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  1. Article ; Online: Chemoselective N-Acylation of Amines with Acylsilanes under Aqueous Acidic Conditions.

    Tian, Jing / Li, Wei / Deng, Xingwang / Lakshminarayanan, Rajamani / Srinivasan, Rajavel

    Organic letters

    2023  Volume 25, Issue 31, Page(s) 5740–5744

    Abstract: We report a facile method for forming amide bonds between acylsilanes and a wide range of amines in the presence of a mild chlorinating agent under aqueous acidic conditions. The reaction is highly chemoselective, as exemplified by the late-stage ... ...

    Abstract We report a facile method for forming amide bonds between acylsilanes and a wide range of amines in the presence of a mild chlorinating agent under aqueous acidic conditions. The reaction is highly chemoselective, as exemplified by the late-stage modification of a panel of approved drugs and natural products containing reactive functionalities.
    Language English
    Publishing date 2023-07-29
    Publishing country United States
    Document type Journal Article
    ISSN 1523-7052
    ISSN (online) 1523-7052
    DOI 10.1021/acs.orglett.3c01911
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Biofilm formation and virulence potential of carbapenem-resistant Pseudomonas aeruginosa.

    Ma, Yeping / Aung, Thet Tun / Lakshminarayanan, Rajamani / Chua, Song Lin

    The Lancet. Microbe

    2023  Volume 4, Issue 7, Page(s) e489

    MeSH term(s) Virulence ; Pseudomonas aeruginosa ; Anti-Bacterial Agents/pharmacology ; Anti-Bacterial Agents/therapeutic use ; Carbapenems/pharmacology ; Biofilms
    Chemical Substances Anti-Bacterial Agents ; Carbapenems
    Language English
    Publishing date 2023-04-24
    Publishing country England
    Document type Letter ; Research Support, Non-U.S. Gov't ; Comment
    ISSN 2666-5247
    ISSN (online) 2666-5247
    DOI 10.1016/S2666-5247(23)00097-6
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  3. Article: Correction: Peguda et al. The Activity of Polyhomoarginine against

    Peguda, Hari Kumar / Lakshminarayanan, Rajamani / Carnt, Nicole A / Gu, Zi / Willcox, Mark D P

    Biology

    2023  Volume 12, Issue 3

    Abstract: In the original publication [ ... ]. ...

    Abstract In the original publication [...].
    Language English
    Publishing date 2023-03-20
    Publishing country Switzerland
    Document type Published Erratum
    ZDB-ID 2661517-4
    ISSN 2079-7737
    ISSN 2079-7737
    DOI 10.3390/biology12030470
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  4. Article ; Online: Correction

    Hari Kumar Peguda / Rajamani Lakshminarayanan / Nicole A. Carnt / Zi Gu / Mark D. P. Willcox

    Biology, Vol 12, Iss 470, p

    Peguda et al. The Activity of Polyhomoarginine against Acanthamoeba castellanii . Biology 2022, 11 , 1726

    2023  Volume 470

    Abstract: In the original publication [.] ...

    Abstract In the original publication [.]
    Keywords n/a ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2023-03-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article: The Activity of Polyhomoarginine against

    Peguda, Hari Kumar / Lakshminarayanan, Rajamani / Carnt, Nicole A / Gu, Zi / Willcox, Mark D P

    Biology

    2022  Volume 11, Issue 12

    Abstract: Arginine-rich peptides can have broad-spectrum anti-bacterial and anti-fungal activities. Polyhomoarginine consists of highly cationic residues which can act on the negatively charged microbial cell membranes. Acanthamoeba is a free-living protozoan ... ...

    Abstract Arginine-rich peptides can have broad-spectrum anti-bacterial and anti-fungal activities. Polyhomoarginine consists of highly cationic residues which can act on the negatively charged microbial cell membranes. Acanthamoeba is a free-living protozoan known to cause a rare corneal infection which is difficult to diagnose and treat. This study evaluated the activity of the polyhomoarginines against Acanthamoeba castellanii. Acanthamoeba amoebicidal, amoebistatic, encystation and excystment assays were performed using protocols described in the literature. The activity of polyhomoarginines (PHAs) of different lengths (10 to 400 residues) was measured against the trophozoites and cysts of Acanthamoeba castellanii ATCC30868 in concentrations ranging from 0.93 μM to 15 μM. Data were represented as mean ± SE and analysed using one-way ANOVA. Overall, PHAs demonstrated good anti-acanthamoeba activity against both trophozoites and cysts. PHA 30 reduced the number of viable trophozoites by 99%, inhibited the formation of cysts by 96% and the emergence of trophozoites from cysts by 67% at 3.75 μM. PHA 10 was similarly active, but at a slightly higher concentration of 15 μM, reducing the numbers of viable trophozoites by 98%, inhibiting cyst formation by 84% and preventing the emergence of trophozoites from cysts by 99%. At their greatest anti-amoeba concentrations, PHA 10 gave only 8% haemolysis at 15 μM while PHA 30 gave <40 % haemolysis at 3.75 μM. Polyhomoarginine 10 showed excellent anti-amoebic activity against both forms of Acanthamoeba castellanii and was non-toxic at its most active concentrations. This implies that polyhomoarginines can be developed into a potential therapeutic agent for Acanthamoeba keratitis. However, there is a need to carry out further pre-clinical and then in vivo experiments in the AK animal model.
    Language English
    Publishing date 2022-11-28
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2661517-4
    ISSN 2079-7737
    ISSN 2079-7737
    DOI 10.3390/biology11121726
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Host Defense Peptides at the Ocular Surface: Roles in Health and Major Diseases, and Therapeutic Potentials.

    Ting, Darren Shu Jeng / Mohammed, Imran / Lakshminarayanan, Rajamani / Beuerman, Roger W / Dua, Harminder S

    Frontiers in medicine

    2022  Volume 9, Page(s) 835843

    Abstract: Sight is arguably the most important sense in human. Being constantly exposed to the environmental stress, irritants and pathogens, the ocular surface - a specialized functional and anatomical unit composed of tear film, conjunctival and corneal ... ...

    Abstract Sight is arguably the most important sense in human. Being constantly exposed to the environmental stress, irritants and pathogens, the ocular surface - a specialized functional and anatomical unit composed of tear film, conjunctival and corneal epithelium, lacrimal glands, meibomian glands, and nasolacrimal drainage apparatus - serves as a crucial front-line defense of the eye. Host defense peptides (HDPs), also known as antimicrobial peptides, are evolutionarily conserved molecular components of innate immunity that are found in all classes of life. Since the first discovery of lysozyme in 1922, a wide range of HDPs have been identified at the ocular surface. In addition to their antimicrobial activity, HDPs are increasingly recognized for their wide array of biological functions, including anti-biofilm, immunomodulation, wound healing, and anti-cancer properties. In this review, we provide an updated review on: (1) spectrum and expression of HDPs at the ocular surface; (2) participation of HDPs in ocular surface diseases/conditions such as infectious keratitis, conjunctivitis, dry eye disease, keratoconus, allergic eye disease, rosacea keratitis, and post-ocular surgery; (3) HDPs that are currently in the development pipeline for treatment of ocular diseases and infections; and (4) future potential of HDP-based clinical pharmacotherapy for ocular diseases.
    Language English
    Publishing date 2022-06-16
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2775999-4
    ISSN 2296-858X
    ISSN 2296-858X
    DOI 10.3389/fmed.2022.835843
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  7. Article ; Online: Host Defense Peptides at the Ocular Surface

    Darren Shu Jeng Ting / Imran Mohammed / Rajamani Lakshminarayanan / Roger W. Beuerman / Harminder S. Dua

    Frontiers in Medicine, Vol

    Roles in Health and Major Diseases, and Therapeutic Potentials

    2022  Volume 9

    Abstract: Sight is arguably the most important sense in human. Being constantly exposed to the environmental stress, irritants and pathogens, the ocular surface – a specialized functional and anatomical unit composed of tear film, conjunctival and corneal ... ...

    Abstract Sight is arguably the most important sense in human. Being constantly exposed to the environmental stress, irritants and pathogens, the ocular surface – a specialized functional and anatomical unit composed of tear film, conjunctival and corneal epithelium, lacrimal glands, meibomian glands, and nasolacrimal drainage apparatus – serves as a crucial front-line defense of the eye. Host defense peptides (HDPs), also known as antimicrobial peptides, are evolutionarily conserved molecular components of innate immunity that are found in all classes of life. Since the first discovery of lysozyme in 1922, a wide range of HDPs have been identified at the ocular surface. In addition to their antimicrobial activity, HDPs are increasingly recognized for their wide array of biological functions, including anti-biofilm, immunomodulation, wound healing, and anti-cancer properties. In this review, we provide an updated review on: (1) spectrum and expression of HDPs at the ocular surface; (2) participation of HDPs in ocular surface diseases/conditions such as infectious keratitis, conjunctivitis, dry eye disease, keratoconus, allergic eye disease, rosacea keratitis, and post-ocular surgery; (3) HDPs that are currently in the development pipeline for treatment of ocular diseases and infections; and (4) future potential of HDP-based clinical pharmacotherapy for ocular diseases.
    Keywords antimicrobial peptide ; cathelicidin ; defensin ; dry eye ; host defense peptide ; infection ; Medicine (General) ; R5-920
    Subject code 610
    Language English
    Publishing date 2022-06-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: Enzyme-Linked Immunosorbent Assay for T-Cell Dependent Immunogenicity Assessment of Therapeutic Peptides.

    Chalasani, Madhavi Latha Somaraju / Lakshminarayanan, Rajamani / Verma, Navin Kumar

    Methods in molecular biology (Clifton, N.J.)

    2019  Volume 1930, Page(s) 129–138

    Abstract: Immunogenicity assessment of therapeutic peptides, proteins, oligonucleotides, and hybrid molecules, such as nucleopeptides, is a major aspect in understanding their safety and efficacy. Both T-cell independent and dependent immune reactions contribute ... ...

    Abstract Immunogenicity assessment of therapeutic peptides, proteins, oligonucleotides, and hybrid molecules, such as nucleopeptides, is a major aspect in understanding their safety and efficacy. Both T-cell independent and dependent immune reactions contribute to an immunogenic response against antigen, including secretion of cytokines and production of an antigen-specific antibody. Various assays exist for detecting and quantifying such immunogenic responses by human T-cells ex vivo or in mouse serum, which primarily include enzyme-linked immunosorbent assay (ELISA, direct and indirect), flow-cytometry and surface plasmon resonance (SPR). ELISA is a popular choice due to its robustness, reliability, sensitivity, ease of automation, and the requirement of simple equipment commonly available in most molecular biology and biochemistry laboratories. The chapter describes the detailed protocol of cytokine analysis by an ELISA method and highlights few crucial steps to be considered while performing the assay for successful immunogenicity studies.
    MeSH term(s) Animals ; Antibodies, Monoclonal/immunology ; Cytokines/immunology ; Cytokines/metabolism ; Enzyme-Linked Immunosorbent Assay/methods ; Humans ; Immunity, Cellular/immunology ; Peptide Fragments/immunology ; Peptide Fragments/therapeutic use ; Serum/metabolism ; T-Lymphocytes/immunology ; T-Lymphocytes/metabolism
    Chemical Substances Antibodies, Monoclonal ; Cytokines ; Peptide Fragments
    Language English
    Publishing date 2019-01-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-9036-8_16
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: The Activity of Polyhomoarginine against Acanthamoeba castellanii

    Peguda, Hari Kumar / Lakshminarayanan, Rajamani / Carnt, Nicole A. / Gu, Zi / Willcox, Mark D. P.

    Biology (Basel). 2022 Nov. 28, v. 11, no. 12

    2022  

    Abstract: Arginine-rich peptides can have broad-spectrum anti-bacterial and anti-fungal activities. Polyhomoarginine consists of highly cationic residues which can act on the negatively charged microbial cell membranes. Acanthamoeba is a free-living protozoan ... ...

    Abstract Arginine-rich peptides can have broad-spectrum anti-bacterial and anti-fungal activities. Polyhomoarginine consists of highly cationic residues which can act on the negatively charged microbial cell membranes. Acanthamoeba is a free-living protozoan known to cause a rare corneal infection which is difficult to diagnose and treat. This study evaluated the activity of the polyhomoarginines against Acanthamoeba castellanii. Acanthamoeba amoebicidal, amoebistatic, encystation and excystment assays were performed using protocols described in the literature. The activity of polyhomoarginines (PHAs) of different lengths (10 to 400 residues) was measured against the trophozoites and cysts of Acanthamoeba castellanii ATCC30868 in concentrations ranging from 0.93 μM to 15 μM. Data were represented as mean ± SE and analysed using one-way ANOVA. Overall, PHAs demonstrated good anti-acanthamoeba activity against both trophozoites and cysts. PHA 30 reduced the number of viable trophozoites by 99%, inhibited the formation of cysts by 96% and the emergence of trophozoites from cysts by 67% at 3.75 μM. PHA 10 was similarly active, but at a slightly higher concentration of 15 μM, reducing the numbers of viable trophozoites by 98%, inhibiting cyst formation by 84% and preventing the emergence of trophozoites from cysts by 99%. At their greatest anti-amoeba concentrations, PHA 10 gave only 8% haemolysis at 15 μM while PHA 30 gave <40 % haemolysis at 3.75 μM. Polyhomoarginine 10 showed excellent anti-amoebic activity against both forms of Acanthamoeba castellanii and was non-toxic at its most active concentrations. This implies that polyhomoarginines can be developed into a potential therapeutic agent for Acanthamoeba keratitis. However, there is a need to carry out further pre-clinical and then in vivo experiments in the AK animal model.
    Keywords Acanthamoeba castellanii ; animal models ; encystment ; excystation ; hemolysis ; keratitis ; peptides ; therapeutics ; trophozoites
    Language English
    Dates of publication 2022-1128
    Publishing place Multidisciplinary Digital Publishing Institute
    Document type Article ; Online
    ZDB-ID 2661517-4
    ISSN 2079-7737
    ISSN 2079-7737
    DOI 10.3390/biology11121726
    Database NAL-Catalogue (AGRICOLA)

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  10. Article ; Online: Thermostability enhancement of polyethylene terephthalate degrading PETase using self- and nonself-ligating protein scaffolding approaches.

    Sana, Barindra / Ding, Ke / Siau, Jia Wei / Pasula, Rupali Reddy / Chee, Sharon / Kharel, Sharad / Lena, Jean-Baptise Henri / Goh, Eunice / Rajamani, Lakshminarayanan / Lam, Yeng Ming / Lim, Sierin / Ghadessy, John F

    Biotechnology and bioengineering

    2023  Volume 120, Issue 11, Page(s) 3200–3209

    Abstract: Polyethylene terephthalate (PET) hydrolase enzymes show promise for enzymatic PET degradation and green recycling of single-use PET vessels representing a major source of global pollution. Their full potential can be unlocked with enzyme engineering to ... ...

    Abstract Polyethylene terephthalate (PET) hydrolase enzymes show promise for enzymatic PET degradation and green recycling of single-use PET vessels representing a major source of global pollution. Their full potential can be unlocked with enzyme engineering to render activities on recalcitrant PET substrates commensurate with cost-effective recycling at scale. Thermostability is a highly desirable property in industrial enzymes, often imparting increased robustness and significantly reducing quantities required. To date, most engineered PET hydrolases show improved thermostability over their parental enzymes. Here, we report engineered thermostable variants of Ideonella sakaiensis PET hydrolase enzyme (IsPETase) developed using two scaffolding strategies. The first employed SpyCatcher-SpyTag technology to covalently cyclize IsPETase, resulting in increased thermostability that was concomitant with reduced turnover of PET substrates compared to native IsPETase. The second approach using a GFP-nanobody fusion protein (vGFP) as a scaffold yielded a construct with a melting temperature of 80°C. This was further increased to 85°C when a thermostable PETase variant (FAST PETase) was scaffolded into vGFP, the highest reported so far for an engineered PET hydrolase derived from IsPETase. Thermostability enhancement using the vGFP scaffold did not compromise activity on PET compared to IsPETase. These contrasting results highlight potential topological and dynamic constraints imposed by scaffold choice as determinants of enzyme activity.
    Language English
    Publishing date 2023-08-09
    Publishing country United States
    Document type Journal Article
    ZDB-ID 280318-5
    ISSN 1097-0290 ; 0006-3592
    ISSN (online) 1097-0290
    ISSN 0006-3592
    DOI 10.1002/bit.28523
    Database MEDical Literature Analysis and Retrieval System OnLINE

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