兰州大学机构库
Tryptic Stability and Antimicrobial Activity of the Derivatives of Polybia-CP with Fine-Tuning Modification in the Side Chain of Lysine
Jia, Fengjing1; Liang, Xiaolei2; Wang, Jiayi1; Zhang, Lishi1; Zhou, Jingjing1; He, Yuhang1; Zhang, Fangfang2; Yan, WJ(阎文锦)1; Wang, KR(王凯荣)1
2020-11-25
Online publication date2020-11
Source PublicationInternational Journal of Peptide Research and Therapeutics   Impact Factor & Quartile Of Published Year  The Latest Impact Factor & Quartile
ISSN1573-3149
EISSN1573-3904
Volume27Issue:2Pages:851-862
page numbers12
AbstractAntimicrobial peptides (AMPs) were believed to be a class of promising antimicrobials to combat the increasing resistant microbes. However, AMPs could be easily degraded by endogenous proteases, which limited their clinic use. Considering that lysine is the only one cationic amino acid residue in polybia-CP which were related to the cleavage of trypsin like serine protease's digestion, we introduced lysine's mimics which kept the key function group side chain -NH2 and only varied the methylene chains in the sequence of polybia-CP to investigate the effect of the introduction of non-proteinogenic amino acids on the activity and stability of antimicrobial peptides. In addition, two analogs in which lysine were substituted by the other two proteinogenic cationic amino acids arginine and histidine also were synthesized to evaluate the effect of fine tuning the function group in lysine on its antimicrobial activity and stability. We found that the introduction of amino acids with shortened side chain length of lysine could enhance the trypsin resistance of the derivatives of polybia-CP, while maintain the same or comparable antimicrobial activity with the parent peptide. In addition, while lysine was substituted by histidine, His-CP demonstrated comparable antimicrobial activity and dramatically improved trypsin resistance. Although the analog exhibited excellent antimicrobial activity while lysine was substituted by Arginine residue (Arg-CP), its enzymatic stability was almost the same as its parent peptide. These results suggest that the fine-tuning of side chain of lysine may offer a promising strategy to improve the tryptic stability and retain the antimicrobial activity of antimicrobial peptide.
KeywordCationic antimicrobial peptide Polybia-CP Tryptic stability Fine-tuning of side chain
PublisherSPRINGER
DOI10.1007/s10989-020-10129-0
Indexed BySCIE
Language英语
Funding ProjectNational Natural Science Foundation of China[82073679][81872723][81601351] ; CAMS Innovation Fund for Medical Sciences (CIFMS)[2019-12M-5-074] ; Natural Science Foundation of Gansu Province, China[20JR5RA245] ; Fundamental Research Funds for the Central Universities[lzujbky-2020- kb13]
WOS Research AreaBiochemistry & Molecular Biology
WOS SubjectBiochemistry & Molecular Biology
WOS IDWOS:000592523600002
PublisherSPRINGER
Original Document TypeArticle
Citation statistics
Document Type期刊论文
Identifierhttps://ir.lzu.edu.cn/handle/262010/441468
Collection兰州大学
基础医学院
Corresponding AuthorYan, Wenjin; Wang, Kairong
Affiliation
1.Lanzhou Univ, Chinese Acad Med Sci, Inst Biochem & Mol Biol,Res Unit Peptide Sci, Sch Basic Med Sci,Key Lab Preclin Study New Drugs, 2019RU066, Lanzhou, Peoples R China
2.Lanzhou Univ, Hosp Lanzhou Univ 1, Dept Gynecol, Key Lab Gynecol Oncol Gansu Prov, Lanzhou, Peoples R China
First Author AffilicationSchool of Basic Medical Sciences
Corresponding Author AffilicationSchool of Basic Medical Sciences
First Signature AffilicationSchool of Basic Medical Sciences
Recommended Citation
GB/T 7714
Jia, Fengjing,Liang, Xiaolei,Wang, Jiayi,et al. Tryptic Stability and Antimicrobial Activity of the Derivatives of Polybia-CP with Fine-Tuning Modification in the Side Chain of Lysine[J]. International Journal of Peptide Research and Therapeutics,2020,27(2):851-862.
APA Jia, Fengjing.,Liang, Xiaolei.,Wang, Jiayi.,Zhang, Lishi.,Zhou, Jingjing.,...&Wang, Kairong.(2020).Tryptic Stability and Antimicrobial Activity of the Derivatives of Polybia-CP with Fine-Tuning Modification in the Side Chain of Lysine.International Journal of Peptide Research and Therapeutics,27(2),851-862.
MLA Jia, Fengjing,et al."Tryptic Stability and Antimicrobial Activity of the Derivatives of Polybia-CP with Fine-Tuning Modification in the Side Chain of Lysine".International Journal of Peptide Research and Therapeutics 27.2(2020):851-862.
Related Services
Recommend this item
Bookmark
Usage statistics
Export to Endnote
Altmetrics Score
Google Scholar
Similar articles in Google Scholar
[Jia, Fengjing]'s Articles
[Liang, Xiaolei]'s Articles
[Wang, Jiayi]'s Articles
Baidu academic
Similar articles in Baidu academic
[Jia, Fengjing]'s Articles
[Liang, Xiaolei]'s Articles
[Wang, Jiayi]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[Jia, Fengjing]'s Articles
[Liang, Xiaolei]'s Articles
[Wang, Jiayi]'s Articles
Terms of Use
No data!
Social Bookmark/Share
File name: Jia-2021-Tryptic Stability and Antimicrobial A.pdf
Format: Adobe PDF
No comment.
Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.