{"title":"Electrostatic Regulation of Bola-Amphiphilic Peptide Self-Assembly and Nanotube Formation Induced by Salt Ions.","authors":"Danni Li, Yongyi Xu, Yingshan Li, Bin Dai","doi":"10.1021/acsabm.5c00199","DOIUrl":null,"url":null,"abstract":"<p><p>Peptide self-assembly into nanostructures offers substantial potential for applications in catalysis, drug delivery, and nanodevice fabrication. However, controlling the morphology of these assemblies remains a challenge. In this study, we investigate the role of salt ions in regulating the self-assembly of the bola-amphiphilic peptide KFFFFK, facilitating a transition from twisted fibrils to nanotubes. Using transmission electron microscopy, we show that the addition of NaCl induces the formation of nanotubes, and we detail the time-dependent assembly process. Increased salt concentrations reduce electrostatic repulsion, promoting the lateral merging of fibrils and supporting the formation of closed nanotubes. This phenomenon is also observed with several other salts. These findings underscore the critical role of electrostatic interactions in peptide self-assembly and highlight the importance of salt concentration in directing assembly pathways. Our results provide valuable insights into the mechanisms of peptide self-assembly and offer a versatile approach for designing advanced biomaterials and nanodevices based on well-defined peptide nanostructures.</p>","PeriodicalId":2,"journal":{"name":"ACS Applied Bio Materials","volume":" ","pages":"4065-4072"},"PeriodicalIF":4.6000,"publicationDate":"2025-05-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"ACS Applied Bio Materials","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1021/acsabm.5c00199","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2025/4/24 0:00:00","PubModel":"Epub","JCR":"Q2","JCRName":"MATERIALS SCIENCE, BIOMATERIALS","Score":null,"Total":0}
引用次数: 0
Abstract
Peptide self-assembly into nanostructures offers substantial potential for applications in catalysis, drug delivery, and nanodevice fabrication. However, controlling the morphology of these assemblies remains a challenge. In this study, we investigate the role of salt ions in regulating the self-assembly of the bola-amphiphilic peptide KFFFFK, facilitating a transition from twisted fibrils to nanotubes. Using transmission electron microscopy, we show that the addition of NaCl induces the formation of nanotubes, and we detail the time-dependent assembly process. Increased salt concentrations reduce electrostatic repulsion, promoting the lateral merging of fibrils and supporting the formation of closed nanotubes. This phenomenon is also observed with several other salts. These findings underscore the critical role of electrostatic interactions in peptide self-assembly and highlight the importance of salt concentration in directing assembly pathways. Our results provide valuable insights into the mechanisms of peptide self-assembly and offer a versatile approach for designing advanced biomaterials and nanodevices based on well-defined peptide nanostructures.
期刊介绍:
ACS Applied Bio Materials is an interdisciplinary journal publishing original research covering all aspects of biomaterials and biointerfaces including and beyond the traditional biosensing, biomedical and therapeutic applications.
The journal is devoted to reports of new and original experimental and theoretical research of an applied nature that integrates knowledge in the areas of materials, engineering, physics, bioscience, and chemistry into important bio applications. The journal is specifically interested in work that addresses the relationship between structure and function and assesses the stability and degradation of materials under relevant environmental and biological conditions.