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137 results on '"Patramanon, Rina"'

9. Revolutionizing elderly care: Building a healthier aging society through innovative long‐term care systems and assessing the long‐term care acceptance model.

Author

Chokphukhiao, Chaturapron, Tun, Wonn Shweyi Thet, Masa, Sakaowrat, Chaiayuth, Somporn, Loeiyood, Jugsun, Pongskul, Cholatip, and Patramanon, Rina

Subjects
ELDER care, LONG-term health care, QUESTIONNAIRES, MULTIPLE regression analysis, CAREGIVERS, LABOR demand, MEDICAL needs assessment, ACTIVE aging, EMPLOYEES' workload
Abstract

Aim: With a growing elderly population, the demand for caregivers is increasing in Khon Kaen, Thailand, with approximately 17 000 elderly residents. This growing number of older people and a shortage of caregivers could overload the healthcare system. Methods: The present study involved 129 healthcare volunteers (caregivers for questionnaires study) and the collection of health data from 290 elderly residents from northeastern Thailand. After training, the volunteers assessed its usefulness through questionnaires. Tool reliability and statistical hypotheses were tested using stratified regression analysis (hierarchical regression) and multiple regression. Results: The relative mean scores of perceived usefulness, perceived ease of use, attitude toward usage and behavioral intention to use technology were 4.51, 4.29, 4.44 and 4.41, respectively. In addition, perceived usefulness and user attitudes positively affected volunteers' willingness to use the system. Conclusion: The study was developed from the awareness of enhancing community quality and ecosystem through a long‐term care system application. Analyzing external factors can enhance technology's future effectiveness. Geriatr Gerontol Int 2024; 24: 477–485. [ABSTRACT FROM AUTHOR]

Published
2024
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11. Unveiling the Potent Antiviral and Antioxidant Activities of an Aqueous Extract from Caesalpinia mimosoides Lamk: Cheminformatics and Molecular Docking Approaches

Author

Klamrak, Anuwatchakij, primary, Nabnueangsap, Jaran, additional, Narkpuk, Jaraspim, additional, Saengkun, Yutthakan, additional, Janpan, Piyapon, additional, Nopkuesuk, Napapuch, additional, Chaveerach, Arunrat, additional, Teeravechyan, Samaporn, additional, Rahman, Shaikh Shahinur, additional, Dobutr, Theerawat, additional, Sitthiwong, Poramet, additional, Maraming, Pornsuda, additional, Nualkaew, Natsajee, additional, Jangpromma, Nisachon, additional, Patramanon, Rina, additional, Daduang, Sakda, additional, and Daduang, Jureerut, additional

Published
2023
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12. The synergistic action of silver nanoparticles and ceftazidime against antibiotic-resistant Burkholderia pseudomallei: a modifying treatment

Author

Tun, Wonn Shweyi Thet, primary, Hongsing, Nuttaya, additional, Sirithongsuk, Pawinee, additional, Nasompak, Sawinee, additional, Daduang, Sakda, additional, Klaynongsruang, Sompong, additional, Taweechaisupapong, Suwimol, additional, Chareonsudjai, Sorujsiri, additional, Prangkio, Panchika, additional, Kosolwattana, Suppanat, additional, and Patramanon, Rina, additional

Published
2023
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14. A Shear‐Thinning, Self‐Healing, Dual‐Cross Linked Hydrogel Based on Gelatin/Vanillin/Fe3+/AGP‐AgNPs: Synthesis, Antibacterial, and Wound‐Healing Assessment

Author

Talodthaisong, Chanon, primary, Patramanon, Rina, additional, Thammawithan, Saengrawee, additional, Lapmanee, Sarawut, additional, Maikaeo, Lamai, additional, Sricharoen, Phitchan, additional, Khongkow, Mattaka, additional, Namdee, Katawut, additional, Jantimaporn, Angkana, additional, Kayunkid, Navaphun, additional, Hutchison, James A., additional, and Kulchat, Sirinan, additional

Published
2023
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15. Unveiling the Potent Antiviral and Antioxidant Activities of an Aqueous Extract from Caesalpinia mimosoides Lamk: Cheminformatics and Molecular Docking Approaches.

Author

Klamrak, Anuwatchakij, Nabnueangsap, Jaran, Narkpuk, Jaraspim, Saengkun, Yutthakan, Janpan, Piyapon, Nopkuesuk, Napapuch, Chaveerach, Arunrat, Teeravechyan, Samaporn, Rahman, Shaikh Shahinur, Dobutr, Theerawat, Sitthiwong, Poramet, Maraming, Pornsuda, Nualkaew, Natsajee, Jangpromma, Nisachon, Patramanon, Rina, Daduang, Sakda, and Daduang, Jureerut

Subjects
MOLECULAR docking, CAESALPINIA, CHEMINFORMATICS, GALLIC acid, PLANT extracts, QUINIC acid, ANTIVIRAL agents
Abstract

Our group previously demonstrated that Caesalpinia mimosoides Lamk exhibits many profound biological properties, including anticancer, antibacterial, and antioxidant activities. However, its antiviral activity has not yet been investigated. Here, the aqueous extract of C. mimosoides was prepared from the aerial parts (leaves, stalks, and trunks) to see whether it exerts anti-influenza (H1N1) effects and to reduce the organic solvents consumed during extraction, making it a desirable approach for the large-scale production for medical uses. Our plant extract was quantified to contain 7 g of gallic acid (GA) per 100 g of a dry sample, as determined using HPLC analysis. It also exerts potent antioxidant activities comparable to those of authentic GA. According to untargeted metabolomics (UPLC-ESI(-)-QTOF-MS/MS) with the aid of cheminformatics tools (MetFrag (version 2.1), SIRIUS (version 5.8.3), CSI:FingerID (version 4.8), and CANOPUS), the major metabolite was best annotated as "gallic acid", phenolics (e.g., quinic acid, shikimic acid, and protocatechuic acid), sugar derivatives, and dicarboxylic acids were deduced from this plant species for the first time. The aqueous plant extract efficiently inhibited an influenza A (H1N1) virus infection of MDCK cells with an IC50 of 5.14 µg/mL. Of equal importance, hemolytic activity was absent for this plant extract, signifying its applicability as a safe antiviral agent. Molecular docking suggested that GA interacts with conserved residues (e.g., Arg152 and Asp151) located in the catalytic inner shell of the viral neuraminidase (NA), sharing the same pocket as those of anti-neuraminidase drugs, such as laninamivir and oseltamivir. Additionally, other metabolites were also found to potentially interact with the active site and the hydrophobic 430-cavity of the viral surface protein, suggesting a possibly synergistic effect of various phytochemicals. Therefore, the C. mimosoides aqueous extract may be a good candidate for coping with increasing influenza virus resistance to existing antivirals. [ABSTRACT FROM AUTHOR]

Published
2024
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20. Gingerol extract-stabilized silver nanoparticles and their applications: colorimetric and machine learning-based sensing of Hg(ii) and antibacterial properties

Author

Plaeyao, Kittiya, primary, Kampangta, Ratchaneekorn, additional, Korkokklang, Yuparat, additional, Talodthaisong, Chanon, additional, Saenchoopa, Apichart, additional, Thammawithan, Saengrawee, additional, Latpala, Krailikhit, additional, Patramanon, Rina, additional, Kayunkid, Navaphun, additional, and Kulchat, Sirinan, additional

Published
2023
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45. Sequence analysis and 3-dimensional molecular modelling of Heteroscorpine from the venom of Heterometrus spp.

Author

Incamnoi, Paroonkorn, Patramanon, Rina, Klaynongsruang, Sompong, Chaveerach, Arunrat, Bunyatratchata, Wandee, Uawonggul, Nunthawun, Sukprasert, Sophida, Namonsai, Teerawat, Noikotr, Kowit, Rungsa, Prapenpuksiri, Daduang, Jureerut, and Daduang, Sakda

Subjects
*HETEROMETRUS, *SEQUENCE analysis, *POLYMERASE chain reaction, *SIGNAL peptides, *CYSTEINE
Abstract

Based on the recently identified sequence of Heteroscorpine-1 (HS-1), the genes encoding the scorpine family of toxins from three Heterometrus spp. in Thailand were amplified by polymerase chain reactions (PCR). All three genomic DNAs encoded a precursor protein consisting of 95 amino acid residues, and these proteins share a highly conserved structure with other known scorpion long-chain K+-channel toxins. Based on the data obtained from our specimens, all scorpine family genes possess a 5' UTR and a region encoding the putative signal peptide. The six cysteine positions are highly conserved in invertebrate defensins and scorpion K+ channel toxins, suggesting the presence of a common three-dimensional structure with a cysteine-stabilised αβ (CSαβ) motif. Our scorpine gene family contains an intron that is completely identical to the known scorpion K+-channel blockers in size, consensus junctions, putative branch point, and A + T abundance. We used α-toxin (PDB i.d. 4hhf.1.A), toxin II (PDB i.d.1aho.1.A) and defensin (PDB i.d. 2b68.1) as templates in our analysis of 3-dimensional structures. Residues Asn48 - Lys55 of the mature Heteroscorpine sequence form the α-helix, residues Lys60 - His64 form β-sheet 1, and residues Lys67 - Gly71 form β-sheet 2. Heteroscorpine is predicted to have this structure due to the presence of 3 disulphide bridges. The structure completely follows the typical Cys pattern of invertebrate defensins (CX4-16CX2HCX6-9GX1CX4-9CX1C). Thus, the scorpine family of toxins is likely to use the same mechanism to penetrate the bacterial cell wall as defensin peptides from other insect families. [ABSTRACT FROM AUTHOR]

Published
2018

50. Antimicrobial Action of the Cyclic Peptide Bactenecin on Burkholderia pseudomallei Correlates with Efficient Membrane Permeabilization.

Author

Madhongsa, Kanjana, Pasan, Supaluk, Phophetleb, Onanong, Nasompag, Sawinee, Thammasirirak, Sompong, Daduang, Sakda, Taweechaisupapong, Suwimol, Lomize, Andrei L., and Patramanon, Rina

Subjects
BURKHOLDERIA infections, MELIOIDOSIS, ANTI-infective agents, SEPSIS, BACTERICIDAL action, ANTIBIOTICS
Abstract

Burkholderia pseudomallei is a category B agent that causes Melioidosis, an acute and chronic disease with septicemia. The current treatment regimen is a heavy dose of antibiotics such as ceftazidime (CAZ); however, the risk of a relapse is possible. Peptide antibiotics are an alternative to classical antibiotics as they exhibit rapid action and are less likely to result in the development of resistance. The aim of this study was to determine the bactericidal activity against B. pseudomallei and examine the membrane disrupting abilities of the potent antimicrobial peptides: bactenecin, RTA3, BMAP-18 and CA-MA. All peptides exhibited >97% bactericidal activity at 20 µM, with bactenecin having slightly higher activity. Long term time-kill assays revealed a complete inhibition of cell growth at 50 µM bactenecin and CA-MA. All peptides inhibited biofilm formation comparable to CAZ, but exhibited faster kinetics (within 1 h). Bactenecin exhibited stronger binding to LPS and induced perturbation of the inner membrane of live cells. Interaction of bactenecin with model membranes resulted in changes in membrane fluidity and permeability, leading to leakage of dye across the membrane at levels two-fold greater than that of other peptides. Modeling of peptide binding on the membrane showed stable and deep insertion of bactenecin into the membrane (up to 9 Å). We propose that bactenecin is able to form dimers or large β-sheet structures in a concentration dependent manner and subsequently rapidly permeabilize the membrane, leading to cytosolic leakage and cell death in a shorter period of time compared to CAZ. Bactenecin might be considered as a potent antimicrobial agent for use against B. pseudomallei. [ABSTRACT FROM AUTHOR]

Published
2013
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