamyl; Xaa=Phe or Val; and Y=pNA [p-nitroanilide], AMC [4-amino-7-methylcoumaride], or AFC [4-amino-7-trifluoromethyl-coumaride]). Substrates were synthesized enzymatically to guarantee selectivity of the reaction and optical purity of the target compounds, simplifying the scheme of synthesis and isolation of products. The hydrolysis of the synthesized substrates was evaluated by C1 cysteine peptidases from different organisms and with different functions, including plant enzymes papain, bromelain, ficin, and mammalian lysosomal cathepsins B and L. The new substrates were selective for C1 cysteine peptidases and were not hydrolyzed by serine, aspartic, or metallo peptidases. We demonstrated an application of the selectivity of the synthesized substrates during the chromatographic separation of a multicomponent set of digestive peptidases from a beetle, Tenebrio molitor. Used in combination with the cysteine peptidase inhibitor E-64, these substrates were able to differentiate cysteine peptidases from peptidases of other classes in midgut extracts from T. molitor larvae and larvae of the genus Tribolium; thus, they are useful in the analysis of complex mixtures containing peptidases from different classes.

Citace poskytuje Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc15008419
003      
CZ-PrNML
005      
20150310123252.0
007      
ta
008      
150306s2014 xxu f 000 0|eng||
009      
AR
024    7_
$a 10.1016/j.ab.2013.12.032 $2 doi
035    __
$a (PubMed)24388866
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a xxu
100    1_
$a Semashko, Tatiana A $u Department of Chemistry, Moscow State University, Moscow 119992, Russia.
245    10
$a Selective chromogenic and fluorogenic peptide substrates for the assay of cysteine peptidases in complex mixtures / $c TA. Semashko, EA. Vorotnikova, VF. Sharikova, KS. Vinokurov, YA. Smirnova, YE. Dunaevsky, MA. Belozersky, B. Oppert, EN. Elpidina, IY. Filippova,
520    9_
$a This study describes the design, synthesis, and use of selective peptide substrates for cysteine peptidases of the C1 papain family, important in many biological processes. The structure of the newly synthesized substrates is Glp-Xaa-Ala-Y (where Glp=pyroglutamyl; Xaa=Phe or Val; and Y=pNA [p-nitroanilide], AMC [4-amino-7-methylcoumaride], or AFC [4-amino-7-trifluoromethyl-coumaride]). Substrates were synthesized enzymatically to guarantee selectivity of the reaction and optical purity of the target compounds, simplifying the scheme of synthesis and isolation of products. The hydrolysis of the synthesized substrates was evaluated by C1 cysteine peptidases from different organisms and with different functions, including plant enzymes papain, bromelain, ficin, and mammalian lysosomal cathepsins B and L. The new substrates were selective for C1 cysteine peptidases and were not hydrolyzed by serine, aspartic, or metallo peptidases. We demonstrated an application of the selectivity of the synthesized substrates during the chromatographic separation of a multicomponent set of digestive peptidases from a beetle, Tenebrio molitor. Used in combination with the cysteine peptidase inhibitor E-64, these substrates were able to differentiate cysteine peptidases from peptidases of other classes in midgut extracts from T. molitor larvae and larvae of the genus Tribolium; thus, they are useful in the analysis of complex mixtures containing peptidases from different classes.
650    _2
$a zvířata $7 D000818
650    _2
$a cysteinové proteasy $x izolace a purifikace $x metabolismus $7 D057056
650    _2
$a enzymatické testy $x metody $7 D057075
650    _2
$a fluorescenční barviva $x analýza $x metabolismus $7 D005456
650    _2
$a hydrolýza $7 D006868
650    _2
$a molekulární modely $7 D008958
650    _2
$a peptidy $x chemie $x metabolismus $7 D010455
650    _2
$a substrátová specifita $7 D013379
650    _2
$a Tenebrio $x enzymologie $x metabolismus $7 D013712
655    _2
$a časopisecké články $7 D016428
655    _2
$a práce podpořená grantem $7 D013485
700    1_
$a Vorotnikova, Elena A $u Faculty of Bioengineering and Bioinformatics, Moscow State University, Moscow 119992, Russia.
700    1_
$a Sharikova, Valeriya F $u Department of Chemistry, Moscow State University, Moscow 119992, Russia.
700    1_
$a Vinokurov, Konstantin S $u Entomological Institute, Biology Centre AV ĈR, Ĉeské Budĕjovice CZ-37005, Czech Republic.
700    1_
$a Smirnova, Yulia A $u A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia.
700    1_
$a Dunaevsky, Yakov E $u A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia.
700    1_
$a Belozersky, Mikhail A $u A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia.
700    1_
$a Oppert, Brenda $u USDA Agricultural Research Service, Center for Grain and Animal Health Research, Manhattan, KS 66502, USA. Electronic address: brenda.oppert@ars.usda.gov.
700    1_
$a Elpidina, Elena N $u A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119992, Russia.
700    1_
$a Filippova, Irina Y $u Department of Chemistry, Moscow State University, Moscow 119992, Russia.
773    0_
$w MED00000335 $t Analytical biochemistry $x 1096-0309 $g Roč. 449, č. - (2014), s. 179-87
856    41
$u https://pubmed.ncbi.nlm.nih.gov/24388866 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y a $z 0
990    __
$a 20150306 $b ABA008
991    __
$a 20150310123529 $b ABA008
999    __
$a ok $b bmc $g 1065692 $s 891219
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2014 $b 449 $c - $d 179-87 $i 1096-0309 $m Analytical biochemistry $n Anal Biochem $x MED00000335
LZP    __
$a Pubmed-20150306

Najít záznam

Citační ukazatele

Možnosti archivace