2011
DOI: 10.1002/anie.201100141
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Calcium Ions to Remotely Control the Reversible Switching of Secondary and Quaternary Structures in Bioconjugates

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Cited by 39 publications
(42 citation statements)
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“…Ponnumallayan and Fee incorporated the ELELELELELFG peptide (EL‐5FG) to obtain reversible self‐assembling hydrogels . Peptides with alternating hydrophilic/hydrophobic residues are known to promote β‐sheet structures and by using glutamic acid as charged residues, the peptide became pH responsive (pH ≈ 5) . The conjugate was obtained through the reaction of NHS‐PEG with peptide's free amine at the N ‐terminus.…”
Section: Self‐assembling Hydrogels Of Peptide–polymer Conjugatesmentioning
confidence: 99%
See 1 more Smart Citation
“…Ponnumallayan and Fee incorporated the ELELELELELFG peptide (EL‐5FG) to obtain reversible self‐assembling hydrogels . Peptides with alternating hydrophilic/hydrophobic residues are known to promote β‐sheet structures and by using glutamic acid as charged residues, the peptide became pH responsive (pH ≈ 5) . The conjugate was obtained through the reaction of NHS‐PEG with peptide's free amine at the N ‐terminus.…”
Section: Self‐assembling Hydrogels Of Peptide–polymer Conjugatesmentioning
confidence: 99%
“…Alternative peptide‐PNIPAAm conjugates were also described by Zhou et al. using the LLEELLEELEELLEEA (LE) peptide, inspired from the sequence reported by Kuhnle et al . LE forms α‐helix structures in the presence of calcium ions .…”
Section: Self‐assembling Hydrogels Of Peptide–polymer Conjugatesmentioning
confidence: 99%
“…Bioinspired peptide-polymer/ protein-polymer conjugates are widely used for a broad range of applications (25), including enzyme stabilization (26)(27)(28)(29) the self-organization of bioconjugates (30)(31)(32)(33), or in adhesive systems, where proteins have proved to serve as excellent interfaces between organic and inorganic materials (34)(35)(36).…”
Section: Bioinspired Design Of Bioconjugatesmentioning
confidence: 99%
“…However, it is challenging to control the self‐assembly behavior of proteins because of the complicated, heterogeneous protein surfaces, which can interact with each other in unpredictable ways (Bai et al, ; Zhou et al, ). In addition, some external factors may also affect the conformation transition of proteins (Zong et al, ), Response:, including pH value, temperature, or redox potential as well as enzymatic modification of peptides (Top et al, ; Williams et al, ; Kühnle et al, ). Moreover, many researches have pointed that some metal ions such as Al 3+ , Fe 3+ , Cu 2+ , and Zn 2+ (Pagel et al, ; Zaykov et al, ; Zhang et al, ), can trigger structural transformations, aggregation, and fibrillation of human α‐synuclein and amyloid‐β peptide.…”
Section: Introductionmentioning
confidence: 99%