Zinc-triggered hydrogelation of a self-assembling β-hairpin peptide.

Zinc-triggered hydrogelation of a self-assembling β-hairpin peptide.
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DOI:
10.1002/anie.201006652
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发表时间:
2011-02-11
期刊:
Angewandte Chemie (International ed. in English)
影响因子:
--
通讯作者:
Schneider JP
Schneider JP
中科院分区:
其他
文献类型:
--
作者:
Micklitsch CM;Knerr PJ;Branco MC;Nagarkar R;Pochan DJ;Schneider JP

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Environmentally responsive hydrogels formed by peptide self-assembly lead to materials with defined structure and utility for a wide range of biomedical applications.[1] The formation of structurally defined materials through the complexation of metal ions by peptides has been of particular interest. In nature, interactions of metals with histidine, methionine, cysteine, aspartic acid, and glutamic acid residues are utilized to induce conformational changes in proteins to drive diverse biological reactions and to form supramolecular structures.[2] Peptides have been developed to take advantage of these naturally occurring ligands to enhance structural stability and promote self-assembly on binding to a variety of metal cations.[3] Additionally, non-natural metal-ligating residues have been synthesized to serve as triggers for higher-order assembly.[4]Zinc is an essential cofactor in transcription factors and enzymes involved in cell replication, protein synthesis, and extracellular remodeling.[5, 6] In wound repair, zinc promotes matrix metalloproteinase debridement and keratinocyte migration at the site of damaged tissue.[6, 7] Topical administration of zinc results in the enhanced healing of both acute and chronic wounds.[8] In addition, zinc can inhibit the growth of several bacterial species, and thus can help to prevent infection in wound beds.[9] Therefore, the development of biomaterials incorporating zinc would be beneficial as wound dressings that help augment the healing process and lower the risk of infection.
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