BIOLOGICAL ADHESIVES. Adaptive synergy between catechol and lysine promotes wet adhesion by surface salt displacement
In physiological fluids and seawater, adhesion of synthetic polymers to solid surfaces is severely limited by high salt, pH, and hydration, yet these conditions have not deterred the evolution of effective adhesion by mussels. Mussel foot proteins provide insights about adhesive adaptations: Notably...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Waite, J Herbert [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015 |
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| Rechteinformationen: |
Nutzungsrecht: Copyright © 2015, American Association for the Advancement of Science. |
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| Schlagwörter: |
Dihydroxyphenylalanine - chemistry |
|---|
| Übergeordnetes Werk: |
Enthalten in: Science - Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883, 349(2015), 6248, Seite 628 |
|---|---|
| Übergeordnetes Werk: |
volume:349 ; year:2015 ; number:6248 ; pages:628 |
| Links: |
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| 520 | |a In physiological fluids and seawater, adhesion of synthetic polymers to solid surfaces is severely limited by high salt, pH, and hydration, yet these conditions have not deterred the evolution of effective adhesion by mussels. Mussel foot proteins provide insights about adhesive adaptations: Notably, the abundance and proximity of catecholic Dopa (3,4-dihydroxyphenylalanine) and lysine residues hint at a synergistic interplay in adhesion. Certain siderophores—bacterial iron chelators—consist of paired catechol and lysine functionalities, thereby providing a convenient experimental platform to explore molecular synergies in bioadhesion. These siderophores and synthetic analogs exhibit robust adhesion energies (E(ad) ≥-15 millijoules per square meter) to mica in saline pH 3.5 to 7.5 and resist oxidation. The adjacent catechol-lysine placement provides a "one-two punch," whereby lysine evicts hydrated cations from the mineral surface, allowing catechol binding to underlying oxides. | ||
| 540 | |a Nutzungsrecht: Copyright © 2015, American Association for the Advancement of Science. | ||
| 650 | 4 | |a Siderophores - chemistry | |
| 650 | 4 | |a Dihydroxyphenylalanine - chemistry | |
| 650 | 4 | |a Proteins - chemistry | |
| 650 | 4 | |a Aluminum Silicates - chemistry | |
| 650 | 4 | |a Titanium - chemistry | |
| 650 | 4 | |a Lysine - chemistry | |
| 650 | 4 | |a Adhesives - chemistry | |
| 650 | 4 | |a Catechols - chemistry | |
| 700 | 1 | |a Rapp, Michael V |4 oth | |
| 700 | 1 | |a Butler, Alison |4 oth | |
| 700 | 1 | |a Maier, Greg P |4 oth | |
| 700 | 1 | |a Israelachvili, Jacob N |4 oth | |
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PQ20160211 (DE-627)OLC1969537442 (DE-599)GBVOLC1969537442 (PRQ)p598-e20326f9539dd527c6bed5462cdc8fd5d6e350268a57926a03e46400131d94950 (KEY)0063888920150000349624800628biologicaladhesivesadaptivesynergybetweencatechola DE-627 ger DE-627 rakwb eng 500 DNB LING fid Waite, J Herbert verfasserin aut BIOLOGICAL ADHESIVES. Adaptive synergy between catechol and lysine promotes wet adhesion by surface salt displacement 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier In physiological fluids and seawater, adhesion of synthetic polymers to solid surfaces is severely limited by high salt, pH, and hydration, yet these conditions have not deterred the evolution of effective adhesion by mussels. Mussel foot proteins provide insights about adhesive adaptations: Notably, the abundance and proximity of catecholic Dopa (3,4-dihydroxyphenylalanine) and lysine residues hint at a synergistic interplay in adhesion. Certain siderophores—bacterial iron chelators—consist of paired catechol and lysine functionalities, thereby providing a convenient experimental platform to explore molecular synergies in bioadhesion. These siderophores and synthetic analogs exhibit robust adhesion energies (E(ad) ≥-15 millijoules per square meter) to mica in saline pH 3.5 to 7.5 and resist oxidation. The adjacent catechol-lysine placement provides a "one-two punch," whereby lysine evicts hydrated cations from the mineral surface, allowing catechol binding to underlying oxides. Nutzungsrecht: Copyright © 2015, American Association for the Advancement of Science. Siderophores - chemistry Dihydroxyphenylalanine - chemistry Proteins - chemistry Aluminum Silicates - chemistry Titanium - chemistry Lysine - chemistry Adhesives - chemistry Catechols - chemistry Rapp, Michael V oth Butler, Alison oth Maier, Greg P oth Israelachvili, Jacob N oth Enthalten in Science Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883 349(2015), 6248, Seite 628 (DE-627)12931482X (DE-600)128410-1 (DE-576)014533189 0036-8075 nnns volume:349 year:2015 number:6248 pages:628 http://www.ncbi.nlm.nih.gov/pubmed/26250681 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-IBL SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_30 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_92 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_131 GBV_ILN_170 GBV_ILN_171 GBV_ILN_179 GBV_ILN_181 GBV_ILN_211 GBV_ILN_252 GBV_ILN_259 GBV_ILN_290 GBV_ILN_600 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2012 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2173 GBV_ILN_2185 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4320 GBV_ILN_4324 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4700 AR 349 2015 6248 628 |
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PQ20160211 (DE-627)OLC1969537442 (DE-599)GBVOLC1969537442 (PRQ)p598-e20326f9539dd527c6bed5462cdc8fd5d6e350268a57926a03e46400131d94950 (KEY)0063888920150000349624800628biologicaladhesivesadaptivesynergybetweencatechola DE-627 ger DE-627 rakwb eng 500 DNB LING fid Waite, J Herbert verfasserin aut BIOLOGICAL ADHESIVES. Adaptive synergy between catechol and lysine promotes wet adhesion by surface salt displacement 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier In physiological fluids and seawater, adhesion of synthetic polymers to solid surfaces is severely limited by high salt, pH, and hydration, yet these conditions have not deterred the evolution of effective adhesion by mussels. Mussel foot proteins provide insights about adhesive adaptations: Notably, the abundance and proximity of catecholic Dopa (3,4-dihydroxyphenylalanine) and lysine residues hint at a synergistic interplay in adhesion. Certain siderophores—bacterial iron chelators—consist of paired catechol and lysine functionalities, thereby providing a convenient experimental platform to explore molecular synergies in bioadhesion. These siderophores and synthetic analogs exhibit robust adhesion energies (E(ad) ≥-15 millijoules per square meter) to mica in saline pH 3.5 to 7.5 and resist oxidation. The adjacent catechol-lysine placement provides a "one-two punch," whereby lysine evicts hydrated cations from the mineral surface, allowing catechol binding to underlying oxides. Nutzungsrecht: Copyright © 2015, American Association for the Advancement of Science. Siderophores - chemistry Dihydroxyphenylalanine - chemistry Proteins - chemistry Aluminum Silicates - chemistry Titanium - chemistry Lysine - chemistry Adhesives - chemistry Catechols - chemistry Rapp, Michael V oth Butler, Alison oth Maier, Greg P oth Israelachvili, Jacob N oth Enthalten in Science Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883 349(2015), 6248, Seite 628 (DE-627)12931482X (DE-600)128410-1 (DE-576)014533189 0036-8075 nnns volume:349 year:2015 number:6248 pages:628 http://www.ncbi.nlm.nih.gov/pubmed/26250681 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-IBL SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_30 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_92 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_131 GBV_ILN_170 GBV_ILN_171 GBV_ILN_179 GBV_ILN_181 GBV_ILN_211 GBV_ILN_252 GBV_ILN_259 GBV_ILN_290 GBV_ILN_600 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2012 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2173 GBV_ILN_2185 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4320 GBV_ILN_4324 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4700 AR 349 2015 6248 628 |
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Enthalten in Science 349(2015), 6248, Seite 628 volume:349 year:2015 number:6248 pages:628 |
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Siderophores - chemistry Dihydroxyphenylalanine - chemistry Proteins - chemistry Aluminum Silicates - chemistry Titanium - chemistry Lysine - chemistry Adhesives - chemistry Catechols - chemistry |
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Waite, J Herbert @@aut@@ Rapp, Michael V @@oth@@ Butler, Alison @@oth@@ Maier, Greg P @@oth@@ Israelachvili, Jacob N @@oth@@ |
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Waite, J Herbert ddc 500 fid LING misc Siderophores - chemistry misc Dihydroxyphenylalanine - chemistry misc Proteins - chemistry misc Aluminum Silicates - chemistry misc Titanium - chemistry misc Lysine - chemistry misc Adhesives - chemistry misc Catechols - chemistry BIOLOGICAL ADHESIVES. Adaptive synergy between catechol and lysine promotes wet adhesion by surface salt displacement |
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500 DNB LING fid BIOLOGICAL ADHESIVES. Adaptive synergy between catechol and lysine promotes wet adhesion by surface salt displacement Siderophores - chemistry Dihydroxyphenylalanine - chemistry Proteins - chemistry Aluminum Silicates - chemistry Titanium - chemistry Lysine - chemistry Adhesives - chemistry Catechols - chemistry |
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ddc 500 fid LING misc Siderophores - chemistry misc Dihydroxyphenylalanine - chemistry misc Proteins - chemistry misc Aluminum Silicates - chemistry misc Titanium - chemistry misc Lysine - chemistry misc Adhesives - chemistry misc Catechols - chemistry |
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biological adhesives. adaptive synergy between catechol and lysine promotes wet adhesion by surface salt displacement |
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BIOLOGICAL ADHESIVES. Adaptive synergy between catechol and lysine promotes wet adhesion by surface salt displacement |
| abstract |
In physiological fluids and seawater, adhesion of synthetic polymers to solid surfaces is severely limited by high salt, pH, and hydration, yet these conditions have not deterred the evolution of effective adhesion by mussels. Mussel foot proteins provide insights about adhesive adaptations: Notably, the abundance and proximity of catecholic Dopa (3,4-dihydroxyphenylalanine) and lysine residues hint at a synergistic interplay in adhesion. Certain siderophores—bacterial iron chelators—consist of paired catechol and lysine functionalities, thereby providing a convenient experimental platform to explore molecular synergies in bioadhesion. These siderophores and synthetic analogs exhibit robust adhesion energies (E(ad) ≥-15 millijoules per square meter) to mica in saline pH 3.5 to 7.5 and resist oxidation. The adjacent catechol-lysine placement provides a "one-two punch," whereby lysine evicts hydrated cations from the mineral surface, allowing catechol binding to underlying oxides. |
| abstractGer |
In physiological fluids and seawater, adhesion of synthetic polymers to solid surfaces is severely limited by high salt, pH, and hydration, yet these conditions have not deterred the evolution of effective adhesion by mussels. Mussel foot proteins provide insights about adhesive adaptations: Notably, the abundance and proximity of catecholic Dopa (3,4-dihydroxyphenylalanine) and lysine residues hint at a synergistic interplay in adhesion. Certain siderophores—bacterial iron chelators—consist of paired catechol and lysine functionalities, thereby providing a convenient experimental platform to explore molecular synergies in bioadhesion. These siderophores and synthetic analogs exhibit robust adhesion energies (E(ad) ≥-15 millijoules per square meter) to mica in saline pH 3.5 to 7.5 and resist oxidation. The adjacent catechol-lysine placement provides a "one-two punch," whereby lysine evicts hydrated cations from the mineral surface, allowing catechol binding to underlying oxides. |
| abstract_unstemmed |
In physiological fluids and seawater, adhesion of synthetic polymers to solid surfaces is severely limited by high salt, pH, and hydration, yet these conditions have not deterred the evolution of effective adhesion by mussels. Mussel foot proteins provide insights about adhesive adaptations: Notably, the abundance and proximity of catecholic Dopa (3,4-dihydroxyphenylalanine) and lysine residues hint at a synergistic interplay in adhesion. Certain siderophores—bacterial iron chelators—consist of paired catechol and lysine functionalities, thereby providing a convenient experimental platform to explore molecular synergies in bioadhesion. These siderophores and synthetic analogs exhibit robust adhesion energies (E(ad) ≥-15 millijoules per square meter) to mica in saline pH 3.5 to 7.5 and resist oxidation. The adjacent catechol-lysine placement provides a "one-two punch," whereby lysine evicts hydrated cations from the mineral surface, allowing catechol binding to underlying oxides. |
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BIOLOGICAL ADHESIVES. Adaptive synergy between catechol and lysine promotes wet adhesion by surface salt displacement |
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