Molecular mechanics of dihydroxyphenylalanine at a silica interface

Zhao Qin; Markus Buehler

doi:10.1063/1.4747214

Molecular mechanics of dihydroxyphenylalanine at a silica interface

Zhao Qin, Markus Buehler

Research output: Contribution to journal › Article › peer-review

28 Scopus citations

Abstract

L-3,4-dihydroxyphenylalanine (DOPA) is an amazing biological glue secreted by marine mussels. Through enhanced sampling molecular dynamics, here we demonstrate that proteins with DOPA residues have a strong affinity to a silica surface with an interfacial strength of several hundreds of thousand N/cm ². The mechanism of such strong adhesion is a pair of hydrogen bonds that forms between DOPA and the substrate, enabling enhanced cooperativity as the DOPA residue lays flat on top the surface. Our predicted adhesion force (743 pN) agrees well with experimental measurements (847 ± 157 pN), including the orientation of the DOPA residue on the surface.

Original language	English (US)
Article number	083702
Journal	Applied Physics Letters
Volume	101
Issue number	8
DOIs	https://doi.org/10.1063/1.4747214
State	Published - Aug 20 2012
Externally published	Yes

ASJC Scopus subject areas

Physics and Astronomy (miscellaneous)

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10.1063/1.4747214

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title = "Molecular mechanics of dihydroxyphenylalanine at a silica interface",

abstract = "L-3,4-dihydroxyphenylalanine (DOPA) is an amazing biological glue secreted by marine mussels. Through enhanced sampling molecular dynamics, here we demonstrate that proteins with DOPA residues have a strong affinity to a silica surface with an interfacial strength of several hundreds of thousand N/cm 2. The mechanism of such strong adhesion is a pair of hydrogen bonds that forms between DOPA and the substrate, enabling enhanced cooperativity as the DOPA residue lays flat on top the surface. Our predicted adhesion force (743 pN) agrees well with experimental measurements (847 ± 157 pN), including the orientation of the DOPA residue on the surface.",

author = "Zhao Qin and Markus Buehler",

note = "Funding Information: This work was supported by ONR (N000141010562 and N000140810844), AFOSR (FA9550-11-1-0199), and additional support from NSF (CMMI-0642545).",

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AU - Qin, Zhao

AU - Buehler, Markus

N1 - Funding Information: This work was supported by ONR (N000141010562 and N000140810844), AFOSR (FA9550-11-1-0199), and additional support from NSF (CMMI-0642545).

PY - 2012/8/20

Y1 - 2012/8/20

N2 - L-3,4-dihydroxyphenylalanine (DOPA) is an amazing biological glue secreted by marine mussels. Through enhanced sampling molecular dynamics, here we demonstrate that proteins with DOPA residues have a strong affinity to a silica surface with an interfacial strength of several hundreds of thousand N/cm 2. The mechanism of such strong adhesion is a pair of hydrogen bonds that forms between DOPA and the substrate, enabling enhanced cooperativity as the DOPA residue lays flat on top the surface. Our predicted adhesion force (743 pN) agrees well with experimental measurements (847 ± 157 pN), including the orientation of the DOPA residue on the surface.

AB - L-3,4-dihydroxyphenylalanine (DOPA) is an amazing biological glue secreted by marine mussels. Through enhanced sampling molecular dynamics, here we demonstrate that proteins with DOPA residues have a strong affinity to a silica surface with an interfacial strength of several hundreds of thousand N/cm 2. The mechanism of such strong adhesion is a pair of hydrogen bonds that forms between DOPA and the substrate, enabling enhanced cooperativity as the DOPA residue lays flat on top the surface. Our predicted adhesion force (743 pN) agrees well with experimental measurements (847 ± 157 pN), including the orientation of the DOPA residue on the surface.

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Molecular mechanics of dihydroxyphenylalanine at a silica interface

Abstract

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