International Journal of Peptide Research and Therapeutics最新文献_第2页

PC12 Cell Conditional Medium Prepared after Latroeggtoxin-VI Treatment Suppresses Glioma Cells 拉特罗格毒素-VI 处理后制备的 PC12 细胞条件培养基可抑制胶质瘤细胞

IF 2 4区生物学

International Journal of Peptide Research and Therapeutics Pub Date : 2024-07-16 DOI: 10.1007/s10989-024-10625-7

Yiwen Zhai, Haiyan Wang, Zhixiang Lei, Si Chen, Minglu Sun, Panfeng Yin, Xianchun Wang

引用次数: 0

Design and Validation of Novel Potential Antiperspirant Peptides Blocking M3-Gαq Sweat Signaling Cascade 阻断 M3-Gαq 汗信号级联的新型潜在止汗肽的设计与验证

IF 2 4区生物学

International Journal of Peptide Research and Therapeutics Pub Date : 2024-07-15 DOI: 10.1007/s10989-024-10628-4

Magdalena Nikolaeva-Koleva, Laura Butrón, Ana Sempere, Verónica Rivero, Gregorio Fernández-Ballester, Ana Espinosa, Matteo Vergassola, Elena Mastrocola, Sara Zucchi, L. Ragni, Giorgina Mangano, Isabel Devesa

引用次数: 0

Peptides and Wound Healing: From Monomer to Combination 肽与伤口愈合：从单体到组合

IF 2.5 4区生物学

International Journal of Peptide Research and Therapeutics Pub Date : 2024-07-12 DOI: 10.1007/s10989-024-10627-5

Chang Liu, Qian Qian Yang, You Lang Zhou

引用次数: 0

Antimicrobial Peptides: Potential Alternative to Antibiotics and Overcoming Limitations for Future Therapeutic Applications 抗菌肽：抗菌肽：抗生素的潜在替代品以及克服未来治疗应用的局限性

IF 2.5 4区生物学

International Journal of Peptide Research and Therapeutics Pub Date : 2024-07-02 DOI: 10.1007/s10989-024-10623-9

Vrushali Somase, Sharav A. Desai, Vipul P. Patel, Vivek Patil, Kunal Bhosale

{"title":"Antimicrobial Peptides: Potential Alternative to Antibiotics and Overcoming Limitations for Future Therapeutic Applications","authors":"Vrushali Somase, Sharav A. Desai, Vipul P. Patel, Vivek Patil, Kunal Bhosale","doi":"10.1007/s10989-024-10623-9","DOIUrl":"https://doi.org/10.1007/s10989-024-10623-9","url":null,"abstract":"Among all health-related issues, the rising concerns about drug resistance led to the look for alternative pharmaceutical drugs that are effective against both infectious and noninfectious diseases. Antimicrobial peptides (AMPs) are small molecular peptides that play a crucial role in the innate immunity of various organisms. They have amphiphilic structure and net positive charge, allowing them to interact with membranes and hydrophobic surfaces, showing strong broad-spectrum activity against different microorganisms, including bacteria, fungi, and viruses. They also exhibit other host-beneficial activities, including immunomodulation, anti-inflammatory, tissue regeneration, etc. AMPs exhibit antimicrobial activity through wide mechanisms of action, particularly by focusing on intracellular targets to inhibit the synthesis of nucleic acids and proteins. These wide ranges of mechanisms of action of AMPs have contributed to the slow development of resistance against microorganisms. The increasing pathogen resistance is a major global public health threat, and AMPs are constantly being explored and developed as another treatment for viral diseases such as HIV infection and (COVID-19). This review analyzes the potential of AMPs to combat antimicrobial resistance developed by several antimicrobial-resistant (AMR) microorganisms against existing antibiotics. This review focuses on the highlights of the sources, synthesis, mode, and mechanism of action, the evaluation of several benefits, and the outline of various hurdles. The review has also included the possible solution to the limitations associated with the clinical applications of AMPs, along with its future perspectives and development needed in drug discovery against AMR pathogens.","PeriodicalId":14217,"journal":{"name":"International Journal of Peptide Research and Therapeutics","volume":null,"pages":null},"PeriodicalIF":2.5,"publicationDate":"2024-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141532168","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Weissellicin LM85 Purified from Weissella confusa LM85 Effluxes Potassium Ions and Depletes Proton Motive Force in Escherichia coli ATCC 25922 从魏氏梭菌中纯化的魏氏霉素 LM85 在大肠杆菌 ATCC 25922 中外流钾离子并消耗质子动力

IF 2.5 4区生物学

International Journal of Peptide Research and Therapeutics Pub Date : 2024-06-29 DOI: 10.1007/s10989-024-10622-w

Manoj Kumar Yadav, Santosh Kumar Tiwari

{"title":"Weissellicin LM85 Purified from Weissella confusa LM85 Effluxes Potassium Ions and Depletes Proton Motive Force in Escherichia coli ATCC 25922","authors":"Manoj Kumar Yadav, Santosh Kumar Tiwari","doi":"10.1007/s10989-024-10622-w","DOIUrl":"https://doi.org/10.1007/s10989-024-10622-w","url":null,"abstract":"Bacteriocins are membrane-acting peptides and generally kill closely related bacteria using pore formation. In this study, we have studied a bacteriocin, weissellicin LM85 from Weissella confusa LM85 to monitor its antimicrobial activity against Escherichia coli ATCC 25922. It was purified from cell-free supernatant of W. confusa LM85 with molecular weight ~ 6.5 kDa and showed minimum inhibitory concentration, 138.3 µg/mL and minimum bactericidal concentration, 553.3 µg/mL against E. coli ATCC 25922. The loss of cell-viability, tested by staining with propidium iodide, suggested bactericidal effect of weissellicin LM85. There was efflux of potassium (K+) ions, dissipation of membrane potential (∆ψ) and transmembrane pH gradient (∆pH) in bacteriocin-treated cells. The target cells were found swollen and ruptured when visualized under electron microscope. It inhibited range of Gram-positive and Gram-negative bacteria such as Lactiplantibacillus plantarum NRRL B-4496, Lpb. plantarum LD4, Lactobacillus acidophilus NRRL B-4495, Enterococcus faecium NRRL B-2354, E. hirae LD3, E. faecalis ATCC 29212, Pediococcus pentosaceus LB44, Vibrio sp., Salmonella enterica subsp. enterica serovar Typhimurium ATCC 13311, Shigella flexneri, Staphylococcus aureus ATCC 25923 and Pseudomonas aeruginosa ATCC 27853. The above results indicate weissellicin LM85 is a membrane-acting peptide with broad host-range of antimicrobial activity and may be used as alternative to clinical antibiotics.","PeriodicalId":14217,"journal":{"name":"International Journal of Peptide Research and Therapeutics","volume":null,"pages":null},"PeriodicalIF":2.5,"publicationDate":"2024-06-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141506028","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Exploring Therapeutic Potential: A Comprehensive Review of Antimicrobial Peptides in Oral Cancer Management 探索治疗潜力：抗菌肽在口腔癌治疗中的应用综述

IF 2.5 4区生物学

International Journal of Peptide Research and Therapeutics Pub Date : 2024-06-22 DOI: 10.1007/s10989-024-10621-x

Vanitha Marunganathan, Ajay Guru, Siva Prasad Panda, Jesu Arockiaraj

{"title":"Exploring Therapeutic Potential: A Comprehensive Review of Antimicrobial Peptides in Oral Cancer Management","authors":"Vanitha Marunganathan, Ajay Guru, Siva Prasad Panda, Jesu Arockiaraj","doi":"10.1007/s10989-024-10621-x","DOIUrl":"https://doi.org/10.1007/s10989-024-10621-x","url":null,"abstract":"Antimicrobial peptides (AMPs) have garnered attention for their differential regulation in cancers like oral squamous cell carcinomas (OSCC), suggesting their potential as novel anti-cancer agents. These small cationic peptides play crucial roles in innate immunity, particularly in the oral cavity where they are produced by salivary glands and epithelium to combat microbial invasion. AMPs exhibit antimicrobial and anti-cancer activities, disrupting microbial cell membranes and inducing cytotoxicity in cancer cells by binding to exposed phosphatidylserine moieties. Certain AMPs also trigger the release of tumor antigens and damage-associated molecular patterns. With increasing resistance to conventional chemotherapy, AMPs present a promising avenue for the development of effective therapeutic agents in oncology. In addition to their direct cytotoxic effects on cancer cells, AMPs exhibit potential in activating adaptive immunity and functioning as tumor suppressor genes. This review explores the properties, mode of action, and potential interaction of AMPs and specific cancer cells, emphasizing their role in combating oral cancer and the need for further research in this area.","PeriodicalId":14217,"journal":{"name":"International Journal of Peptide Research and Therapeutics","volume":null,"pages":null},"PeriodicalIF":2.5,"publicationDate":"2024-06-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141506029","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Stability of Multi-Peptide Vaccines in Conditions Enabling Accessibility in Limited Resource Settings 多肽疫苗在资源有限条件下的稳定性

IF 2.5 4区生物学

International Journal of Peptide Research and Therapeutics Pub Date : 2024-06-19 DOI: 10.1007/s10989-024-10620-y

Emily G. Ashkani, Brian D. McKenna, Jennifer L. Bryant, Dilza Trevisan-Silva, Nicholas E. Sherman, Kimberly A. Chianese-Bullock, Craig L. Slingluff

引用次数: 0

Exploring the Potential of Designed Peptides Containing Lysine and Arginine Repeats against VIM-2 Metallo-Beta-Lactamases 探索含有赖氨酸和精氨酸重复序列的设计肽对抗 VIM-2 金属-β-内酰胺酶的潜力

IF 2.5 4区生物学

International Journal of Peptide Research and Therapeutics Pub Date : 2024-06-17 DOI: 10.1007/s10989-024-10619-5

Ananya Anurag Anand, Amaresh Kumar Sahoo, Sintu Kumar Samanta

{"title":"Exploring the Potential of Designed Peptides Containing Lysine and Arginine Repeats against VIM-2 Metallo-Beta-Lactamases","authors":"Ananya Anurag Anand, Amaresh Kumar Sahoo, Sintu Kumar Samanta","doi":"10.1007/s10989-024-10619-5","DOIUrl":"https://doi.org/10.1007/s10989-024-10619-5","url":null,"abstract":"The persistent development of bacterial resistance to β-lactam antibiotics presents a serious risk to public health worldwide. The ability of metallo-β-lactamases (MBLs) to hydrolyze a wide range of β-lactam antibiotics and render them ineffective makes them a difficult challenge. The identification and design of clinically useful inhibitors against MBLs like Verona integron-encoded metallo-β-lactamase-2 (VIM-2) is still challenging. In this study, we examine the inhibitory capacity of peptides against VIM-2 of Pseudomonas aeruginosa. Deriving inspiration from earlier studies on arginine-rich peptides, we hypothesized that lysine repeats with similar nature may show comparable binding with VIM-2.We found that lysine repeats are much more stable than arginine repeats, and show comparable binding with VIM-2. Initially, we designed a library of peptides containing various combinations of lysine and arginine residues, with the sequence length of 30 amino acids. By means of computational modeling, Protein-Peptide docking and molecular dynamics simulations, we evaluated the stability and binding affinity of these peptides in complex with VIM-2. Peptides showing best binding with VIM-2 were subjected to optimization where length was reduced to 12 residues. This optimization was performed to reduce charge and potential toxicity, enhancing the translational prospects of the sequences. We observed that PolyKR (6) was found to be the lead candidate. We demonstrate that incorporation of KR repeats in peptide sequences can be of help in enhancing their binding affinity towards VIM-2. Further, wet-laboratory validation needs to be performed in order to study the interaction of the peptide with the VIM-2 MBL in detail.","PeriodicalId":14217,"journal":{"name":"International Journal of Peptide Research and Therapeutics","volume":null,"pages":null},"PeriodicalIF":2.5,"publicationDate":"2024-06-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141506031","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The Role and Development of Peptide Vaccines in Cervical Cancer Treatment 多肽疫苗在宫颈癌治疗中的作用与发展

IF 2.5 4区生物学

International Journal of Peptide Research and Therapeutics Pub Date : 2024-05-24 DOI: 10.1007/s10989-024-10617-7

Minhui Wang, Yanyu Gong, Wenyan Kang, Xiaomin Liu, Xiaoqiu Liang

引用次数: 0

Molecular Basis of JZTX-III Inhibiting the Fast Inactivation of Voltage-Gated Sodium Channel Nav1.5 JZTX-III 抑制电压门控钠通道 Nav1.5 快速失活的分子基础

IF 2.5 4区生物学

International Journal of Peptide Research and Therapeutics Pub Date : 2024-05-23 DOI: 10.1007/s10989-024-10618-6

Bo Chen, Min Lu, Xiongzhi Zeng

引用次数: 0