MUTANT P21 PEPTIDES COULD ACT AS AN IMPROVED CYCLIN A INHIBITORS FOR CANCER THERAP Y (Record no. 11155)

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fixed length control field a
003 - CONTROL NUMBER IDENTIFIER
control field OSt
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20200211095310.0
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 200211b xxu||||| |||| 00| 0 eng d
040 ## - CATALOGING SOURCE
Original cataloging agency AIKTC-KRRC
Transcribing agency AIKTC-KRRC
100 ## - MAIN ENTRY--PERSONAL NAME
9 (RLIN) 12076
Author Agarwal, Tarun
245 ## - TITLE STATEMENT
Title MUTANT P21 PEPTIDES COULD ACT AS AN IMPROVED CYCLIN A INHIBITORS FOR CANCER THERAP Y
Remainder of title : AN IN SILICO VALIDATION
250 ## - EDITION STATEMENT
Volume, Issue number Vol.11(2)
260 ## - PUBLICATION, DISTRIBUTION, ETC.
Place of publication, distribution, etc. M P
Name of publisher, distributor, etc. Innovare Academic Sciences Pvt Ltd
Year 2019
300 ## - PHYSICAL DESCRIPTION
Pagination 59-64p.
520 ## - SUMMARY, ETC.
Summary, etc. Objective: <br/>The present study delineates <br/>the <br/>generation of mutant peptide library from a known anticancer peptide, p21 <br/>and <br/>in silico<br/> evaluation <br/>for<br/>their <br/>affinity towards cyclin<br/>. A substrate binding groove. <br/>Method<br/>s: <br/>Mutant <br/>peptide library <br/>was created based on their AntiCP<br/> score<br/> and was docked with cyclin A using ClusPro2.0 web server. The docked <br/>structures were further simulated into an aqueous environment using Gromacs 4.5.6. Visualization was<br/> performed using PyMol software and <br/>interaction analysis was done using Discovery Studio Visualizer 4.1 Client and LigPlot plus tool.<br/>Result<br/>s: <br/>A total of 57 mutant peptides were generate<br/>d; <br/>out of which only 3 namely, K3C <br/>(Lys3Cys)<br/>, K3F<br/> (Lys3Phe)<br/>, and K3W (<br/>Lys3Trp) <br/>had<br/> a <br/>greater<br/> affinity for cyclin A than <br/>WILD<br/> p21 peptide<br/> (HSKRRLIFS<br/>). Molecular dynamic s<br/>imulation studies showed that <br/>the <br/>peptides remained docked <br/>into the substrate binding groove throughout the run. Among all the peptides, K3C <br/>showed <br/>a <br/>significantly higher<br/> negative binding energy <br/>with <br/>cyclin A <br/>as<br/> compar<br/>ed<br/> to WILD. <br/>Conclusio<br/>n: <br/>The<br/> overall<br/> results<br/> suggested that <br/>K3C<br/> mutant peptide had ~30 % higher affinity towards cyclin A and thus, could further be explored <br/>for its anticancer potential. The study also <br/>provides<br/> an insight into the crucial interactions governing the recognition of substrate binding groove of <br/>cyclin A for<br/> the<br/> development <br/>of novel peptide<br/>-based<br/> anticancer therapeutics
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
9 (RLIN) 4639
Topical term or geographic name entry element PHARMACEUTICS
700 ## - ADDED ENTRY--PERSONAL NAME
9 (RLIN) 12077
Co-Author Annamalai, Nithyanan
773 0# - HOST ITEM ENTRY
Title International journal of pharmacy and pharmaceutical science
Place, publisher, and date of publication Bhopal Innovare Academic Sciences Pvt Ltd
International Standard Serial Number 2656-0097
856 ## - ELECTRONIC LOCATION AND ACCESS
URL https://innovareacademics.in/journals/index.php/ijpps/article/view/30577/19155
Link text Click here
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Koha item type Articles Abstract Database
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    Dewey Decimal Classification     School of Pharmacy School of Pharmacy Archieval Section 11/02/2020   2020889 11/02/2020 11/02/2020 Articles Abstract Database
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