Guest organization by an amino acid-derived amide linkage in a cluster-based open framework

Ramanathan Vaidhyanathan; Craig A. Bridges; Darren Bradshaw; Matthew J. Rosseinsky

doi:10.1021/cg100336g

Guest organization by an amino acid-derived amide linkage in a cluster-based open framework

Ramanathan Vaidhyanathan
, Craig A. Bridges
, Darren Bradshaw
, Matthew J. Rosseinsky

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

9 Scopus citations

Abstract

Amino acid-functionalized Ni₄(OH)₃Cl tetrahedral clusters containing peptide linkages are linked into hexagonal planes connected pairwise into layers by neutral linkers. These layers stack to afford an open-framework structure, with large cavities occupied by non-ice-geometry (H₂O)₁₆ clusters. The layer stacking motif and the guest cluster geometry are both determined by an intricate hierarchy of hydrogen-bonding interactions defined by the array of peptides supported by the tetrahedral units. The (H₂O)₁₆ cluster adopts a non-ice-like structure due to the resulting highly symmetrical arrangement of the amide groups around the water molecules and the participation of two hydroxide anions per cluster.

Original language	English
Pages (from-to)	4348-4356
Number of pages	9
Journal	Crystal Growth and Design
Volume	10
Issue number	10
DOIs	https://doi.org/10.1021/cg100336g
State	Published - Oct 6 2010
Externally published	Yes

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10.1021/cg100336g

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title = "Guest organization by an amino acid-derived amide linkage in a cluster-based open framework",

abstract = "Amino acid-functionalized Ni4(OH)3Cl tetrahedral clusters containing peptide linkages are linked into hexagonal planes connected pairwise into layers by neutral linkers. These layers stack to afford an open-framework structure, with large cavities occupied by non-ice-geometry (H2O)16 clusters. The layer stacking motif and the guest cluster geometry are both determined by an intricate hierarchy of hydrogen-bonding interactions defined by the array of peptides supported by the tetrahedral units. The (H2O)16 cluster adopts a non-ice-like structure due to the resulting highly symmetrical arrangement of the amide groups around the water molecules and the participation of two hydroxide anions per cluster.",

author = "Ramanathan Vaidhyanathan and Bridges, \{Craig A.\} and Darren Bradshaw and Rosseinsky, \{Matthew J.\}",

year = "2010",

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doi = "10.1021/cg100336g",

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AU - Vaidhyanathan, Ramanathan

AU - Bridges, Craig A.

AU - Bradshaw, Darren

AU - Rosseinsky, Matthew J.

PY - 2010/10/6

Y1 - 2010/10/6

N2 - Amino acid-functionalized Ni4(OH)3Cl tetrahedral clusters containing peptide linkages are linked into hexagonal planes connected pairwise into layers by neutral linkers. These layers stack to afford an open-framework structure, with large cavities occupied by non-ice-geometry (H2O)16 clusters. The layer stacking motif and the guest cluster geometry are both determined by an intricate hierarchy of hydrogen-bonding interactions defined by the array of peptides supported by the tetrahedral units. The (H2O)16 cluster adopts a non-ice-like structure due to the resulting highly symmetrical arrangement of the amide groups around the water molecules and the participation of two hydroxide anions per cluster.

AB - Amino acid-functionalized Ni4(OH)3Cl tetrahedral clusters containing peptide linkages are linked into hexagonal planes connected pairwise into layers by neutral linkers. These layers stack to afford an open-framework structure, with large cavities occupied by non-ice-geometry (H2O)16 clusters. The layer stacking motif and the guest cluster geometry are both determined by an intricate hierarchy of hydrogen-bonding interactions defined by the array of peptides supported by the tetrahedral units. The (H2O)16 cluster adopts a non-ice-like structure due to the resulting highly symmetrical arrangement of the amide groups around the water molecules and the participation of two hydroxide anions per cluster.

UR - https://www.scopus.com/pages/publications/77957696019

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JO - Crystal Growth and Design

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IS - 10

ER -

Guest organization by an amino acid-derived amide linkage in a cluster-based open framework

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