{"title":"通过基本亮氨酸拉链结构域构建用于植物基因转染的肽/质粒 DNA 复合物","authors":"Kota Nomura, Seiya Fujita, Yuki Shimatani, Taichi Kurita, Chonprakun Thagun, Naoya Abe, Kazusato Oikawa, Kousuke Tsuchiya, Hirotaka Uji, Keiji Numata","doi":"10.1038/s41428-024-00901-0","DOIUrl":null,"url":null,"abstract":"An important method for plant genetic modification is using peptide/pDNA complexes to transfer genes into plant cells. With conventional carrier peptides, the peptide sequence must contain a high amount of cationic amino acids to condense and introduce pDNA. As a result, the dissociation of pDNA from the complex is inefficient, often causing problems. Herein, we designed a new peptide carrier that mimics the basic leucine zipper (bZIP) domain of DNA-binding proteins, in which (LU)4 is the leucine zipper motif and (KUA)3 is the basic DNA-binding and cell-penetrating motif (U = α-aminoisobutyric acid). After (KUA)3-(LU)4 peptide was mixed with pDNA, DNA molecules were condensed to form nanoparticles of approximately 130 nm. Furthermore, when complexes of (KUA)3-(LU)4 peptide and pDNA were introduced into the leaves of Arabidopsis thaliana (A. thaliana), expression of the reporter protein was detected in the plant cells. Thus, (KUA)3-(LU)4 peptide that mimics the bZIP domain is a novel and efficient carrier for pDNA with high dissociation efficiency. A new peptide carrier that mimics the basic leucine zipper domain (bZIP) of DNA-binding proteins was designed, in which (LU)4 is the leucine zipper motif and (KUA)3 is the basic DNA-binding motif (U = α-aminoisobutyric acid). When mixed with pDNA, (KUA)3-(LU)4 peptide condensed DNA molecules to form nanoparticles. Furthermore, when complexes of the (KUA)3-(LU)4 peptide and pDNA were introduced into the leaves of Arabidopsis thaliana (A. thaliana), the reporter protein was expressed in plant cells. Thus, (KUA)3-(LU)4 is an efficient carrier of pDNA with high dissociation efficiency.","PeriodicalId":20302,"journal":{"name":"Polymer Journal","volume":null,"pages":null},"PeriodicalIF":2.3000,"publicationDate":"2024-03-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.com/articles/s41428-024-00901-0.pdf","citationCount":"0","resultStr":"{\"title\":\"Construction of peptide/plasmid DNA complexes for plant gene transfection via the basic leucine zipper domain\",\"authors\":\"Kota Nomura, Seiya Fujita, Yuki Shimatani, Taichi Kurita, Chonprakun Thagun, Naoya Abe, Kazusato Oikawa, Kousuke Tsuchiya, Hirotaka Uji, Keiji Numata\",\"doi\":\"10.1038/s41428-024-00901-0\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"An important method for plant genetic modification is using peptide/pDNA complexes to transfer genes into plant cells. With conventional carrier peptides, the peptide sequence must contain a high amount of cationic amino acids to condense and introduce pDNA. As a result, the dissociation of pDNA from the complex is inefficient, often causing problems. Herein, we designed a new peptide carrier that mimics the basic leucine zipper (bZIP) domain of DNA-binding proteins, in which (LU)4 is the leucine zipper motif and (KUA)3 is the basic DNA-binding and cell-penetrating motif (U = α-aminoisobutyric acid). After (KUA)3-(LU)4 peptide was mixed with pDNA, DNA molecules were condensed to form nanoparticles of approximately 130 nm. Furthermore, when complexes of (KUA)3-(LU)4 peptide and pDNA were introduced into the leaves of Arabidopsis thaliana (A. thaliana), expression of the reporter protein was detected in the plant cells. Thus, (KUA)3-(LU)4 peptide that mimics the bZIP domain is a novel and efficient carrier for pDNA with high dissociation efficiency. A new peptide carrier that mimics the basic leucine zipper domain (bZIP) of DNA-binding proteins was designed, in which (LU)4 is the leucine zipper motif and (KUA)3 is the basic DNA-binding motif (U = α-aminoisobutyric acid). When mixed with pDNA, (KUA)3-(LU)4 peptide condensed DNA molecules to form nanoparticles. Furthermore, when complexes of the (KUA)3-(LU)4 peptide and pDNA were introduced into the leaves of Arabidopsis thaliana (A. thaliana), the reporter protein was expressed in plant cells. Thus, (KUA)3-(LU)4 is an efficient carrier of pDNA with high dissociation efficiency.\",\"PeriodicalId\":20302,\"journal\":{\"name\":\"Polymer Journal\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":2.3000,\"publicationDate\":\"2024-03-05\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.nature.com/articles/s41428-024-00901-0.pdf\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Polymer Journal\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://www.nature.com/articles/s41428-024-00901-0\",\"RegionNum\":4,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"POLYMER SCIENCE\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Polymer Journal","FirstCategoryId":"92","ListUrlMain":"https://www.nature.com/articles/s41428-024-00901-0","RegionNum":4,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"POLYMER SCIENCE","Score":null,"Total":0}
Construction of peptide/plasmid DNA complexes for plant gene transfection via the basic leucine zipper domain
An important method for plant genetic modification is using peptide/pDNA complexes to transfer genes into plant cells. With conventional carrier peptides, the peptide sequence must contain a high amount of cationic amino acids to condense and introduce pDNA. As a result, the dissociation of pDNA from the complex is inefficient, often causing problems. Herein, we designed a new peptide carrier that mimics the basic leucine zipper (bZIP) domain of DNA-binding proteins, in which (LU)4 is the leucine zipper motif and (KUA)3 is the basic DNA-binding and cell-penetrating motif (U = α-aminoisobutyric acid). After (KUA)3-(LU)4 peptide was mixed with pDNA, DNA molecules were condensed to form nanoparticles of approximately 130 nm. Furthermore, when complexes of (KUA)3-(LU)4 peptide and pDNA were introduced into the leaves of Arabidopsis thaliana (A. thaliana), expression of the reporter protein was detected in the plant cells. Thus, (KUA)3-(LU)4 peptide that mimics the bZIP domain is a novel and efficient carrier for pDNA with high dissociation efficiency. A new peptide carrier that mimics the basic leucine zipper domain (bZIP) of DNA-binding proteins was designed, in which (LU)4 is the leucine zipper motif and (KUA)3 is the basic DNA-binding motif (U = α-aminoisobutyric acid). When mixed with pDNA, (KUA)3-(LU)4 peptide condensed DNA molecules to form nanoparticles. Furthermore, when complexes of the (KUA)3-(LU)4 peptide and pDNA were introduced into the leaves of Arabidopsis thaliana (A. thaliana), the reporter protein was expressed in plant cells. Thus, (KUA)3-(LU)4 is an efficient carrier of pDNA with high dissociation efficiency.
期刊介绍:
Polymer Journal promotes research from all aspects of polymer science from anywhere in the world and aims to provide an integrated platform for scientific communication that assists the advancement of polymer science and related fields. The journal publishes Original Articles, Notes, Short Communications and Reviews.
Subject areas and topics of particular interest within the journal''s scope include, but are not limited to, those listed below:
Polymer synthesis and reactions
Polymer structures
Physical properties of polymers
Polymer surface and interfaces
Functional polymers
Supramolecular polymers
Self-assembled materials
Biopolymers and bio-related polymer materials
Polymer engineering.