Journal of Peptide Science最新文献

A high hydrophobic moment arginine-rich peptide screened by a machine learning algorithm enhanced ADC antitumor activity. 通过机器学习算法筛选出的高疏水矩富含精氨酸的多肽增强了 ADC 的抗肿瘤活性。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-12-01 Epub Date: 2024-07-01 DOI: 10.1002/psc.3628

Ruo-Long Su, Xue-Wei Cao, Jian Zhao, Fu-Jun Wang

{"title":"A high hydrophobic moment arginine-rich peptide screened by a machine learning algorithm enhanced ADC antitumor activity.","authors":"Ruo-Long Su, Xue-Wei Cao, Jian Zhao, Fu-Jun Wang","doi":"10.1002/psc.3628","DOIUrl":"10.1002/psc.3628","url":null,"abstract":"Cell-penetrating peptides (CPPs) with better biomolecule delivery properties will expand their clinical applications. Using the MLCPP2.0 machine algorithm, we screened multiple candidate sequences with potential cellular uptake ability from the nuclear localization signal/nuclear export signal database and verified them through cell-penetrating fluorescent tracing experiments. A peptide (NCR) derived from the Rev protein of the caprine arthritis-encephalitis virus exhibited efficient cell-penetrating activity, delivering over four times more EGFP than the classical CPP TAT, allowing it to accumulate in lysosomes. Structural and property analysis revealed that a high hydrophobic moment and an appropriate hydrophobic region contribute to the high delivery activity of NCR. Trastuzumab emtansine (T-DM1), a HER2-targeted antibody-drug conjugate, could improve its anti-tumor activity by enhancing targeted delivery efficiency and increasing lysosomal drug delivery. This study designed a new NCR vector to non-covalently bind T-DM1 by fusing domain Z, which can specifically bind to the Fc region of immunoglobulin G and effectively deliver T-DM1 to lysosomes. MTT results showed that the domain Z-NCR vector significantly enhanced the cytotoxicity of T-DM1 against HER2-positive tumor cells while maintaining drug specificity. Our results make a useful attempt to explore the potential application of CPP as a lysosome-targeted delivery tool.","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141476795","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

Intramolecular lactam cross-linking of short oligoureas. 短寡聚内酰胺分子内交联。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-12-01 Epub Date: 2024-07-15 DOI: 10.1002/psc.3644

Paulina Bachurska-Szpala, Rafał Chojnacki, Karolina Pulka-Ziach

引用次数: 0

Low-molecular-weight gels from amino acid and peptide derivatives for controlled release and delivery. 用于控释和给药的氨基酸和肽衍生物低分子量凝胶。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-12-01 Epub Date: 2024-07-15 DOI: 10.1002/psc.3643

Demetra Giuri, Fabia Cenciarelli, Claudia Tomasini

引用次数: 0

PICKAPEP: An application for parameter calculation and visualization of cyclized and modified peptidomimetics. PICKAPEP：用于环化和修饰拟肽物的参数计算和可视化的应用程序。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-12-01 Epub Date: 2024-07-31 DOI: 10.1002/psc.3646

Vanessa Erckes, Mattis Hilleke, Clemens Isert, Christian Steuer

{"title":"PICKAPEP: An application for parameter calculation and visualization of cyclized and modified peptidomimetics.","authors":"Vanessa Erckes, Mattis Hilleke, Clemens Isert, Christian Steuer","doi":"10.1002/psc.3646","DOIUrl":"10.1002/psc.3646","url":null,"abstract":"The interest in peptides and especially in peptidomimetic structures has risen enormously in the past few years. Novel modification strategies including nonnatural amino acids, sophisticated cyclization strategies, and side chain modifications to improve the pharmacokinetic properties of peptides are continuously arising. However, a calculator tool accompanying the current development in peptide sciences towards modified peptides is missing. Herein, we present the application PICKAPEP, enabling the virtual construction and visualization of peptidomimetics ranging from well-known cyclized and modified peptides such as ciclosporin A up to fully self-designed peptide-based structures with custom amino acids. Calculated parameters include the molecular weight, the water-octanol partition coefficient, the topological polar surface area, the number of rotatable bonds, and the peptide SMILES code. To our knowledge, PICKAPEP is the first tool allowing users to add custom amino acids as building blocks and also the only tool giving the possibility to process large peptide libraries and calculate parameters for multiple peptides at once. We believe that PICKAPEP will support peptide researchers in their work and will find wide application in current as well as future peptide drug development processes. PICKAPEP is available open source for Windows and Mac operating systems (https://www.research-collection.ethz.ch/handle/20.500.11850/681174).","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141860099","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

Conformational analysis of a new peptide derived from feline immunodeficiency virus gp36 in SDS micelles: An NMR-MD based investigation. 猫免疫缺陷病毒 gp36 的新肽在 SDS 胶束中的构象分析：基于 NMR-MD 的研究。

IF 1.8 4区生物学

Journal of Peptide Science Pub Date : 2024-12-01 Epub Date: 2024-07-18 DOI: 10.1002/psc.3645

Angelo Santoro, Michela Buonocore, Mohammad Firoznezhad, Manuela Grimaldi, Anna Maria D'Ursi

{"title":"Conformational analysis of a new peptide derived from feline immunodeficiency virus gp36 in SDS micelles: An NMR-MD based investigation.","authors":"Angelo Santoro, Michela Buonocore, Mohammad Firoznezhad, Manuela Grimaldi, Anna Maria D'Ursi","doi":"10.1002/psc.3645","DOIUrl":"10.1002/psc.3645","url":null,"abstract":"Feline immunodeficiency virus (FIV) shares structural similarities with human immunodeficiency virus (HIV): the surface glycoprotein gp36 corresponds to the HIV gp41, which drives virus-host cell interactions and is targeted by the peptide entry inhibitor enfuvirtide. Following a similar drug design strategy for the development of an anti-FIV therapy, the present study investigates 627-646gp36 NHR, a peptide sequence derived from a region of gp36 that was previously found to interfere with the antiviral activity of the peptide C8, which instead derives from the gp36 MPER. CD, NMR, and MD simulations were employed to probe the conformational characteristics of 627-646gp36 NHR in the membrane-mimicking environment of SDS micelles. Our data show that 627-646gp36 NHR is characterized by three dynamic helix structures. MD simulations involving 627-646gp36 NHR, C8, and a larger protein, including the CHR and MPER regions, suggest that the interaction of C8 with the MPER region, the origin of the antiviral activity of C8, is disfavored in the presence of 627-646gp36 NHR in the simulation. This evidence can be useful for interpreting the molecular mechanism that leads to interference with the activity of C8, providing information on the folding/unfolding mechanism of the viral glycoprotein to design new strategies to inhibit viral entry.","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141731227","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

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":"https://doi.org/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":null,"pages":null},"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":"https://doi.org/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":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2024-10-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","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":"","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

{"title":"Carbocyclic setmelanotide analogs maintain biochemical potency at melanocortin 4 receptors.","authors":"Samuel Gary, Anuradha Roy, Steven Bloom","doi":"10.1002/psc.3656","DOIUrl":"https://doi.org/10.1002/psc.3656","url":null,"abstract":"The melanocortin 4 receptor (MC4R) plays a critical role in satiety and energy homeostasis, and its dysregulation is implicated in numerous hyperphagic and obese disease states. Setmelanotide, a disulfide-based cyclic peptide, can rescue MC4R activity and treat obesities caused by genetic defects in MC4R signaling. But this peptide has moderate blood-brain barrier penetrance and metabolic stability, which can limit its efficacy in practice. Based on the cryo-electron microscopy structure of setmelanotide-bound MC4R, we hypothesized that replacing its lone disulfide bond with more metabolically stable and permeability-enhancing carbon-based linker groups could improve pharmacokinetic properties without abolishing activity. To test this, we used chemistry developed by our lab to prepare 11 carbocyclic (alkyl, aryl, perfluoroalkyl, and ethereal) analogs of setmelanotide and determined their biochemical potencies at MC4R in vitro. Ten analogs displayed full agonism, showing that disulfide replacement is tolerant of linkers ranging in size, rigidity, and functional groups, with heteroatom- or aryl-rich linkers displaying superior potencies.","PeriodicalId":16946,"journal":{"name":"Journal of Peptide Science","volume":null,"pages":null},"PeriodicalIF":1.8,"publicationDate":"2024-10-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142468318","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