The supramolecular chemistry of β-sheets.

The supramolecular chemistry of β-sheets.
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DOI:
10.1021/ja3088407
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发表时间:
2013-04-17
影响因子:
15
通讯作者:
Nowick, James S.
Nowick, James S.
中科院分区:
化学1区
文献类型:
--
作者:
Cheng, Pin-Nan;Pham, Johnny D.;Nowick, James S.

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Interactions among β-sheets occur widely in protein quaternary structure, protein-protein interaction, and protein aggregation and are central in Alzheimer’s and other amyloid-related diseases. This Perspective looks at the structural biology of these important yet under-appreciated interactions from a supramolecular chemist’s point of view. Common themes in the supramolecular interactions of β-sheets are identified and richly illustrated though examples from proteins, amyloids, and chemical model systems. β-Sheets interact through edge-to-edge hydrogen bonding to form extended layers and through face-to-face hydrophobic or van der Waals interactions to form layered sandwich-like structures. Side chains from adjacent layers can fit together through simple hydrophobic contacts or can participate in complementary interdigitation or knob-hole interactions. The layers can be aligned, offset, or rotated. The right-handed twist of β-sheets provides additional opportunities for stabilization of edge-to-edge contacts and rotated layered structures.
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