{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T00:59:00Z","timestamp":1760144340155,"version":"build-2065373602"},"reference-count":34,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2024,4,11]],"date-time":"2024-04-11T00:00:00Z","timestamp":1712793600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Bioengineering"],"abstract":"<jats:p>We have investigated the morphology of two-dimensional monolayers of gramicidin-D (GD) and alamethicin (Al) formed on the water surface by the dropping method (DM) using surface tension measurement (STm), Brewster angle microscopy (BAM), and atomic force microscopy (AFM). Dynamic light scattering (DLS) revealed that GD in alcoholic solutions formed a dimeric helical structure. According to the CD and NMR spectroscopies, GD molecules existed in dimer form in methanol and lipid membrane environments. The STm results and BAM images revealed that the GD dimer monolayer was in a liquid expanded (LE) state, whereas the Al monolayer was in a liquid condensed (LC) state. The limiting molecular area (A0) was 6.2 \u00b1 0.5 nm2 for the GD-dimer and 3.6 \u00b1 0.5 nm2 for the Al molecule. The AFM images also showed that the molecular long axes of both the GD-dimer and Al were horizontal to the water surface. The stability of each monolayer was confirmed by the time dependence of the surface pressure (\u03c0) observed using the STm method. The DM monolayer preparation method for GD-dimer and Al peptide molecules is a useful technique for revealing how the model biological membrane\u2019s components assemble in two dimensions on the water surface.<\/jats:p>","DOI":"10.3390\/bioengineering11040366","type":"journal-article","created":{"date-parts":[[2024,4,12]],"date-time":"2024-04-12T03:34:37Z","timestamp":1712892877000},"page":"366","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Morphology Observation of Two-Dimensional Monolayers of Model Proteins on Water Surface as Revealed by Dropping Method"],"prefix":"10.3390","volume":"11","author":[{"given":"Yukie","family":"Asada","sequence":"first","affiliation":[{"name":"Department of Life Science and Applied Chemistry, Graduate School of Engineering, Nagoya Institute of Technology, Nagoya 466-8555, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shinya","family":"Tanaka","sequence":"additional","affiliation":[{"name":"Department of Life Science and Applied Chemistry, Graduate School of Engineering, Nagoya Institute of Technology, Nagoya 466-8555, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hirotaka","family":"Nagano","sequence":"additional","affiliation":[{"name":"Department of Life Science and Applied Chemistry, Graduate School of Engineering, Nagoya Institute of Technology, Nagoya 466-8555, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hiroki","family":"Noguchi","sequence":"additional","affiliation":[{"name":"Department of Life Science and Applied Chemistry, Graduate School of Engineering, Nagoya Institute of Technology, Nagoya 466-8555, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Akihiro","family":"Yoshino","sequence":"additional","affiliation":[{"name":"Department of Life Science and Applied Chemistry, Graduate School of Engineering, Nagoya Institute of Technology, Nagoya 466-8555, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Keijiro","family":"Taga","sequence":"additional","affiliation":[{"name":"Department of Life Science and Applied Chemistry, Graduate School of Engineering, Nagoya Institute of Technology, Nagoya 466-8555, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yasushi","family":"Yamamoto","sequence":"additional","affiliation":[{"name":"Department of Life Science and Applied Chemistry, Graduate School of Engineering, Nagoya Institute of Technology, Nagoya 466-8555, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3292-8335","authenticated-orcid":false,"given":"Zameer","family":"Shervani","sequence":"additional","affiliation":[{"name":"Food & Energy Security Research & Product Centre, Sendai 980-0871, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2024,4,11]]},"reference":[{"key":"ref_1","unstructured":"Shimabayashi, S., Terada, H., and Okabayashi, H. (1990). Biocolloid 1&2, Hirokawa Publishing."},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Gennis, R.B. (1990). Biomembrane, Molecular Structure and Function, Springer.","DOI":"10.1007\/978-1-4757-2065-5"},{"key":"ref_3","unstructured":"Hatta, I., and Murata, M. (2000). Dynamics of Biomembrane, Kyoritsu Shuppan Co., Ltd."},{"key":"ref_4","unstructured":"Nelson, D.L., and Cox, M.M. (2017). Lehninger Principles of Biochemistry, 7th ed, WH Freeman."},{"key":"ref_5","unstructured":"Nakamura, H., and Arisaka, F. (1999). Protein Shape and Properties, Kyoritsu Shuppan, Co. Ltd."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"2011","DOI":"10.1021\/ja01087a027","article-title":"The Structure of Valine- and Isoleucine-Gramicidin A","volume":"87","author":"Sarges","year":"1965","journal-title":"J. Am. Chem. Soc."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"7413","DOI":"10.1074\/jbc.M309658200","article-title":"The Linear Pentadecapeptide Gramicidin Is Assembled by Four Multimodular Nonribosomal Peptide Synthetases That Comprise 16 Modules with 56 Catalytic Domains","volume":"279","author":"Kessler","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1757","DOI":"10.1016\/j.bpj.2017.08.049","article-title":"Exchange of Gramicidin between Lipid Bilayers: Implications for the Mechanism of Channel Formation","volume":"113","author":"Lum","year":"2017","journal-title":"Biophys. J."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1038\/217713a0","article-title":"Action Potentials Induced in Biomolecular Lipid Membranes","volume":"217","author":"Mueller","year":"1968","journal-title":"Nature"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1027","DOI":"10.1002\/cbdv.200790095","article-title":"The History of Alamethicin: A Review of the Most Extensively Studied Peptaibol","volume":"4","author":"Balazs","year":"2007","journal-title":"Chem. Biodiv."},{"key":"ref_11","unstructured":"Kawai, T. (2005). Interfaces and Surfactants\u2014Fundamentals and Applications, Japan Oil Chemists\u2019 Society."},{"key":"ref_12","unstructured":"Suezaki, Y. (2007). Physics of Lipid Membrane, Kyusyu University Press."},{"key":"ref_13","first-page":"36","article-title":"Lipid monolayer and interaction with anesthetics","volume":"1","author":"Yamamoto","year":"2016","journal-title":"Encycl. Biocol. Bioint. Sc."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"115","DOI":"10.4236\/jbpc.2013.44016","article-title":"Morphology observation of dipalmitoyl phosphatidyl choline (DPPC) monolayer on water surface by dropping method","volume":"4","author":"Yoshida","year":"2013","journal-title":"J. Biophys. Chem."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"98","DOI":"10.4236\/jbpc.2016.74009","article-title":"Morphological Observation of Specific Condensation Effect of Cholesterol on Dipalmitoyl Phosphatidyl Choline (DPPC) Monolayer by Dropping Method","volume":"7","author":"Yokoyama","year":"2016","journal-title":"J. Biophys. Chem."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"15","DOI":"10.4236\/jbpc.2019.102002","article-title":"Structural Change in Dimyristoyl Phosphatidyl Choline (DMPC) Molecule Alkyl Chains on the Addition of Cholesterol to DMPC Monolayer: Specific Addition Effect of Cholesterol","volume":"10","author":"Ito","year":"2019","journal-title":"J. Biophys. Chem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"52","DOI":"10.24018\/ejchem.2022.3.1.79","article-title":"Morphological Behavior of DPPC-DMPC Two-dimensional Mixed Monolayer on Water Surface by Dropping Method","volume":"3","author":"Watanabe","year":"2022","journal-title":"Eur. J. Adv. Chem. Res."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"39","DOI":"10.4236\/jbpc.2017.84004","article-title":"Surface Properties of Novel Surfactant, Dihexadecyl Gemini Phosphate, Monolayers on Water Surface by Dropping Method","volume":"8","author":"Kobayashi","year":"2017","journal-title":"J. Biophys. Chem."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/0040-6090(94)90534-7","article-title":"Transition to three-dimensional structures in monolayers of a series of long-chain acids on the water surface by compression studied by transmission electron microscopy and atomic force microscopy","volume":"242","author":"Kato","year":"1994","journal-title":"Thin Solid Film."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1002\/(SICI)1097-0282(199712)42:7<771::AID-BIP3>3.0.CO;2-Q","article-title":"Solvent Effects on the Conformation and Far UV CD Spectra of Gramicidin","volume":"42","author":"Chen","year":"1997","journal-title":"Bipolymers"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/j.bbamem.2013.10.011","article-title":"Importance of indole N-H hydrogen bonding in the organization and dynamics of gramicidin channels","volume":"1838","author":"Chaudhuri","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"6994","DOI":"10.1021\/bi00527a033","article-title":"Solution Dimensions of the Gramicidin Dimer by Dynamic Light Scattering","volume":"20","author":"Michielsent","year":"1981","journal-title":"Biochemistry"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1016\/S0006-3495(86)83642-6","article-title":"Structure of gramicidin A","volume":"49","author":"Wallace","year":"1986","journal-title":"Biophys. J."},{"key":"ref_24","first-page":"327","article-title":"The dynamic nature of gramicidin. Biomembr. A Multi-Vol. Treatise Transmembrane Recept","volume":"6","author":"Doyle","year":"1997","journal-title":"Channels"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1393","DOI":"10.1016\/j.bbamem.2006.03.002","article-title":"Investigations of antimicrobial peptides in planar film systems","volume":"1758","author":"Volinsky","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1042\/bj1170757","article-title":"The Primary Structure of Alamethicin","volume":"117","author":"Payne","year":"1970","journal-title":"Biochem. J."},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Czernek, J., and Brus, J. (2021). Modeling the Structure of Crystalline Alamethicin and Its NMR Chemical Shift Tensors. Antibiotics, 10.","DOI":"10.3390\/antibiotics10101265"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"2789","DOI":"10.1016\/j.bbamem.2015.07.019","article-title":"Structure and orientation of antibiotic peptide Alamethicin in phospholipid bilayers as revealed by chemical shift oscillation analysis of solid state nuclear magnetic resonance and molecular dynamics simulation","volume":"1848","author":"Nagano","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"11084","DOI":"10.1021\/la0477486","article-title":"Microscopic Visualization of Alamethicin Incorporation into Model Membrane Monolayers","volume":"20","author":"Volinsky","year":"2004","journal-title":"Langmuir"},{"key":"ref_30","unstructured":"Gaines, G.L. (1966). Insoluble Monolayers at Liquid-Gas Interface, Interscience Publishers."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"9474","DOI":"10.1021\/jp101668n","article-title":"Grazing Incidence Diffraction and X-ray Reflectivity Studies of the Interactions of Inorganic Mercury Salts with Membrane Lipids in Langmuir Monolayers at the Air\/Water Interface","volume":"114","author":"Broniatowski","year":"2010","journal-title":"J. Phys. Chem. B"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"9086","DOI":"10.1021\/acs.langmuir.5b01775","article-title":"Detailed Analysis of the Surface Area and Elasticity in the Saturated 1,2-Diacylphosphatidylcholine\/Cholesterol Binary Monolayer System","volume":"31","author":"Miyoshi","year":"2015","journal-title":"Langmuir"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/j.bbamem.2015.11.025","article-title":"Biophysical characterization of monofilm model systems composed of selected tear film phospholipids","volume":"1858","author":"Patterson","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1007\/s10450-019-00117-2","article-title":"Properties of the Langmuir and Langmuir-Blodgett monolayers of cholesterol-cyclosporine A on water and polymer support","volume":"25","author":"Przykaza","year":"2019","journal-title":"Adsorption"}],"container-title":["Bioengineering"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2306-5354\/11\/4\/366\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T14:26:36Z","timestamp":1760106396000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2306-5354\/11\/4\/366"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,4,11]]},"references-count":34,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2024,4]]}},"alternative-id":["bioengineering11040366"],"URL":"https:\/\/doi.org\/10.3390\/bioengineering11040366","relation":{},"ISSN":["2306-5354"],"issn-type":[{"type":"electronic","value":"2306-5354"}],"subject":[],"published":{"date-parts":[[2024,4,11]]}}}