Conversion of cationic amphiphilic lytic peptides to cell-penetration peptides
Conversion of cationic amphiphilic lytic peptides to cell-penetration peptides
复制标题
阳离子两亲性裂解肽转化为细胞渗透肽
DOI：
10.1002/pep2.24146
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发表时间：
2020
期刊：
影响因子：
2.4
通讯作者：
and Shiroh Futaki*
中科院分区：
文献类型：
--
作者：
Hao-Hsin Yu;Kentarou Sakamoto;Misao Akishiba;Naoki Tamemoto;Hisaaki Hirose;Ikuhiko Nakase;Miki Imanishi;Fatemeh Madani;Astrid Grslund;and Shiroh Futaki*
The 8th Peptide Engineering Meeting (PEM8) took place at the Harnack House in Berlin (Germany) from the 8th to 10th November 2018. Approximately 150 established scientists and young researchers from 19 different countries met and gave lectures, presented posters and discussed the latest findings in peptide and protein engineering. Meetings of the PEM series are international symposia that take place every 3 years alternately in North America, Europe and Asia. It is an established forum for topics relevant to chemists, biologists and other scientists in the fields of protein folding and materials science. In particular, concepts such as the structure-based design of peptides, peptide-protein interactions, peptide-membrane interactions, bioactive peptides and peptide-based materials are discussed. It also serves as an excellent platform for promoting international cooperation. Earlier meetings of this series took place in Osaka (Japan, 1997), Naples (Italy, 2000), Boston (USA, 2003), Yokohama (Japan, 2006), Barcelona (Spain, 2009), Atlanta (USA, 2012) and Pune (India, 2015). The next meeting of this series will take place in Boston (USA, 2021). Studying the secondary structure properties of new nonproteinogenic amino acids and their impact on peptide folding, as well as their application in the rational design of peptides has been, and continues to be, one of the main research directions of the peptide engineering community. As such, the demand for exchange and discussion of scientific ideas and results led to the PEM series. The incorporation of non-proteinogenic amino acids into peptides has developed into a general strategy in engineering of peptide-like drugs or peptidebased materials as these building blocks not only extend nature's toolbox but also show favorable impact on secondary structure, absorption of drugs and metabolic stability. For the first time, current topics in carbohydrate engineering became part of the lecture program. The issue opens with a Review by Haley I. Merritt et al. summarising contemporary methods for the design of stable secondary and tertiary peptide structures generated to enable selective binding to protein targets. Amino acid residues that are important for a certain recognition event are preorganised at these scaffolds such that efficient binding to the protein target is supported. Besides describing numerous methods for synthetic access to the desired stabilised secondary and tertiary peptide structure mimics, including α-helices, β-sheets, helical oligomers and nonregular loops, an impressive and very useful list with examples of protein-protein complexes that have been successfully targeted with these mimics is provided at the end of the piece. Indeed, the Review describes one of the main endeavors of peptide and protein engineers over the past 50 years: the understanding, generation and application of peptide structures with defined folding properties. The second Review, by Martina Delbianco and Peter H. Seeberger, is dedicated to the latest subject added to the symposia: reflecting the state of research in the field of helical folding of polysaccharides. In analogy to polypeptides and polynucleotides, helical folding is one of the major secondary structures that polysaccharides adopt. However, determination of the conformation of polysaccharides in solution remains, in most cases, elusive because of their intrinsic complexity and lack of adequate analytical techniques. The Review discusses the various helical shapes adopted by polysaccharides, includes methodologies that are used to tune polysaccharides' conformation, and describes the generation of tailor-made probes for structural studies, with the aim to …
