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Interactions of Zoospores of Ulva linza with Arginine-Rich Oligopeptide Monolayers
Linköping University, Department of Physics, Chemistry and Biology, Sensor Science and Molecular Physics. Linköping University, The Institute of Technology.ORCID iD: 0000-0002-1639-5735
University of Birmingham.
Linköping University, Department of Physics, Chemistry and Biology, Sensor Science and Molecular Physics. Linköping University, The Institute of Technology.
Linköping University, Department of Physics, Chemistry and Biology, Molecular Physics. Linköping University, Faculty of Science & Engineering.
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2009 (English)In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 25, no 16, 9375-9383 p.Article in journal (Refereed) Published
Abstract [en]

We recently reported oil the strong interactions of zoospores of the green alga, Ulva linza with all arginine-rich oligopeptide self-assembled monolayer (SAM) [Biofouling 2008, 24, 303-312], where the arginine-rich peptide induced not only high spore settlement, but also a form of abnormal settlement, or "pseudo-settlement", whereby it proportion of spores do not go through the normal process of surface exploration, adhesive exocytosis, and loss of flagella. Further. it was demonstrated that both the total number of settled spores and the fraction of pseudosettled spores were related to the surface density of the arginine-rich peptide. Here we present a further investigation of the interactions of zoospores of ulva with a set of oligomeric, de nom designed, arginine-rich peptides, specifically aimed to test the effect of peptide primary structure on the interaction. Via variations in the peptide length and by permutations in the amino acid sequences, we gain further insight into the spore-surface interactions. The interpretation of the biological assays is supported by physicochemical characterization of the SAMs using infrared spectroscopy, ellipsometry, and contact angle measurement. Results confirm the importance of arginine residues for the anomalous pseudosettlement, and we found that settlement is modulated by variations in both the total length and peptide primary structure. To elucidate the Causes of the anomalous settlement and the possible relation to peptide-membrane interactions, we also compared the settlement of the "naked" zoospores of Ulva(which present it lipoprotein membrane to the exterior without a discrete polysaccharide cell wall), with the settlement of diatoms (unicellular algae that are surrounded by it silica cell wall), onto the peptide SAMs. Cationic SAMs do not notably affect settlement (attachment), adhesion strength, or viability of diatom cells, Suggesting that the effect of the peptides on zoospores of Ulva is mediated via specific peptide-membrane interactions.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2009. Vol. 25, no 16, 9375-9383 p.
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:liu:diva-19996DOI: 10.1021/la900688gOAI: oai:DiVA.org:liu-19996DiVA: diva2:232446
Note

The previous status of this article was Manuscript.

Available from: 2009-08-24 Created: 2009-08-24 Last updated: 2017-12-13Bibliographically approved
In thesis
1. Structural and Functional Studies of De Novo Designed Peptides at Surfaces
Open this publication in new window or tab >>Structural and Functional Studies of De Novo Designed Peptides at Surfaces
2008 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

The work presented in this thesis deals with the structural and functional properties of peptides at surfaces. The interaction of peptides with surfaces is an ever so common occurrence in our every day life, from the bug squashed on the windshield of our car to the barnacle on our boat, and from the blood plasma used in the hospital to the proteins in our cells. The effect these occurrences has on our lives is diverse, the bug is annoying whereas the barnacle settlement of ship hull is costly for marine transportation, the blood plasma contains components of vital importance for our immunological defense system and the proteins in our cells are crucial for regulatory processes and life.One part of this thesis, performed as a part of the EU-founded project AMBIO, deals with the concept of marine biofouling. A number of short peptides have been designed, synthesized, and used to investigate their effect on the settlement on marine biofoulers, such as the Ulva linza algae and the Navicula diatom, on template surfaces coated with thin layers of these molecules. The surfaces have been thoroughly investigated with respect of their physio-chemical properties before and after submersion in artificial seawater and ultimately in suspensions containing the organisms. The most interesting results were obtained with an arginine-rich peptide coating that when introduced to Ulva linza zoospores, displayed extensive settlement, compared to reference surfaces. In addition, a large fraction of the settled spores had an abnormal morphology.The other part of this thesis is focused on designed peptides that when adsorbed on a negatively charged surface adopts a well-defined secondary structure, either α-helical or β-sheet. Precisely placed amino acids in the peptides will strongly disfavor structure in solution, primarily due to electrostatic repulsion, but when the peptides are adsorbed on the negatively charged surfaces, they adopt a well-defined secondary structure due to ion pair bonding. These interactions have been thoroughly investigated by systematic variations of the side-chains. In order to determine the factors contributing to the induced structure, several peptides with different amino acid sequences have been synthesized. Factors that have been investigated include 1) the positive charge density, 2) distribution of positive charges, 3) negative charge density, 4) increasing hydrophobicity, and 5) incorporating amino acids with different helix propensities. Moreover, pH dependence and the effect of different interaction partners have also been investigated. It has also been shown that the system can be modified to incorporate a catalytic site that is only active when the helix is formed. This research will increase our understanding of peptide-surface interactions and might be of importance for both bionanotechnology and medicine.

Place, publisher, year, edition, pages
Linköping: Linköping University Electronic Press, 2008. 52 p.
Series
Linköping Studies in Science and Technology. Dissertations, ISSN 0345-7524 ; 1199
Keyword
Biofouling, vesicles, nanoparticles, peptide, peptide design, circular dichroism
National Category
Physical Chemistry
Identifiers
urn:nbn:se:liu:diva-15022 (URN)978-91-7393-840-2 (ISBN)
Public defence
2008-09-05, Planck, Campus Valla, Linköpings universitet, Linköping, 10:15 (English)
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Available from: 2008-10-09 Created: 2008-10-09 Last updated: 2017-01-11Bibliographically approved

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Ederth, ThomasNygren, PatrikDu, Chun-XiaEkblad, TobiasZhou, YeFalk, MagnusLiedberg, Bo

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