Zobrazeno 1 - 10
of 221
pro vyhledávání: '"Hans G. Börner"'
Autor:
Britta Seidt, Valeria Samsoninkova, Felix Hanßke, André Gjardy, Peter Fratzl, Hans G. Börner, Wolfgang Wagermaier
Publikováno v:
Frontiers in Materials, Vol 6 (2020)
In this study, a bio-inspired hybrid material is investigated by in situ X-ray scattering experiments in combination with mechanical tensile testing. The material is composed of nanometer-sized spherical magnesium fluoride particles which are linked
Externí odkaz:
https://doaj.org/article/5b7036321d5b4280a672181ef431e82b
Autor:
Jana M. Krüger, Ching-Yi Choi, Francisco Lossada, Peng Wang, Oliver Löschke, Dietmar Auhl, Hans G. Börner
Publikováno v:
Macromolecules. 55:989-1002
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2e29a0705c619cf99283f5470990e301
https://doi.org/10.1021/acs.macromol.1c02192
https://doi.org/10.1021/acs.macromol.1c02192
Autor:
Hans G. Börner, Jana M. Krüger
Publikováno v:
Angewandte Chemie. 133:6479-6484
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cd603d35a743425316d9207c1999bd4b
https://doi.org/10.1002/ange.202015833
https://doi.org/10.1002/ange.202015833
Publikováno v:
Soft Matter
A His-rich domain of preCollagen-D found in byssal threads is derivatized with Cys and Dopa flanks to allow for mussel-inspired polymerization. Artificial mussel glue proteins are accessed that combine cysteinyldopa for adhesion with sequences for pH
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4fb6472eee89199d167ae52b4d5f11f
https://doi.org/10.1039/d0sm02118k
https://doi.org/10.1039/d0sm02118k
Publikováno v:
ACS macro letters. 9(2)
Using peptide sequences for the design of functional peptoids is demonstrated for a peptide-based formulation additive that was specifically tailored to solubilize the photosensitizer meta-tetra(hy...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cf49bf0ed6ed60061c52dad4b29bd09
https://pubmed.ncbi.nlm.nih.gov/35638686
https://pubmed.ncbi.nlm.nih.gov/35638686
Publikováno v:
ACS macro letters. 5(5)
Protease activable antifouling coatings based on peptide-poly(ethylene glycol) conjugates are shown. The material-specific adsorption of a bioconjugate is temporarily suppressed by extending a titanium binding sequence with a proteolytically cleavabl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::614f069dbd1ac56e12af34878fef875d
https://pubmed.ncbi.nlm.nih.gov/35632375
https://pubmed.ncbi.nlm.nih.gov/35632375
Publikováno v:
ACS macro letters. 8(6)
Peptides with suitable substrate properties for a specific tyrosinase are selected by combinatorial means from a one-bead-one-compound (OBOC) peptide library. The identified sequences exhibit tyrosine residues that are rapidly oxidized to 3,4-dihydro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::099092d5ecbe9fd1d591937ffbf2bd32
https://pubmed.ncbi.nlm.nih.gov/35619530
https://pubmed.ncbi.nlm.nih.gov/35619530
Autor:
Hans G. Börner, Patrick Wilke
Publikováno v:
ACS macro letters. 1(7)
Enzyme-activated polymer coatings based on peptide–polymer conjugates are described. Tyrosinase is used to “switch on” adhesive functions of a mussel-glue derived peptide segment, leading to bioconjugates that adhere to steel. The coating resis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f73f713b55e8ec694eb87afb950fe6b3
https://pubmed.ncbi.nlm.nih.gov/35607135
https://pubmed.ncbi.nlm.nih.gov/35607135
Publikováno v:
Advanced Engineering Materials. 25:2201279
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b2941dc1f0ae12b2f9b3cee89035ae52
https://doi.org/10.1002/adem.202201279
https://doi.org/10.1002/adem.202201279
Publikováno v:
Angewandte Chemie. 131:10858-10863
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::843b2fbcf1e3954b96ed47957057e3fb
https://doi.org/10.1002/ange.201902217
https://doi.org/10.1002/ange.201902217