Swati Singh, Varshita Srivastava, P. Godara, H. Banavath, Harshita Tak, Arya Nayak, D. Kumari, B. Naik, D. Prusty
Monkeypox is a zoonotic disease caused by the Poxviridiea family virus Monkeypox. According to the Centers for Disease Control and Prevention, 70,420 monkeypox virus infections had been reported in 107 countries as of October 6, 2022. New studies have concluded that the monkeypox outbreak is caused by a strain with a unique mutation, increasing the possibility that the virus may develop resistance to current medicines by accumulating mutations in therapeutic targets. As peptide‐based therapeutics impede the drug target through multiple interactions, it may offer a better therapeutic solution to the possible drug resistance issue related to monkeypox treatment. Therefore, in this work, we screened an antiviral peptide library, the CPP site 2.0 database, against the p37 target protein using molecular docking approaches. The p37 is required for the viral pathogen's successful egression and spread. The allergenicity and physicochemical properties of the peptides were thoroughly analyzed before the molecular docking studies for selecting druggable candidates. The interactions of the peptides bearing the highest docking score were validated further by using molecular dynamics (MD) simulation studies. Our investigation revealed that two cell‐penetrating peptides of the CPP site 2.0 database might effectively prevent the egression and spread of the MPXV by inhibiting p37. Following more testing, these peptides can be explored in developing peptide‐based therapies against the MPX therapy.
{"title":"An in‐silico‐based study identified peptide inhibitors that can block the egression of the monkeypox virus by inhibiting the p37 protein target","authors":"Swati Singh, Varshita Srivastava, P. Godara, H. Banavath, Harshita Tak, Arya Nayak, D. Kumari, B. Naik, D. Prusty","doi":"10.1002/pep2.24325","DOIUrl":"https://doi.org/10.1002/pep2.24325","url":null,"abstract":"Monkeypox is a zoonotic disease caused by the Poxviridiea family virus Monkeypox. According to the Centers for Disease Control and Prevention, 70,420 monkeypox virus infections had been reported in 107 countries as of October 6, 2022. New studies have concluded that the monkeypox outbreak is caused by a strain with a unique mutation, increasing the possibility that the virus may develop resistance to current medicines by accumulating mutations in therapeutic targets. As peptide‐based therapeutics impede the drug target through multiple interactions, it may offer a better therapeutic solution to the possible drug resistance issue related to monkeypox treatment. Therefore, in this work, we screened an antiviral peptide library, the CPP site 2.0 database, against the p37 target protein using molecular docking approaches. The p37 is required for the viral pathogen's successful egression and spread. The allergenicity and physicochemical properties of the peptides were thoroughly analyzed before the molecular docking studies for selecting druggable candidates. The interactions of the peptides bearing the highest docking score were validated further by using molecular dynamics (MD) simulation studies. Our investigation revealed that two cell‐penetrating peptides of the CPP site 2.0 database might effectively prevent the egression and spread of the MPXV by inhibiting p37. Following more testing, these peptides can be explored in developing peptide‐based therapies against the MPX therapy.","PeriodicalId":19825,"journal":{"name":"Peptide Science","volume":" ","pages":""},"PeriodicalIF":2.4,"publicationDate":"2023-07-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43220124","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}
Pub Date : 2023-07-01Epub Date: 2023-05-25DOI: 10.1002/pep2.24323
Ziyong Z Hong, Ruixuan R Yu, Xiaoyu Zhang, Allison M Webb, Nathaniel L Burge, Michael G Poirier, Jennifer J Ottesen
Simple and efficient total synthesis of homogeneous and chemically modified protein samples remains a significant challenge. Here, we report development of a convergent hybrid phase native chemical ligation (CHP-NCL) strategy for facile preparation of proteins. In this strategy, proteins are split into ~100-residue blocks, and each block is assembled on solid support from synthetically accessible peptide fragments before ligated together into full-length protein in solution. With the new method, we increase the yield of CENP-A synthesis by 2.5-fold compared to the previous hybrid phase ligation approach. We further extend the new strategy to the total chemical synthesis of 212-residue linker histone H1.2 in unmodified, phosphorylated, and citrullinated forms, each from eight peptide segments with only one single purification. We demonstrate that fully synthetic H1.2 replicates the binding interactions of linker histones to intact mononucleosomes, as a proxy for the essential function of linker histones in the formation and regulation of higher order chromatin structure.
{"title":"Development of Convergent Hybrid Phase Ligation for Efficient and Convenient Total Synthesis of Proteins.","authors":"Ziyong Z Hong, Ruixuan R Yu, Xiaoyu Zhang, Allison M Webb, Nathaniel L Burge, Michael G Poirier, Jennifer J Ottesen","doi":"10.1002/pep2.24323","DOIUrl":"10.1002/pep2.24323","url":null,"abstract":"<p><p>Simple and efficient total synthesis of homogeneous and chemically modified protein samples remains a significant challenge. Here, we report development of a convergent hybrid phase native chemical ligation (CHP-NCL) strategy for facile preparation of proteins. In this strategy, proteins are split into ~100-residue blocks, and each block is assembled on solid support from synthetically accessible peptide fragments before ligated together into full-length protein in solution. With the new method, we increase the yield of CENP-A synthesis by 2.5-fold compared to the previous hybrid phase ligation approach. We further extend the new strategy to the total chemical synthesis of 212-residue linker histone H1.2 in unmodified, phosphorylated, and citrullinated forms, each from eight peptide segments with only one single purification. We demonstrate that fully synthetic H1.2 replicates the binding interactions of linker histones to intact mononucleosomes, as a proxy for the essential function of linker histones in the formation and regulation of higher order chromatin structure.</p>","PeriodicalId":19825,"journal":{"name":"Peptide Science","volume":"115 4","pages":""},"PeriodicalIF":1.5,"publicationDate":"2023-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10488053/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10605700","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}
Nidhi Gour, Vivekshinh Kshtriya, B. Koshti, Monisha Patel, D. Boukhvalov
We report for the very first time the controlled structural changes in the self‐assemblies of N‐(9‐fluorenylmethoxycarbonyl)‐O‐tert‐butyl‐l‐threonine (Fmoc‐Thr(tBu)‐OH) (FTU) to well defined unique morphologies. The self‐assembling properties of FTU were very interesting and intriguing as it resulted in the formation of unusual structures which resembles fibrous dumbbells and double‐sided broomstick‐like morphologies along with conventional spheres and rods under controlled conditions of concentration and temperature. The self‐assembly of other derivatives of threonine as well as another hydroxyl containing amino acid with same modification that is, ((N‐(9H‐fluoren‐9‐yl)methoxy)carbonyl)‐O‐(tert‐butyl)‐l‐serine (Fmoc‐Ser(tBu)‐OH) (FSU) was also studied to understand the crucial role of –Fmoc, ‐tBu and an additional –CH3 group present in the structure of FTU in the process of self‐assembly. Solvent dependent morphological studies of FTU and FSU suggest important role of solubility parameters and crystallization in formation of these unusual structures. The control experiments of co‐incubation with tannic acid and urea and solution state 1H‐NMR studies elucidate π–π stacking interactions as the key driving force for the structure formation. Further, the interactions which can occur between pairs of FTU and FSU which cause initial self‐assembly was studied theoretically via computational modeling. These studies suggest pair of FTU can either interact via head‐to‐head (HH) or head‐to‐tail (HT) configurations and the most favorable probabilities of either of these interactions lead to morphological transitions in FTU self‐assembly under varying conditions. The studies reported herein hence demonstrate that bioorganic molecules like protected single amino acids can be efficiently used as scaffold for self‐assembly and provide a very simple and facile bottom‐up‐approach for the design of uncommon novel micro/nanoarchitects for multifarious applications.
{"title":"Controlled aggregation properties of threonine modified by protecting groups to unusual self‐assembled structures","authors":"Nidhi Gour, Vivekshinh Kshtriya, B. Koshti, Monisha Patel, D. Boukhvalov","doi":"10.1002/pep2.24324","DOIUrl":"https://doi.org/10.1002/pep2.24324","url":null,"abstract":"We report for the very first time the controlled structural changes in the self‐assemblies of N‐(9‐fluorenylmethoxycarbonyl)‐O‐tert‐butyl‐l‐threonine (Fmoc‐Thr(tBu)‐OH) (FTU) to well defined unique morphologies. The self‐assembling properties of FTU were very interesting and intriguing as it resulted in the formation of unusual structures which resembles fibrous dumbbells and double‐sided broomstick‐like morphologies along with conventional spheres and rods under controlled conditions of concentration and temperature. The self‐assembly of other derivatives of threonine as well as another hydroxyl containing amino acid with same modification that is, ((N‐(9H‐fluoren‐9‐yl)methoxy)carbonyl)‐O‐(tert‐butyl)‐l‐serine (Fmoc‐Ser(tBu)‐OH) (FSU) was also studied to understand the crucial role of –Fmoc, ‐tBu and an additional –CH3 group present in the structure of FTU in the process of self‐assembly. Solvent dependent morphological studies of FTU and FSU suggest important role of solubility parameters and crystallization in formation of these unusual structures. The control experiments of co‐incubation with tannic acid and urea and solution state 1H‐NMR studies elucidate π–π stacking interactions as the key driving force for the structure formation. Further, the interactions which can occur between pairs of FTU and FSU which cause initial self‐assembly was studied theoretically via computational modeling. These studies suggest pair of FTU can either interact via head‐to‐head (HH) or head‐to‐tail (HT) configurations and the most favorable probabilities of either of these interactions lead to morphological transitions in FTU self‐assembly under varying conditions. The studies reported herein hence demonstrate that bioorganic molecules like protected single amino acids can be efficiently used as scaffold for self‐assembly and provide a very simple and facile bottom‐up‐approach for the design of uncommon novel micro/nanoarchitects for multifarious applications.","PeriodicalId":19825,"journal":{"name":"Peptide Science","volume":" ","pages":""},"PeriodicalIF":2.4,"publicationDate":"2023-06-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"45164817","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}
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}
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
{"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}
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