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  1. Article ; Online: Identification of Potential ACE2-Derived Peptide Mimetics in SARS-CoV-2 Omicron Variant Therapeutics using Computational Approaches.

    Paul, Stanly / Nadendla, Swathi / Sobhia, M Elizabeth

    The journal of physical chemistry letters

    2022  Volume 13, Issue 32, Page(s) 7420–7428

    Abstract: The COVID-19 pandemic has become a global health challenge because of the emergence of distinct variants. Omicron, a new variant, is recognized as a variant of concern (VOC) by the World Health Organization (WHO) because of its higher mutations and ... ...

    Abstract The COVID-19 pandemic has become a global health challenge because of the emergence of distinct variants. Omicron, a new variant, is recognized as a variant of concern (VOC) by the World Health Organization (WHO) because of its higher mutations and accelerated human infection. The infection rate is strongly dependent on the binding rate of the receptor binding domain (RBD) against human angiotensin converting enzyme-2 (ACE2
    MeSH term(s) Angiotensin-Converting Enzyme 2 ; Biomimetic Materials/therapeutic use ; Humans ; Mutation ; Pandemics ; Peptides/metabolism ; Peptidyl-Dipeptidase A/chemistry ; Protein Binding ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus/chemistry ; COVID-19 Drug Treatment
    Chemical Substances Peptides ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; Peptidyl-Dipeptidase A (EC 3.4.15.1) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
    Language English
    Publishing date 2022-08-05
    Publishing country United States
    Document type Journal Article
    ISSN 1948-7185
    ISSN (online) 1948-7185
    DOI 10.1021/acs.jpclett.2c01155
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Design and development of potent h-ACE2 derived peptide mimetics in SARS-CoV-2 Omicron variant therapeutics

    Paul, Stanly M L / Nadendla, Swathi / Sobhia, Elizabeth M

    bioRxiv

    Abstract: The pandemic of COVID- 19 has become the global health challenge due to the emergence of new variants. The Receptor binding domain (RBD) of spike protein that makes direct interaction with ACE-2 has shown unique mutated residues in most of the variants ... ...

    Abstract The pandemic of COVID- 19 has become the global health challenge due to the emergence of new variants. The Receptor binding domain (RBD) of spike protein that makes direct interaction with ACE-2 has shown unique mutated residues in most of the variants of concern (VOC). Recently WHO declared the Omicron (B.1.1.529) as VOC considering it as a highly mutated variant which includes a total of 60 mutations out of which 15 mutations occurred in RBD region of SARS-CoV-2. Inhibition of Protein-protein (Omicron RBD-h-ACE2) interaction was already proved to inhibit the viral infection. In this study, by using molecular dynamic simulations efforts are made to explore the atomistic details of Omicron RBD-h-ACE2 interaction. Based on MD simulations, h-ACE2 motif is found to be interacting with omicron RBD domain. Interaction analysis had provided key residues interacting with Omicron-RBD that helped to extract h-ACE2 peptide. Here, rational design of the peptides that have resemblance with h-ACE2 is done and the peptide library is subjected for inhibition studies against Omicron-RBD. The current study helped to identify the significant peptides that can inhibit Omicron-RBD. Altogether the performed studies will provide an opportunity to develop potential therapeutic peptidomimetics effective against Omicron variant of SARS-CoV-2.
    Keywords covid19
    Language English
    Publishing date 2022-02-02
    Publisher Cold Spring Harbor Laboratory
    Document type Article ; Online
    DOI 10.1101/2022.02.01.478632
    Database COVID19

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  3. Article ; Online: Protein tyrosine phosphatase inhibitors: a patent review (2002 - 2011).

    Sobhia, Masilamani Elizabeth / Paul, Stanly / Shinde, Ranajit / Potluri, Mrudula / Gundam, Venkatesh / Kaur, Amandeep / Haokip, Thongtinlal

    Expert opinion on therapeutic patents

    2012  Volume 22, Issue 2, Page(s) 125–153

    Abstract: Introduction: The protein tyrosine phosphatases (PTPases or PTPs) are highly conserved phosphatases that regulate the tyrosine phosphorylation and consequently, the cellular functions. Protein tyrosine phosphorylation is the major post-translational ... ...

    Abstract Introduction: The protein tyrosine phosphatases (PTPases or PTPs) are highly conserved phosphatases that regulate the tyrosine phosphorylation and consequently, the cellular functions. Protein tyrosine phosphorylation is the major post-translational modification to regulate signal transduction in cells. PTPs control diverse processes such as focal adhesion dynamics, cell-cell adhesion, insulin signaling, cytoskeletal functions, synaptogenesis and neurite growth. The availability of numerous X-ray crystal structures of PTPs, along with their inhibitors, has provided the opportunity for the structure-based design of effective inhibitors having potential for the treatment of various disorders.
    Areas covered: The main focus of the present review is to get an insight into the most clinically relevant therapeutic PTP inhibitors published in patents over the past 10 years.
    Expert opinion: Several computational studies are being carried out to understand ligand binding modes, selectivity interactions and conformational changes during inhibitor binding. PTP inhibitors that are of current interest include quinolyl, cyclic alabenzimidazole, pyrazine, (ethynediyl)bis-benzene, pyridopyrimidine, triazolopyridine, cyclo propylphenyl phenyloxamides, oxindole and azoloarin derivatives. The development of allosteric site-directed PTP inhibitors may help in understanding the absorption and selectivity of PTP inhibitors.
    MeSH term(s) Animals ; Binding Sites ; Drug Design ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/therapeutic use ; Humans ; Legislation, Drug ; Models, Molecular ; Molecular Structure ; Molecular Targeted Therapy ; Patents as Topic ; Protein Conformation ; Protein Tyrosine Phosphatases/antagonists & inhibitors ; Protein Tyrosine Phosphatases/chemistry ; Protein Tyrosine Phosphatases/metabolism ; Signal Transduction/drug effects ; Structure-Activity Relationship
    Chemical Substances Enzyme Inhibitors ; Protein Tyrosine Phosphatases (EC 3.1.3.48)
    Language English
    Publishing date 2012-02
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1186201-4
    ISSN 1744-7674 ; 0962-2594 ; 1354-3776
    ISSN (online) 1744-7674
    ISSN 0962-2594 ; 1354-3776
    DOI 10.1517/13543776.2012.661414
    Database MEDical Literature Analysis and Retrieval System OnLINE

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