Molecular interactions between DOPA and surfaces with different functional groups: a chemical force microscopy study. Issue 52 (26th June 2017)
- Record Type:
- Journal Article
- Title:
- Molecular interactions between DOPA and surfaces with different functional groups: a chemical force microscopy study. Issue 52 (26th June 2017)
- Main Title:
- Molecular interactions between DOPA and surfaces with different functional groups: a chemical force microscopy study
- Authors:
- Zhang, Wei
Yang, Hui
Liu, Fanghui
Chen, Ting
Hu, Guangxin
Guo, Donghong
Hou, Qingfeng
Wu, Xu
Su, Yu
Wang, Jinben - Abstract:
- Abstract : The adhesion of mussel foot proteins (Mfps) to a variety of surfaces has been widely investigated, but the mechanisms behind the mussel adhesion to surfaces with different properties are far from being understood. Abstract : The adhesion of mussel foot proteins (Mfps) to a variety of surfaces has been widely investigated, but the mechanisms behind the mussel adhesion to surfaces with different properties are far from being understood. Most of Mfps contain a significant amount of 3, 4-dihydroxyphenylalanine (DOPA) which is considered to be responsible for the strong wet adhesion. In the present work, self-assembled monolayers (SAMs) were prepared as a series of model surfaces with variable functional groups. DOPA-surface interactions were investigated using chemical force microscopy (CFM) for the first time, in which an atomic force microscope (AFM) tip was chemically modified with DOPA terminated groups. The ability of DOPA to adhere to different surfaces with variable wettability was compared, showing that DOPA behaves with the strongest and weakest adhesion to C6 H5 - and OH-terminated surfaces, respectively. The interaction strength of DOPA at different surfaces does not always increase with the increase of surface wettability, because the hydrophobic interaction does not play a decisive role in DOPA adhering to surfaces. By the use of classical and extended Derjaguin–Landau–Verwey–Overbeek (DLVO) theories, the contribution of non-DLVO forces was isolated. WeAbstract : The adhesion of mussel foot proteins (Mfps) to a variety of surfaces has been widely investigated, but the mechanisms behind the mussel adhesion to surfaces with different properties are far from being understood. Abstract : The adhesion of mussel foot proteins (Mfps) to a variety of surfaces has been widely investigated, but the mechanisms behind the mussel adhesion to surfaces with different properties are far from being understood. Most of Mfps contain a significant amount of 3, 4-dihydroxyphenylalanine (DOPA) which is considered to be responsible for the strong wet adhesion. In the present work, self-assembled monolayers (SAMs) were prepared as a series of model surfaces with variable functional groups. DOPA-surface interactions were investigated using chemical force microscopy (CFM) for the first time, in which an atomic force microscope (AFM) tip was chemically modified with DOPA terminated groups. The ability of DOPA to adhere to different surfaces with variable wettability was compared, showing that DOPA behaves with the strongest and weakest adhesion to C6 H5 - and OH-terminated surfaces, respectively. The interaction strength of DOPA at different surfaces does not always increase with the increase of surface wettability, because the hydrophobic interaction does not play a decisive role in DOPA adhering to surfaces. By the use of classical and extended Derjaguin–Landau–Verwey–Overbeek (DLVO) theories, the contribution of non-DLVO forces was isolated. We found out DOPA can adhere to each surface functional group, since DOPA residues containing o -hydroxy or aromatic rings alone can control the adhesion process, and the aromatic ring is oriented perpendicularly or parallel to the surface. This study served as a basis for understanding the relationship between DOPA adhesion mechanisms and different wet surfaces, representing important concepts for the design of bioadhesive materials and anti-adhesion surfaces. … (more)
- Is Part Of:
- RSC advances. Volume 7:Issue 52(2017)
- Journal:
- RSC advances
- Issue:
- Volume 7:Issue 52(2017)
- Issue Display:
- Volume 7, Issue 52 (2017)
- Year:
- 2017
- Volume:
- 7
- Issue:
- 52
- Issue Sort Value:
- 2017-0007-0052-0000
- Page Start:
- 32518
- Page End:
- 32527
- Publication Date:
- 2017-06-26
- Subjects:
- Chemistry -- Periodicals
540.5 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/RA ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c7ra04228k ↗
- Languages:
- English
- ISSNs:
- 2046-2069
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8036.750300
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 643.xml