M. Nolan, M. Schüttel, Eoin M. Scanlan, Alexander L. Nielsen
{"title":"Nanomole‐scale photochemical thiol‐ene chemistry for high‐throughput late‐stage diversification of peptide macrocycles","authors":"M. Nolan, M. Schüttel, Eoin M. Scanlan, Alexander L. Nielsen","doi":"10.1002/pep2.24310","DOIUrl":"https://doi.org/10.1002/pep2.24310","url":null,"abstract":"","PeriodicalId":19825,"journal":{"name":"Peptide Science","volume":" ","pages":""},"PeriodicalIF":2.4,"publicationDate":"2023-04-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43602843","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}
{"title":"Erratum: Current peptide vaccine and immunotherapy approaches against Alzheimer's disease","authors":"","doi":"10.1002/pep2.24309","DOIUrl":"https://doi.org/10.1002/pep2.24309","url":null,"abstract":"In the published article cited above, there was an error at the start of paragraph five, section two, β-Amyloid peptide vaccines where ACI-24 is introduced: the company behind ACI-24 was mis-attributed. The first sentence of the paragraph originally read: ACI-24 (AC Immune, Roche and Genentech) is designed to avoid eliciting a Th-1 response to Aβ. The sentence should read: ACI-24 (AC Immune) is designed to avoid eliciting a Th-1 response to Aβ. There was also an error at the start of paragraph six, section two, β-Amyloid peptide vaccines where ABvac40 is introduced: the company behind ABvac40 was mis-attributed. The first sentence of the paragraph originally read: ABvac40 (Axon Neuroscience SE) is designed to target the C-terminus of Aβ1–40. The sentence should read: ABvac40 (Araclon Biotech) is designed to target the C-terminus of Aβ1–40. The authors apologise for any inconvenience this may have caused. DOI: 10.1002/pep2.24309","PeriodicalId":19825,"journal":{"name":"Peptide Science","volume":" ","pages":""},"PeriodicalIF":2.4,"publicationDate":"2023-04-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44061825","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}
J. C. Espeche, Romina Varas, P. Maturana, A. Cutró, P. Maffía, A. Hollmann
{"title":"Membrane permeability and antimicrobial peptides: Much more than just making a hole","authors":"J. C. Espeche, Romina Varas, P. Maturana, A. Cutró, P. Maffía, A. Hollmann","doi":"10.1002/pep2.24305","DOIUrl":"https://doi.org/10.1002/pep2.24305","url":null,"abstract":"","PeriodicalId":19825,"journal":{"name":"Peptide Science","volume":" ","pages":""},"PeriodicalIF":2.4,"publicationDate":"2023-03-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"45367084","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}
Eliana Dell’Olmo, Katia Pane, Martina Schibeci, Angela Cesaro, Maria G De Luca, Shurooq Ismail, R. Gaglione, Angela Arciello
{"title":"Host defense peptides identified in human apolipoprotein B as natural food bio‐preservatives: Evaluation of their biosafety and digestibility","authors":"Eliana Dell’Olmo, Katia Pane, Martina Schibeci, Angela Cesaro, Maria G De Luca, Shurooq Ismail, R. Gaglione, Angela Arciello","doi":"10.1002/pep2.24308","DOIUrl":"https://doi.org/10.1002/pep2.24308","url":null,"abstract":"","PeriodicalId":19825,"journal":{"name":"Peptide Science","volume":" ","pages":""},"PeriodicalIF":2.4,"publicationDate":"2023-03-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48698764","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}
S. Chowdhary, Tim Pelzer, Mareike Saathoff, Elisa Quaas, Johanna Pendl, M. Fulde, B. Koksch
{"title":"Fine‐tuning the antimicrobial activity of β‐hairpin peptides with fluorinated amino acids","authors":"S. Chowdhary, Tim Pelzer, Mareike Saathoff, Elisa Quaas, Johanna Pendl, M. Fulde, B. Koksch","doi":"10.1002/pep2.24306","DOIUrl":"https://doi.org/10.1002/pep2.24306","url":null,"abstract":"","PeriodicalId":19825,"journal":{"name":"Peptide Science","volume":" ","pages":""},"PeriodicalIF":2.4,"publicationDate":"2023-03-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46527363","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}
James R B Eastwood, Ethan I. Weisberg, Dana Katz, R. Zuckermann, K. Kirshenbaum
{"title":"Guidelines for designing peptoid structures: Insights from the Peptoid Data Bank","authors":"James R B Eastwood, Ethan I. Weisberg, Dana Katz, R. Zuckermann, K. Kirshenbaum","doi":"10.1002/pep2.24307","DOIUrl":"https://doi.org/10.1002/pep2.24307","url":null,"abstract":"The number of structural studies of peptoids has grown dramatically over the past 20 years. To date, over 100 high‐resolution structures have been reported for peptoids, which are typically defined as N‐substituted glycine oligomers. We have collected these structures and standardized their sequence representations to facilitate structural analysis as the dataset continues to grow. These structures are presented online as The Peptoid Data Bank (databank.peptoids.org), which also provides persistent links to the published structural data. This review analyzes the present collection of structures and finds extensive support for grouping side chains by their chemistry at the position adjacent to the backbone nitrogen. Groups of side chains with similar chemistry at this position show similar influences on the conformational preferences of the backbone. We also observe a relationship between the side chain and backbone conformations for many monomers that has not previously attracted significant discussion: the values of the χ1 and ϕ dihedrals are correlated. We outline a general design strategy for attaining a specific backbone conformation based on the patterns seen in the collected structures.","PeriodicalId":19825,"journal":{"name":"Peptide Science","volume":" ","pages":""},"PeriodicalIF":2.4,"publicationDate":"2023-03-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47638341","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}
Peptide SciencePub Date : 2023-03-01Epub Date: 2022-11-12DOI: 10.1002/pep2.24298
Tahmina A Milly, Yftah Tal-Gan
{"title":"Targeting Peptide-Based Quorum Sensing Systems for the Treatment of Gram-Positive Bacterial Infections.","authors":"Tahmina A Milly, Yftah Tal-Gan","doi":"10.1002/pep2.24298","DOIUrl":"10.1002/pep2.24298","url":null,"abstract":"<p><p>Bacteria utilize a cell density-dependent communication system called quorum sensing (QS) to coordinate group behaviors. In Gram-positive bacteria, QS involves the production of and response to auto-inducing peptide (AIP) signaling molecules to modulate group phenotypes, including pathogenicity. As such, this bacterial communication system has been identified as a potential therapeutic target against bacterial infections. More specifically, developing synthetic modulators derived from the native peptide signal paves a new way to selectively block the pathogenic behaviors associated with this signaling system. Moreover, rational design and development of potent synthetic peptide modulators allows in depth understanding of the molecular mechanisms that drive QS circuits in diverse bacterial species. Overall, studies aimed at understanding the role of QS in microbial social behavior could result in the accumulation of significant knowledge of microbial interactions, and consequently lead to the development of alternative therapeutic agents to treat bacterial infectivity. In this review, we discuss recent advances in the development of peptide-based modulators to target QS systems in Gram-positive pathogens, with a focus on evaluating the therapeutic potential associated with these bacterial signaling pathways.</p>","PeriodicalId":19825,"journal":{"name":"Peptide Science","volume":"115 2","pages":""},"PeriodicalIF":2.4,"publicationDate":"2023-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10312355/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10127943","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}
Peptide SciencePub Date : 2023-03-01Epub Date: 2023-01-30DOI: 10.1002/pep2.24303
Amy H Guadagno, Scott H Medina
{"title":"The manifold role of octapeptide repeats in prion protein assembly.","authors":"Amy H Guadagno, Scott H Medina","doi":"10.1002/pep2.24303","DOIUrl":"10.1002/pep2.24303","url":null,"abstract":"<p><p>Prion protein misfolding is associated with fatal neurodegenerative disorders such as kuru, Creutzfeldt-Jakob disease, and several animal encephalopathies. While the C-terminal 106-126 peptide has been well studied for its role in prion replication and toxicity, the octapeptide repeat (OPR) sequence found within the N-terminal domain has been relatively under explored. Recent findings that the OPR has both local and long-range effects on prion protein folding and assembly, as well as its ability to bind and regulate transition metal homeostasis, highlights the important role this understudied region may have in prion pathologies. This review attempts to collate this knowledge to advance a deeper understanding on the varied physiologic and pathologic roles the prion OPR plays, and connect these findings to potential therapeutic modalities focused on OPR-metal binding. Continued study of the OPR will not only elucidate a more complete mechanistic model of prion pathology, but may enhance knowledge on other neurodegenerative processes underlying Alzheimer's, Parkinson's, and Huntington's diseases.</p>","PeriodicalId":19825,"journal":{"name":"Peptide Science","volume":"115 2","pages":""},"PeriodicalIF":1.5,"publicationDate":"2023-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10162500/pdf/nihms-1871399.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9439671","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}
Peptide SciencePub Date : 2023-03-01Epub Date: 2022-11-12DOI: 10.1002/pep2.24297
Shilpa R Rao, Thomas W Harmon, Shelby L Heath, Jacob A Wolfe, Jacqueline R Santhouse, Gregory L O'Brien, Alexis N Distefano, Zachary E Reinert, W Seth Horne
{"title":"Chemical Shifts of Artificial Monomers Used to Construct Heterogeneous-Backbone Protein Mimetics in Random Coil and Folded States.","authors":"Shilpa R Rao, Thomas W Harmon, Shelby L Heath, Jacob A Wolfe, Jacqueline R Santhouse, Gregory L O'Brien, Alexis N Distefano, Zachary E Reinert, W Seth Horne","doi":"10.1002/pep2.24297","DOIUrl":"10.1002/pep2.24297","url":null,"abstract":"<p><p>The construction of protein-sized synthetic chains that blend natural amino acids with artificial monomers to create so-called heterogeneous-backbones is a powerful approach to generate complex folds and functions from bio-inspired agents. A variety of techniques from structural biology commonly used to study natural proteins have been adapted to investigate folding in these entities. In NMR characterization of proteins, proton chemical shift is a straightforward to acquire, information-rich metric that bears directly on a variety of properties related to folding. Leveraging chemical shift to gain insight into folding requires a set of reference chemical shift values corresponding to each building block type (i.e., the 20 canonical amino acids in the case of natural proteins) in a random coil state and knowledge of systematic changes in chemical shift associated with particular folded conformations. Although well documented for natural proteins, these issues remain unexplored in the context of protein mimetics. Here, we report random coil chemical shift values for a library of artificial amino acid monomers frequently used to construct heterogeneous-backbone protein analogues as well as a spectroscopic signature associated with one monomer class, β<sup>3</sup>-residues bearing proteinogenic side chains, adopting a helical folded conformation. Collectively, these results will facilitate the continued utilization of NMR for the study of structure and dynamics in protein-like artificial backbones.</p>","PeriodicalId":19825,"journal":{"name":"Peptide Science","volume":"115 2","pages":""},"PeriodicalIF":2.4,"publicationDate":"2023-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10312354/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10127938","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}