Nonionic Water-Soluble Oligo(ethylene glycol)-Modified Polypeptides with a β-Sheet Conformation.

التفاصيل البيبلوغرافية
العنوان:	Nonionic Water-Soluble Oligo(ethylene glycol)-Modified Polypeptides with a β-Sheet Conformation.
المؤلفون:	Jing X; Beijing National Laboratory for Molecular Sciences, Center for Soft Matter Science and Engineering, Key Laboratory of Polymer Chemistry and Physics of Ministry of Education, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China., Zhu Z; Changping Laboratory, Beijing 102200, China., Wang S; Beijing National Laboratory for Molecular Sciences, Center for Soft Matter Science and Engineering, Key Laboratory of Polymer Chemistry and Physics of Ministry of Education, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China., Xin J; Beijing National Laboratory for Molecular Sciences, Center for Soft Matter Science and Engineering, Key Laboratory of Polymer Chemistry and Physics of Ministry of Education, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China., Zhou H; Beijing National Laboratory for Molecular Sciences, Center for Soft Matter Science and Engineering, Key Laboratory of Polymer Chemistry and Physics of Ministry of Education, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China., Wang L; Beijing National Laboratory for Molecular Sciences, Center for Soft Matter Science and Engineering, Key Laboratory of Polymer Chemistry and Physics of Ministry of Education, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China., Tong H; Department of Instrument Analysis Center of Xi'an Jiaotong University, Xi'an 710049, China., Cui C; Department of Instrument Analysis Center of Xi'an Jiaotong University, Xi'an 710049, China., Zhang Y; Department of Applied Chemistry, School of Science, MOE Key Laboratory for Nonequilibrium Synthesis and Modulation of Condensed Matter (Xi'an Jiaotong University), Xi'an Key Laboratory of Sustainable Energy Materials Chemistry and State Key Laboratory for Mechanical Behavior of Materials, Xi'an Jiaotong University, Xi'an 710049, China., Sun F; Department of Chemical and Biological Engineering, the Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong 999077, China., Yang L; Beijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China., Gao Y; Beijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China.; Changping Laboratory, Beijing 102200, China., Lu H; Beijing National Laboratory for Molecular Sciences, Center for Soft Matter Science and Engineering, Key Laboratory of Polymer Chemistry and Physics of Ministry of Education, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China.
المصدر:	Biomacromolecules [Biomacromolecules] 2024 Aug 12; Vol. 25 (8), pp. 5343-5351. Date of Electronic Publication: 2024 Jul 13.
نوع المنشور:	Journal Article
اللغة:	English
بيانات الدورية:	Publisher: American Chemical Society Country of Publication: United States NLM ID: 100892849 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1526-4602 (Electronic) Linking ISSN: 15257797 NLM ISO Abbreviation: Biomacromolecules Subsets: MEDLINE
أسماء مطبوعة:	Original Publication: Washington, DC : American Chemical Society, c2000-
مواضيع طبية MeSH:	Peptides/chemistry , Solubility , Water/chemistry , Protein Conformation, beta-Strand, Polyethylene Glycols/chemistry ; Lysine/chemistry ; Hydrogels/chemistry ; Ethylene Glycol/chemistry ; Protein Structure, Secondary ; Polymerization
مستخلص:	The secondary structures of polypeptides, such as an α-helix and a β-sheet, often impart specific properties and functions, making the regulation of their secondary structures of great significance. Particularly, water-soluble polypeptides bearing a β-sheet conformation are rare and challenging to achieve. Here, a series of oligo(ethylene glycol)-modified lysine N -carboxylic anhydrides ( ^{EG m} K-NCA, where m = 1-3) and the corresponding polymers ^{EG m} K n are synthesized, with urethane bonds as the linker between the side-chain EG and lysine. The secondary structure of ^{EG m} K n is delicately regulated by both m and n , the length (number of repeating units) of EG and the degree of polymerization (DP), respectively. Among them, ^EG2 K n adopts a β-sheet conformation with good water solubility at an appropriate DP and forms physically cross-linked hydrogels at a concentration as low as 1 wt %. The secondary structures of ^EG1 K n can be tuned by DP, exhibiting either a β-sheet or an α-helix, whereas ^EG3 K n appears to a adopt pure and stable α-helix with no dependence on DP. Compared to previous works reporting EG-modified lysine-derived polypeptides bearing exclusively an α-helix conformation, this work highlights the important and unexpected role of the urethane connecting unit and provides useful case studies for understanding the secondary structure of polypeptides.
المشرفين على المادة:	0 (Peptides) 059QF0KO0R (Water) 3WJQ0SDW1A (Polyethylene Glycols) K3Z4F929H6 (Lysine) 0 (Hydrogels) FC72KVT52F (Ethylene Glycol)
تواريخ الأحداث:	Date Created: 20240713 Date Completed: 20240812 Latest Revision: 20240812
رمز التحديث:	20240813
DOI:	10.1021/acs.biomac.4c00759
PMID:	39001815
قاعدة البيانات:	MEDLINE

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تدمد:	1526-4602
DOI:	10.1021/acs.biomac.4c00759