R. Miller , S. Treppo , A. Voigt , W. Zingg , A.W. Neumann
{"title":"Contact angle kinetics of human albumin solutions at solid surfaces","authors":"R. Miller , S. Treppo , A. Voigt , W. Zingg , A.W. Neumann","doi":"10.1016/0166-6622(93)80001-V","DOIUrl":null,"url":null,"abstract":"<div><p>Contact angle kinetics of sessile drops of albumin solution on hydrophilic acetal and hydrophobic FC 721 surfaces were measured using axisymmetric drop shape analysis. Young's equation is used to calculate the solid/liquid interfacial tension from measured contact angles and surface tensions as a function of time. The change in solid/liquid interfacial tension is a result of protein adsorption. It indicates that at the hydrophilic acetal surface the albumin molecules, interact only weakly, whereas the interaction with the hydrophobic FC 721 surface is quite strong.</p></div>","PeriodicalId":10488,"journal":{"name":"Colloids and Surfaces","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1993-01-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0166-6622(93)80001-V","citationCount":"33","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Colloids and Surfaces","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/016666229380001V","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 33
Abstract
Contact angle kinetics of sessile drops of albumin solution on hydrophilic acetal and hydrophobic FC 721 surfaces were measured using axisymmetric drop shape analysis. Young's equation is used to calculate the solid/liquid interfacial tension from measured contact angles and surface tensions as a function of time. The change in solid/liquid interfacial tension is a result of protein adsorption. It indicates that at the hydrophilic acetal surface the albumin molecules, interact only weakly, whereas the interaction with the hydrophobic FC 721 surface is quite strong.
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