Journal of Peptide Science最新文献_第8页

In memory of Prof. Luis Moroder 纪念路易斯-莫罗德教授

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-11-26 DOI: 10.1002/psc.3660

Yuji Kobayashi

引用次数: 0

The versatility of peptide hydrogels: From self-assembly to drug delivery applications 多肽水凝胶的多功能性：从自组装到药物输送应用

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-11-19 DOI: 10.1002/psc.3662

Julie Heremans, Steven Ballet, Charlotte Martin

{"title":"The versatility of peptide hydrogels: From self-assembly to drug delivery applications","authors":"Julie Heremans, Steven Ballet, Charlotte Martin","doi":"10.1002/psc.3662","DOIUrl":"10.1002/psc.3662","url":null,"abstract":"Pharmaceuticals often suffer from limitations such as low solubility, low stability, and short half-life. To address these challenges and reduce the need for frequent drug administrations, a more efficient delivery is required. In this context, the development of controlled drug delivery systems, acting as a protective depot for the drug, has expanded significantly over the last decades. Among these, injectable hydrogels have emerged as a promising platform, especially in view of the rise of biologicals as therapeutics. Hydrogels are functional, solid-like biomaterials, composed of cross-linked hydrophilic polymers and high water content. Their physical properties, which closely mimic the extracellular matrix, make them suitable for various biomedical applications. This review discusses the different types of hydrogel systems and their self-assembly process, with an emphasis on peptide-based hydrogels. Due to their structural and functional diversity, biocompatibility, synthetic accessibility, and tunability, peptides are regarded as promising and versatile building blocks. A comprehensive overview of the variety of peptide hydrogels is outlined, with β-sheet forming sequences being highlighted. Key factors to consider when using peptide hydrogels as a controlled drug delivery system are reviewed, along with a discussion of the main drug release mechanisms and the emerging trend towards affinity-based systems to further refine drug release profiles.","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 2","pages":""},"PeriodicalIF":1.8,"publicationDate":"2024-11-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142676027","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}

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Identification and synthesis of a long-chain antimicrobial peptide from the venom of the Liocheles australasiae scorpion 鉴定和合成澳大利亚蝎子毒液中的长链抗菌肽。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-11-03 DOI: 10.1002/psc.3661

Masahiro Miyashita, Shoichi Sakai, Ryota Okabe, Sayaka Kawai, Takumi Kishimoto, Atsushi Kitanaka, Naoya Mitani, Yoshiaki Nakagawa

{"title":"Identification and synthesis of a long-chain antimicrobial peptide from the venom of the Liocheles australasiae scorpion","authors":"Masahiro Miyashita, Shoichi Sakai, Ryota Okabe, Sayaka Kawai, Takumi Kishimoto, Atsushi Kitanaka, Naoya Mitani, Yoshiaki Nakagawa","doi":"10.1002/psc.3661","DOIUrl":"10.1002/psc.3661","url":null,"abstract":"Scorpion venom contains linear peptides without disulfide bonds in addition to peptides with disulfide bonds. Many such linear peptides have an amphiphilic α-helical structure, often with antimicrobial activity and can be classified into three groups based on their molecular size. Among them, long-chain antimicrobial peptides consisting of more than 40 residues have not been thoroughly studied due to the difficulty of synthesizing them. We have previously reported a transcriptome analysis of the venom gland of Liocheles australasiae that revealed precursor sequences of long-chain antimicrobial peptides. In the study reported here, we identified the mature structure of one such long-chain antimicrobial peptide, LaCT1, which we synthesized using chemical ligation to confirm its structure and evaluate its biological activities. The result showed that LaCT1 exhibited significant antimicrobial activity. In addition, we identified its partial peptides consisting of an N- or C-terminal region, which may be generated by enzymatic cleavage in the venom. Among them, only the peptide containing the N-terminal half region was active. LaCT1 also not only showed insecticidal activity but also synergistically enhanced the effects of another insecticidal peptide identified in L. australasiae venom as well. These results provide insights into the role of antimicrobial peptides in scorpion venom.","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 2","pages":""},"PeriodicalIF":1.8,"publicationDate":"2024-11-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142568504","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

Editorial for the Special Collection “Women in Peptide Science” 为 "多肽科学中的女性 "特辑撰写社论。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-10-28 DOI: 10.1002/psc.3659

Anna Maria Papini, Ines Neundorf, Diana Imhof

引用次数: 0

Impairing protein–protein interactions in an essential tRNA modification complex: An innovative antimicrobial strategy against Pseudomonas aeruginosa 破坏重要 tRNA 修饰复合物中蛋白质与蛋白质之间的相互作用：针对铜绿假单胞菌的创新抗菌策略。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-10-22 DOI: 10.1002/psc.3658

Michela Bollati, Elettra Fasola, Stefano Pieraccini, Francesca Freddi, Paolo Cocomazzi, Francesco Oliva, Merlin Klußmann, Angelo Maspero, Umberto Piarulli, Silvia Ferrara, Sara Pellegrino, Giovanni Bertoni, Silvia Gazzola

{"title":"Impairing protein–protein interactions in an essential tRNA modification complex: An innovative antimicrobial strategy against Pseudomonas aeruginosa","authors":"Michela Bollati, Elettra Fasola, Stefano Pieraccini, Francesca Freddi, Paolo Cocomazzi, Francesco Oliva, Merlin Klußmann, Angelo Maspero, Umberto Piarulli, Silvia Ferrara, Sara Pellegrino, Giovanni Bertoni, Silvia Gazzola","doi":"10.1002/psc.3658","DOIUrl":"10.1002/psc.3658","url":null,"abstract":"Protein–protein interactions (PPIs) have been recognized as a promising target for the development of new drugs, as proved by the growing number of PPI modulators reaching clinical trials. In this context, peptides represent a valid alternative to small molecules, owing to their unique ability to mimic the target protein structure and interact with wider surface areas. Among the possible fields of interest, bacterial PPIs represent an attractive target to face the urgent necessity to fight antibiotic resistance. Growing attention has been paid to the YgjD/YeaZ/YjeE complex responsible for the essential t6A37 tRNA modification in bacteria. We previously identified an α-helix on the surface of Pseudomonas aeruginosa YeaZ, crucial for the YeaZ-YeaZ homodimer formation and the conserved YeaZ-YgjD interactions. Herein, we present our studies for impairing the PPIs involved in the formation of the YeaZ dimers through synthetic peptide derivatives of this helical moiety, both in vitro with purified components and on P. aeruginosa cells. Our results proved the possibility of targeting those PPIs which are usually essential for protein functioning and thus are refractory to mutational changes and antibiotic resistance development.","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 2","pages":""},"PeriodicalIF":1.8,"publicationDate":"2024-10-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11669939/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142468320","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Development and applications of enzymatic peptide and protein ligation 酶肽和蛋白质连接技术的开发与应用。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-10-21 DOI: 10.1002/psc.3657

Yan Cui, Dongyang Han, Xuerong Bai, Weiwei Shi

引用次数: 0

Carbocyclic setmelanotide analogs maintain biochemical potency at melanocortin 4 receptors 羧环塞美拉诺肽类似物在黑皮质素 4 受体上保持生化效力。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-10-12 DOI: 10.1002/psc.3656

Samuel Gary, Anuradha Roy, Steven Bloom

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Synthesis and characterization of new antimicrobial peptides derived from Temporin F 从 Temporin F 提取的新型抗菌肽的合成和表征。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-10-02 DOI: 10.1002/psc.3655

Lucas Melo Bosquetti, Cyntia Silva Oliveira, Giselle Cerchiaro, Vani Xavier Oliveira Junior

{"title":"Synthesis and characterization of new antimicrobial peptides derived from Temporin F","authors":"Lucas Melo Bosquetti, Cyntia Silva Oliveira, Giselle Cerchiaro, Vani Xavier Oliveira Junior","doi":"10.1002/psc.3655","DOIUrl":"10.1002/psc.3655","url":null,"abstract":"Antimicrobial peptides (AMPs) are a promising source of new compounds against resistant bacteria. Temporins are a class of AMPs found on the amphibian Rana temporaria and show activity against Gram-positive and Gram-negative bacteria. There are few studies on how these antimicrobials have been used, but new Temporin-F derivatives were engineered with Lys-substitutions to assess the impact of the net charge on antimicrobial activity and toxicity. We demonstrated through some assays that it is possible to increase the antibacterial activity while maintaining a reduced peptide hemolytic activity with specific substitutions. Our lead synthetic peptide, G6K-Temporin F, has shown higher antimicrobial activity against Gram-negative and Gram-positive bacteria in vitro (MIC range 2 to 32 μmol L−1), with low hemolytic activity maintained, resulting in an increase in the therapeutic window (TW), of 12.5. Also, it showed more resistant to enzymatic degradation. On the other hand, more significant increases in net charges, such as in P3K-G11K-Temporin F, result in a severe increase in toxicity with lower gains in antimicrobial activity (TW of 0.65). In conclusion, we demonstrated that a moderate increase in net charge can lead to a more active analog and G6K-Temporin F is revealed to be promising as a candidate for new AMP therapeutics.","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 2","pages":""},"PeriodicalIF":1.8,"publicationDate":"2024-10-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142365640","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

RGD-functionalised self-assembling peptide hydrogel induces a proliferative profile in human osteoblasts in vitro RGD 功能化自组装肽水凝胶在体外诱导人类成骨细胞增殖。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-09-27 DOI: 10.1002/psc.3653

Luis A. Castillo-Díaz, Julie E. Gough, Aline F. Miller, Alberto Saiani

{"title":"RGD-functionalised self-assembling peptide hydrogel induces a proliferative profile in human osteoblasts in vitro","authors":"Luis A. Castillo-Díaz, Julie E. Gough, Aline F. Miller, Alberto Saiani","doi":"10.1002/psc.3653","DOIUrl":"10.1002/psc.3653","url":null,"abstract":"Self-assembling peptide hydrogels (SAPHs) have been used in the past decade as reliable three-dimensional (3D) synthetic scaffolds for the culture of a variety of mammalian cells in vitro. Thanks to their versatile physicochemical properties, they allow researchers to tailor the hydrogel properties, including stiffness and functionality to the targeted cells and cells' behaviour. One of the advantages of using SAPH scaffolds is the ease of functionalisation. In the present work, we discuss the effect that functionalising the FEFEFKFK (F, phenylalanine; K, lysine; and E, glutamic acid) hydrogel scaffold using the cell-binding RGDS (fibronectin — R, arginine; G, glycine; D, aspartic acid; S, serine) epitope affects the material properties as well as the function of encapsulated human osteoblast cells. RGDS functionalisation resulted in cells adopting an elongated morphology, suggesting attachment and increased proliferation. While this led to higher cell viability, it also resulted in a decrease in extra-cellular matrix (ECM) protein production as well as a decrease in calcium ion deposition, suggesting lower mineralisation capabilities. The work clearly shows that SAPHs are a flexible platform that allow the modification of scaffolds in a controlled manner to investigate cell–material interactions.","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 2","pages":""},"PeriodicalIF":1.8,"publicationDate":"2024-09-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11669940/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142348959","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Combination of the amide-to-triazole substitution strategy with alternative structural modifications for the metabolic stabilization of tumor-targeting, radiolabeled peptides 将酰胺-三唑取代策略与替代性结构修饰相结合，实现肿瘤靶向放射性标记肽的代谢稳定性

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-09-11 DOI: 10.1002/psc.3654

Xabier Guarrochena, Maximilian Anderla, Philipp Salomon, Irene V. J. Feiner, Berthold A. Nock, Theodosia Maina, Thomas L. Mindt

{"title":"Combination of the amide-to-triazole substitution strategy with alternative structural modifications for the metabolic stabilization of tumor-targeting, radiolabeled peptides","authors":"Xabier Guarrochena, Maximilian Anderla, Philipp Salomon, Irene V. J. Feiner, Berthold A. Nock, Theodosia Maina, Thomas L. Mindt","doi":"10.1002/psc.3654","DOIUrl":"10.1002/psc.3654","url":null,"abstract":"Radiolabeled peptides play a key role in nuclear medicine to selectively deliver radionuclides to malignancies for diagnosis (imaging) and therapy. Yet, their efficiency is often compromised by low metabolic stability. The use of 1,4-disubstituted 1,2,3-triazoles (1,4-Tzs) as stable amide bond bioisosteres can increase the half-life of peptides in vivo while maintaining their biological properties. Previously, the amide-to-triazole substitution strategy was used for the stabilization of the pansomatostatin radioligand [111In]In-AT2S, resulting in the mono-triazolo-peptidomimetic [111In]In-XG1, a radiotracer with moderately enhanced stability in vivo and retained ability to bind multiple somatostatin receptor (SSTR) subtypes. However, inclusion of additional 1,4-Tz led to a loss of affinity towards SST2R, the receptor overexpressed by most SSTR-positive cancers. To enhance further the stability of [111In]In-XG1, alternative modifications at the enzymatically labile position Thr10-Phe11 were employed. Three novel 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid (DOTA)-peptide conjugates were synthesized with a 1,4-Tz (Asn5-Ψ[Tz]-Phe6) and either a β-amino acid (β-Phe11), reduced amide bond (Thr10-Ψ[NH]-Phe11), or N-methylated amino acid (N-Me-Phe11). Two of the new peptidomimetics were more stable in blood plasma in vitro than [111In]In-XG1. Yet none of them retained high affinity towards SST2R. We demonstrate for the first time the combination of the amide-to-triazole substitution strategy with alternative stabilization methods to improve the metabolic stability of tumor-targeting peptides.","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":"31 1","pages":""},"PeriodicalIF":1.8,"publicationDate":"2024-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/psc.3654","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142224468","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0