Molecular hierarchic conformations of peptide fibrils with polar growth mechanism by dynamically mapping ionic charge carriers | Research Square window.SnipcartSettings = { analytics: { enabled: false } }; (function() { var accessVector = localStorage.getItem('access_vector') || ''; window.dataLayer = window.dataLayer || []; if (accessVector) { window.dataLayer.push({ user: { profile: { profileInfo: { snid: accessVector } } } }); } })(); (function(w,d,s,l,i){w[l]=w[l]||[];w[l].push({'gtm.start':new Date().getTime(),event:'gtm.js'});var f=d.getElementsByTagName(s)[0],j=d.createElement(s),dl=l!='dataLayer'?'&l='+l:'';j.async=true;j.src='https://www.googletagmanager.com/gtm.js?id='+i+dl;f.parentNode.insertBefore(j,f);})(window,document,'script','dataLayer','GTM-K279D39R'); Browse Preprints In Review Journals COVID-19 Preprints AJE Video Bytes Research Tools Research Promotion AJE Professional Editing AJE Rubriq About Preprint Platform In Review Editorial Policies Our Team Advisory Board Help Center Sign In Submit a Preprint Cite Share Download PDF Article Molecular hierarchic conformations of peptide fibrils with polar growth mechanism by dynamically mapping ionic charge carriers Linhao Sun, Ayhan Yurtsever, Takeshi Fukuma, Shinji Watanabe This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-6702722/v1 This work is licensed under a CC BY 4.0 License Status: Posted Version 1 posted You are reading this latest preprint version Abstract Harness of surface charge has been widely found in materials functionalization, life-related bioactivities and chemical reactions. Specifically, ionic charge carriers (ICC), it plays a key role in bio-nano coupling interfaces such as protein corona phenomenon. However, in thermodynamics and kinetic conditions, understanding the roles of ICC at bio-nano interfaces affecting biomolecular conformations, systematic energy landscapes, and on-demand bio-nano-functions is still a challenge task, lacking direct visualization of ICC and dynamically revealing its specific effect on surface characteristics of bio-nano interactions. We utilized high-speed ion conductance microscopy combined with high-resolution AFM techniques and peptide self-assembly on mica as a good model to explore significant roles of ICC in 1) differing peptide hierarchic conformations including amorphous and ordered phases in dynamics, 2) unveiling asymmetrical polar growth mechanism and 3) bias-modulated assembly-disassembly reversible process at peptide-mica interfaces. This work sheds light on quantifying the significant role of ICC at bio-nano hybrid soft interfaces. Biological sciences/Biotechnology/Nanobiotechnology/Biosensors Physical sciences/Chemistry/Biochemistry/Peptides Biological sciences/Biological techniques/Electrophysiology/Voltage clamp Biological sciences/Biotechnology/Nanobiotechnology/Nanofabrication and nanopatterning Biological sciences/Biotechnology/Nanobiotechnology/Nanopores Full Text Additional Declarations There is NO Competing Interest. Supplementary Files Supplementarymaterials.pdf Cite Share Download PDF Status: Posted Version 1 posted You are reading this latest preprint version Research Square lets you share your work early, gain feedback from the community, and start making changes to your manuscript prior to peer review in a journal. As a division of Research Square Company, we’re committed to making research communication faster, fairer, and more useful. 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