Pub Date : 2019-05-09DOI: 10.1039/9781788013857-00014
D. Stelitano, G. Franci, A. Chianese, S. Galdiero, G. Morelli, M. Galdiero
It has been estimated that the 90% of the world population is affected by HSV-1 or HSV-2 infections. Clinical manifestations associated with these infectious agents range from cold sores and genital lesions to keratitis, encephalitis and meningoencephalitis. Nowadays these viruses represent a global health and economic burden. Despite a century of scientific research a vaccine for HSV-1 and HSV-2 viruses is still not available. However, in the last years HSV glycoproteins have strongly emerged as putative candidates for vaccine development. In this chapter we provide insights into HSV glycoproteins structure, function and the current state of art in the development of a vaccine for these pathogens.
{"title":"HSV membrane glycoproteins, their function in viral entry and their use in vaccine studies","authors":"D. Stelitano, G. Franci, A. Chianese, S. Galdiero, G. Morelli, M. Galdiero","doi":"10.1039/9781788013857-00014","DOIUrl":"https://doi.org/10.1039/9781788013857-00014","url":null,"abstract":"It has been estimated that the 90% of the world population is affected by HSV-1 or HSV-2 infections. Clinical manifestations associated with these infectious agents range from cold sores and genital lesions to keratitis, encephalitis and meningoencephalitis. Nowadays these viruses represent a global health and economic burden. Despite a century of scientific research a vaccine for HSV-1 and HSV-2 viruses is still not available. However, in the last years HSV glycoproteins have strongly emerged as putative candidates for vaccine development. In this chapter we provide insights into HSV glycoproteins structure, function and the current state of art in the development of a vaccine for these pathogens.","PeriodicalId":111070,"journal":{"name":"Amino Acids, Peptides and Proteins","volume":"9 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2019-05-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"125058429","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-05-09DOI: 10.1039/9781788013857-00127
Naresh Kumar
Non-destructive and label-free nanoscale chemical characterisation of peptides and proteins is essential in order to comprehend their biological function. Over the last two decades, Tip-enhanced Raman spectroscopy (TERS) has emerged as a powerful analytical tool for highly sensitive topographical and chemical characterisation of a surface at the nanoscale. Herein, the capabilities and potential TERS for nanoscale investigation of amino acids, peptides and proteins are discussed. The unique chemical insights obtained via TERS characterisation of these biomolecules reported in various studies are critically evaluated. Finally, practical guidelines are presented for the acquisition, analysis and interpretation of TERS data from peptides and protein samples.
{"title":"Nanoscale chemical characterisation of peptides and proteins using tip-enhanced Raman spectroscopy","authors":"Naresh Kumar","doi":"10.1039/9781788013857-00127","DOIUrl":"https://doi.org/10.1039/9781788013857-00127","url":null,"abstract":"Non-destructive and label-free nanoscale chemical characterisation of peptides and proteins is essential in order to comprehend their biological function. Over the last two decades, Tip-enhanced Raman spectroscopy (TERS) has emerged as a powerful analytical tool for highly sensitive topographical and chemical characterisation of a surface at the nanoscale. Herein, the capabilities and potential TERS for nanoscale investigation of amino acids, peptides and proteins are discussed. The unique chemical insights obtained via TERS characterisation of these biomolecules reported in various studies are critically evaluated. Finally, practical guidelines are presented for the acquisition, analysis and interpretation of TERS data from peptides and protein samples.","PeriodicalId":111070,"journal":{"name":"Amino Acids, Peptides and Proteins","volume":"101 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2019-05-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"132452068","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-05-09DOI: 10.1039/9781788013857-00044
F. Hudecz
This chapter is to outline the design, synthesis, chemical and functional characterization of a set of structurally related branched polymeric polypeptides with poly[Lys] backbone. It has been documented that the composition and amino acid sequence of the branch could markedly determine the physico-chemical characteristics including solution conformation, the interaction phospholipid mono- or bilayers as well as the biological properties, like cytotoxicity, blood clearance, biodistribution, immunoreactivity of the compound and even related bioconjugates with chemotherapeutic agent, peptide epitope or reporter entity. The synthesis, structural and functional characterization of conjugates, in which (i) various antitumour, antiparasitic compounds (e.g. daunomycin, methotrexate, GnRH analogue), (ii) imaging agents (e.g. radionuclides, fluorophores) or (iii) B- and/or T-cell epitope peptides from viral (e.g. Herpes simplex virus), bacterial (e.g. M. tuberculosis) and various disease (e.g. tumour, Alzheimer disease) related proteins are attached covalently to selected poly[Lys] branched polymeric polypeptides are discussed.
{"title":"Branched polymeric polypeptides with poly[Lys]","authors":"F. Hudecz","doi":"10.1039/9781788013857-00044","DOIUrl":"https://doi.org/10.1039/9781788013857-00044","url":null,"abstract":"This chapter is to outline the design, synthesis, chemical and functional characterization of a set of structurally related branched polymeric polypeptides with poly[Lys] backbone. It has been documented that the composition and amino acid sequence of the branch could markedly determine the physico-chemical characteristics including solution conformation, the interaction phospholipid mono- or bilayers as well as the biological properties, like cytotoxicity, blood clearance, biodistribution, immunoreactivity of the compound and even related bioconjugates with chemotherapeutic agent, peptide epitope or reporter entity. The synthesis, structural and functional characterization of conjugates, in which (i) various antitumour, antiparasitic compounds (e.g. daunomycin, methotrexate, GnRH analogue), (ii) imaging agents (e.g. radionuclides, fluorophores) or (iii) B- and/or T-cell epitope peptides from viral (e.g. Herpes simplex virus), bacterial (e.g. M. tuberculosis) and various disease (e.g. tumour, Alzheimer disease) related proteins are attached covalently to selected poly[Lys] branched polymeric polypeptides are discussed.","PeriodicalId":111070,"journal":{"name":"Amino Acids, Peptides and Proteins","volume":"29 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2019-05-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"124815947","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-05-09DOI: 10.1039/9781788013857-00091
Eugeni M. Ryadnov, M. Ryadnov
This chapter discusses molecular mechanisms involving proteins of three main classes – tau proteins, amyloid-β and presenilins – that lead to the symptoms characteristic of the Alzheimer's disease. A particular focus is placed on primary structure modifications, conformations and conformational transitions of these proteins. The work highlights specialist research findings published over the last few years to the time of its submission. The reviewed literature is sourced from different databases including Web of Science, RCSB Protein Data Bank and PubMed. A reference to background information is also provided to cover an unlimited timeframe. Individual sections are arranged according to each of the three proteins, emphasising the mechanistic implications of each protein in the neuropathology of AD.
本章讨论了导致阿尔茨海默病特征症状的三种主要蛋白质(tau蛋白、淀粉样蛋白-β和早老素)的分子机制。特别关注的是这些蛋白质的初级结构修饰、构象和构象转变。这项工作突出了过去几年到提交时发表的专家研究成果。综述文献来自不同的数据库，包括Web of Science, RCSB Protein Data Bank和PubMed。还提供了对背景资料的参考，以涵盖无限的时间范围。根据这三种蛋白质中的每一种进行单独的切片排列，强调每种蛋白质在阿尔茨海默病神经病理学中的机制含义。
{"title":"Peptide-mediated pathogenesis of Alzheimer's disease","authors":"Eugeni M. Ryadnov, M. Ryadnov","doi":"10.1039/9781788013857-00091","DOIUrl":"https://doi.org/10.1039/9781788013857-00091","url":null,"abstract":"This chapter discusses molecular mechanisms involving proteins of three main classes – tau proteins, amyloid-β and presenilins – that lead to the symptoms characteristic of the Alzheimer's disease. A particular focus is placed on primary structure modifications, conformations and conformational transitions of these proteins. The work highlights specialist research findings published over the last few years to the time of its submission. The reviewed literature is sourced from different databases including Web of Science, RCSB Protein Data Bank and PubMed. A reference to background information is also provided to cover an unlimited timeframe. Individual sections are arranged according to each of the three proteins, emphasising the mechanistic implications of each protein in the neuropathology of AD.","PeriodicalId":111070,"journal":{"name":"Amino Acids, Peptides and Proteins","volume":"1 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2019-05-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"130154852","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2019-05-09DOI: 10.1039/9781788013857-00001
B. Vértessy
Despite the simplistic general view of DNA being assembled by only four deoxynucleotides, non-canonical bases constitute a significant part of the genome and play an important role in epigenetics and other physiological processes. Uracil is among the most frequently occurring non-canonical base in DNA and in order to maintain normal cell function, proteins involved in uracil-DNA metabolism require an adequate set of specific binding sites that provide ample distinctive power for nucleobases. Here we present on overview of how this distinction is governed by molecular interactions between side chain and main chain atoms of the protein binding sites and the uracil base.
{"title":"Search and destroy: versatile proteins offer unique structural solutions against uracil in DNA","authors":"B. Vértessy","doi":"10.1039/9781788013857-00001","DOIUrl":"https://doi.org/10.1039/9781788013857-00001","url":null,"abstract":"Despite the simplistic general view of DNA being assembled by only four deoxynucleotides, non-canonical bases constitute a significant part of the genome and play an important role in epigenetics and other physiological processes. Uracil is among the most frequently occurring non-canonical base in DNA and in order to maintain normal cell function, proteins involved in uracil-DNA metabolism require an adequate set of specific binding sites that provide ample distinctive power for nucleobases. Here we present on overview of how this distinction is governed by molecular interactions between side chain and main chain atoms of the protein binding sites and the uracil base.","PeriodicalId":111070,"journal":{"name":"Amino Acids, Peptides and Proteins","volume":"28 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2019-05-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"123504871","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Amino Acids, Peptides and Proteins","authors":"S. Damodaran, K. Parkin","doi":"10.1201/9781315372914-6","DOIUrl":"https://doi.org/10.1201/9781315372914-6","url":null,"abstract":"","PeriodicalId":111070,"journal":{"name":"Amino Acids, Peptides and Proteins","volume":"13 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2017-05-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"132860847","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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