Novel binders derived from an albumin-binding domain scaffold targeting human prostate secretory protein 94 (PSP94)

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F15%3A00464077" target="_blank" >RIV/86652036:_____/15:00464077 - isvavai.cz</a>

Alternative codes found

RIV/61388971:_____/15:00464077

Result on the web

<a href="http://dx.doi.org/10.1007/s13238-015-0194-9" target="_blank" >http://dx.doi.org/10.1007/s13238-015-0194-9</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s13238-015-0194-9" target="_blank" >10.1007/s13238-015-0194-9</a>

Result language

angličtina

Original language name

Novel binders derived from an albumin-binding domain scaffold targeting human prostate secretory protein 94 (PSP94)

Original language description

Prostate secretory protein 94 (PSP94), a dominant protein of human seminal plasma known also as β-microseminoprotein (MSMB), has recently been shown to decrease serum level expression during prostate cancer (PC) progression and indicated as a novel promising serum oncomarker with a predictive role in PC diagnosis. In this work we aimed to generate a novel class of protein binders targeted to human PSP94 that can serve as robust capture proteins for improved PC diagnostics. We used high-complex combinatorial library derived from an albumin-binding domain (ABD) scaffold of streptococcal protein G with a theoretical complexity up to 2 x 1014 protein variants and ribosome display to generate a plasmid library of selected variants. Individual clones were characterized by binding of ABD-derived proteins to recombinant PSP94 and sequentially compared and characterized. Collection of 35 ABD-derived protein binders of human PSP94 (called PAB binders), corresponding to 29 different sequence variants, was generated. PAB036, PAB046 and PAB050 were identified as the most promising binding candidates characterized in ELISA. Their stability was verified by thermal shift assay and the binding affinity to the recombinant PSP94 was estimated by microscale thermophoresis. These PAB variants bound to PSP94-expressing human LNCaP prostate carcinoma cells and this binding was dose-dependently inhibited by recombinant PSP94. Thus, we generated a unique collection of novel proteins binders of human PSP94 that can serve as a valuable tool for human PSP94 detection and, with a further modification, as high-affinity capture proteins for the development of biosensors for more complex PC diagnostics.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EB - Genetics and molecular biology

OECD FORD branch

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Project

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Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2015

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Protein & Cell

ISSN

1674-800X

e-ISSN

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Volume of the periodical

6

Issue of the periodical within the volume

10

Country of publishing house

CN - CHINA

Number of pages

6

Pages from-to

774-779

UT code for WoS article

000362653100010

EID of the result in the Scopus database

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